Anthocyanins Genetics and Genomics

Carrot Anthocyanins Genetics and Genomics: Standing and Views to Enhance Its Software for the Meals Colorant Trade

Purple or black carrots (Daucus carota ssp. sativus var. atrorubens Alef) are characterised by their darkish purple- to black-colored roots, owing their look to excessive anthocyanin concentrations.
In recent times, there was rising curiosity in using black carrot anthocyanins as pure meals dyes. Black carrot roots include giant portions of mono-acylated anthocyanins, which impart a measure of heat-, light- and pH-stability, enhancing the color-stability of meals merchandise over their shelf-life.
The genetic pathway controlling anthocyanin biosynthesis seems properly conserved amongst land vegetation; nevertheless, totally different variants of anthocyanin-related genes between cultivars leads to tissue-specific accumulations of purple pigments.
Thus, broad genetic variations of anthocyanin profile, and tissue-specific distributions in carrot tissues and organs, could be noticed, and the ratio of acylated to non-acylated anthocyanins varies considerably within the purple carrot germplasm.
Moreover, anthocyanins synthesis can be influenced by a variety of exterior elements, equivalent to abiotic stressors and/or chemical elicitors, straight affecting the anthocyanin yield and stability potential in meals and beverage functions.
On this examine, we critically evaluation and talk about the present information on anthocyanin range, genetics and the molecular mechanisms controlling anthocyanin accumulation in carrots. We additionally present a view of the present information gaps and development wants as regards growing and making use ofrevolutionary molecular instruments to enhance the yield, product efficiency and stability of carrot anthocyanin to be used as a pure meals colorant.
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human anti-human IL-8 mAb(N8)

E4A09D07-N8 50ug
EUR 275
Description: Biotin-Conjugated, FITC-Conjugated , AF350 Conjugated , AF405M-Conjugated ,AF488-Conjugated, AF514-Conjugated ,AF532-Conjugated, AF555-Conjugated ,AF568-Conjugated , HRP-Conjugated, AF405S-Conjugated, AF405L-Conjugated , AF546-Conjugated, AF594-Conjugated , AF610-Conjugated, AF635-Conjugated , AF647-Conjugated , AF680-Conjugated , AF700-Conjugated , AF750-Conjugated , AF790-Conjugated , APC-Conjugated , PE-Conjugated , Cy3-Conjugated , Cy5-Conjugated , Cy5.5-Conjugated , Cy7-Conjugated Antibody

Anti-Human IL-8 Antibody

101-M08 500 µg
EUR 246.75
Description: Il-8 or CXCL8 was originally discovered and purified as a neutrophil chemotactic and activating factor. It was also referred to as neutrophil chemotactic factor (NCF), neutrophil activating protein (NAP), monocytederived neutrophil chemotactic factor (MDNCF), T lymphocyte chemotactic factor (TCF), granulocyte chemotactic protein (GCP) and leukocyte adhesion inhibitor (LAI). Many cell types, including monocyte/macrophages, T cells, neutrophils, fibroblasts, endothelial cells, keratinocytes, hepatocytes, chondrocytes, and various tumor cell lines, can produce CXCL8 in response to a wide variety of proinflammatory stimuli such as exposure to IL-1, TNF, LPS, and viruses. CXCL8 is a member of the alpha (CXC) subfamily of chemokines, which also includes platelet factor-4, GRO, and IP10.

Anti-Human IL-8 Antibody

102-P38 100 µg
EUR 245.7
Description: Il-8 or CXCL8 was originally discovered and purified as a neutrophil chemotactic and activating factor. It was also referred to as neutrophil chemotactic factor (NCF), neutrophil activating protein (NAP), monocytederived neutrophil chemotactic factor (MDNCF), T lymphocyte chemotactic factor (TCF), granulocyte chemotactic protein (GCP) and leukocyte adhesion inhibitor (LAI). Many cell types, including monocyte/macrophages, T cells, neutrophils, fibroblasts, endothelial cells, keratinocytes, hepatocytes, chondrocytes, and various tumor cell lines, can produce CXCL8 in response to a wide variety of proinflammatory stimuli such as exposure to IL-1, TNF, LPS, and viruses. CXCL8 is a member of the alpha (CXC) subfamily of chemokines, which also includes platelet factor-4, GRO, and IP10.

Anti-Human IL-8 Antibody

GWB-817E77 1 mL Ask for price

Human Interleukin-8 (IL-8) Antibody

13102-05011 150 ug
EUR 175

Human IL-8

90258-A 5 µg
EUR 130
Description: Recombinant human Interleukin-8 is a disulfide-linked monomer protein consisting of 78 amino acid residues, migrates as an approximately 9 kDa protein under non-reducing and reducing conditions in SDS-PAGE. Optimized DNA sequence encoding Human Interleukin-8 mature chain was expressed in E. coli.

Human IL-8

90258-B 25 µg
EUR 205
Description: Recombinant human Interleukin-8 is a disulfide-linked monomer protein consisting of 78 amino acid residues, migrates as an approximately 9 kDa protein under non-reducing and reducing conditions in SDS-PAGE. Optimized DNA sequence encoding Human Interleukin-8 mature chain was expressed in E. coli.

human IL-8

M851530020 1 unit
EUR 804.84

Anti-CXCL8 / IL-8 Reference Antibody (Genentech anti-IL-8)

E24CHA784 100 μg
EUR 225
Description: Available in various conjugation types.

human-anti-human-IL-8-mAb(1H)

E409C16-hA100 Inflammation-Storm-Antibodies
EUR 276.5
Description: Inflammation Storm Antibodies

human-anti-human-IL-8-mAb(2H)

E409C16-hB100 Inflammation-Storm-Antibodies
EUR 276.5
Description: Inflammation Storm Antibodies

Anti-IL-8 Antibody

A00423 1 mL
EUR 1444.8
Description: Rabbit Polyclonal IL-8 Antibody. Validated in IP, WB and tested in Human.

Anti-IL-8 Antibody

A2062-100 100 µg
EUR 472.8

Anti-IL-8 Antibody

ER1706-67 100ul
EUR 189
Description: Interleukin 8 (IL-8 or chemokine (C-X-C motif) ligand 8, CXCL8) is a chemokine produced by macrophages and other cell types such as epithelial cells, airway smooth muscle cells and endothelial cells. IL-8, also known as neutrophil chemotactic factor, has two primary functions. It induces chemotaxis in target cells, primarily neutrophils but also other granulocytes, causing them to migrate toward the site of infection. IL-8 also stimulates phagocytosis once they have arrived. IL-8 is also known to be a potent promoter of angiogenesis. In target cells, IL-8 induces a series of physiological responses required for migration and phagocytosis, such as increases in intracellular Ca2+, exocytosis (e.g. histamine release), and the respiratory burst. IL-8 can be secreted by any cells with toll-like receptors that are involved in the innate immune response and has been demonstrated to be a signatory chemokine of CR2+ naive T cells, also known as recent thymic emigrants. Usually, it is the macrophages that see an antigen first, and thus are the first cells to release IL-8 to recruit other cells. Both monomer and homodimer forms of IL-8 have been reported to be potent inducers of the chemokine receptors CXCR1 and CXCR2. The homodimer is more potent, but methylation of Leu25 can block the activity of homodimers.

Anti-IL-8 Antibody

ER1901-61 100ul
EUR 189
Description: IL-8, also known as neutrophil chemotactic factor, has two primary functions. It induces chemotaxis in target cells, primarily neutrophils but also other granulocytes, causing them to migrate toward the site of infection. IL-8 also stimulates phagocytosis once they have arrived. IL-8 is also known to be a potent promoter of angiogenesis. In target cells, IL-8 induces a series of physiological responses required for migration and phagocytosis, such as increases in intracellular Ca2+, exocytosis (e.g. histamine release), and the respiratory burst.IL-8 can be secreted by any cells with toll-like receptors that are involved in the innate immune response. Usually, it is the macrophages that see an antigen first, and thus are the first cells to release IL-8 to recruit other cells. Both monomer and homodimer forms of IL-8 have been reported to be potent inducers of the chemokine receptors CXCR1 and CXCR2. The homodimer is more potent, but methylation of Leu25 can block the activity of homodimers.

Anti-IL-8 Antibody

R1511-15 100ul
EUR 189

Anti-IL-8 Antibody

Y123169 100 µl
EUR 320

Anti-IL-8 antibody

STJ98175 100 µl
EUR 280.8
Description: Mouse monoclonal to IL-8.

Anti-IL-8 antibody

STJ97710 200 µl
EUR 236.4
Description: Mouse monoclonal to IL-8.

Anti-IL-8 antibody

STJ97717 200 µl
EUR 236.4
Description: Mouse monoclonal to IL-8.

Anti-IL-8 antibody

STJ97720 200 µl
EUR 236.4
Description: Mouse monoclonal to IL-8.

anti-IL-8 (3E4D8)

LF-MA30011 100 ul
EUR 448.8
Description: Mouse Monoclonal to IL-8

Anti- Interleukin-8 (IL-8) Antibody

GWB-7ACF57 0.05 mg Ask for price

mAb mouse anti-human IL-8

CT264 0.5 mg
EUR 312

mouse anti-human IL-8 mAb

E409C16-m100 100μL
EUR 395
Description: Available in various conjugation types.

Recombinant Human IL-8 (72a.a.)(rHu IL-8/CXCL8)

701081 25ul
EUR 235
Description: Fully biologically active when compared to standard. The ED50 as determined by a chemotaxis bioassay using human CXCR2 transfected mouse BaF3 cells is less than 2 ng/ml, corresponding to a specific activity of > 5.0 × 105 IU/mg.

Recombinant Human IL-8 (77a.a.)(rHu IL-8/CXCL8)

701082 25ul
EUR 235
Description: Fully biologically active when compared to standard. The ED50 as determined by a chemotaxis bioassay using human CXCR2 transfected mouse BaF3 cells is less than 2 ng/ml, corresponding to a specific activity of > 5.0 × 105 IU/mg.

IL-8/CXCL8, Human

HY-P7224 50ug
EUR 596.4

Human IL-8 Protein

abx060803-25ug 25 ug
EUR 644.4

Human IL-8 Protein

abx060804-25ug 25 ug
EUR 644.4

Human IL-8 protein

PRP1022-100ug 100 μg
EUR 449
Description: Human IL-8 protein, expressed in E. coli

Human IL-8 protein

PRP1022-10ug 10 μg
EUR 59
Description: Human IL-8 protein, expressed in E. coli

Human IL-8 protein

PRP1022-1mg 1 mg
EUR 2609
Description: Human IL-8 protein, expressed in E. coli

Human IL-8 protein

PRP1022-50ug 50 μg
EUR 249
Description: Human IL-8 protein, expressed in E. coli

Human IL-8 Protein

E2RB20061PT 100ul
EUR 485
Description: Biotin-Conjugated, FITC-Conjugated , AF350 Conjugated , AF405M-Conjugated ,AF488-Conjugated, AF514-Conjugated ,AF532-Conjugated, AF555-Conjugated ,AF568-Conjugated , HRP-Conjugated, AF405S-Conjugated, AF405L-Conjugated , AF546-Conjugated, AF594-Conjugated , AF610-Conjugated, AF635-Conjugated , AF647-Conjugated , AF680-Conjugated , AF700-Conjugated , AF750-Conjugated , AF790-Conjugated , APC-Conjugated , PE-Conjugated , Cy3-Conjugated , Cy5-Conjugated , Cy5.5-Conjugated , Cy7-Conjugated Antibody

Interleukin-8 (IL-8) (72a.a) Human

GWB-3997EC 0.025 mg Ask for price

Recombinant Human IL-8

6487 5 µg
EUR 194

Recombinant Human IL-8

P0180 100ug
EUR 626.83
Description: Recombinant Human protein for IL-8

Recombinant Human IL-8

SJB05-01 25µg/vial
EUR 342

Human Interleukin-8 (IL-8) Antibody (Biotin Conjugate)

13102-05021 150 ug
EUR 229

Rabbit anti-IL-8 Antibody

DL90596A-100ul 100 ul
EUR 270
Description: CXCL8; Interleukin-8; IL-8; C-X-C motif chemokine 8; Emoctakin; Granulocyte chemotactic protein 1; GCP-1; Monocyte-derived neutrophil chemotactic factor; MDNCF; Monocyte-derived neutrophil-activating peptide; MONAP; Neutrophil-activating protein 1; NAP-1; Protein 3-10C; T-cell chemotactic factor

Rabbit anti-IL-8 Antibody

DL90596A-50ul 50 ul
EUR 189
Description: CXCL8; Interleukin-8; IL-8; C-X-C motif chemokine 8; Emoctakin; Granulocyte chemotactic protein 1; GCP-1; Monocyte-derived neutrophil chemotactic factor; MDNCF; Monocyte-derived neutrophil-activating peptide; MONAP; Neutrophil-activating protein 1; NAP-1; Protein 3-10C; T-cell chemotactic factor

Rabbit anti-IL-8 Antibody

YLD4345-100ul 100 ul
EUR 320
Description: Rabbit polyclonal antibody to IL-8

Rabbit anti-IL-8 Antibody

YLD4345-50ul 50 ul
EUR 200
Description: Rabbit polyclonal antibody to IL-8

Anti-IL-8 Monoclonal Antibody

A00423-1 100ul
EUR 476.4
Description: Mouse Monoclonal Antibody for IL-8 Antibody (CXCL8) detection. Tested with IHC in Human, Mouse, Rat.

human DIAplex Human Inflammation - IL-8, IL-17a,

M880130004 1 unit
EUR 650.27

Human IL-8 ELISA antibody pair

CT748-10 10-plate
EUR 656.4

Human IL-8 ELISA antibody pair

CT748-20 20-plate
EUR 1118.4

Anti-swine IL-8 PAb

GWB-OC22N2 1 kit Ask for price

Anti-bovine IL-8 PAb

GWB-03EYX4 100 ug Ask for price

Anti-rabbit IL-8 PAb

GWB-VPE0Z2 1 kit Ask for price

Anti-feline IL-8 PAb

GWB-FEZA83 1 kit Ask for price

Anti-dolphin IL-8 PAb

GWB-KI0031 1 kit Ask for price

Anti-Human IL-8 (I8-S2) Antibody

Y052802 100 µg
EUR 490

Anti-Human IL-17 (CTLA-8) Antibody

101-M783 100 µg
EUR 399
Description: The IL-17 family is comprised of at least six proinflammatory cytokines that share a conserved cysteine-knot structure but diverge at the N-terminus. IL-17 family members are glycoproteins secreted as dimers that induce local cytokine production and recruit granulocytes to sites of inflammation. IL-17 is induced by IL-15 and IL-23, mainly in activated CD4+ T cells distinct from Th1 or Th2 cells. IL-17F is the most homologous to IL-17, but is induced only by IL-23 in activated monocytes. IL-17B binds the IL-17B receptor, but not the IL-17 receptor; it is most homologous with IL-17D, which is expressed by resting CD4+ T cells and CD19+ B cells. IL-17E is mainly produced by Th2 cells and recruits eosinophils to lung tissue. IL-17C has a very restricted expression pattern but has been detected in adult prostate and fetal kidney libraries.

Mouse Monoclonal anti-Human IL-8 Antibody

xAP-0435 100ug
EUR 280

Mouse Monoclonal anti-Human IL-8 Antibody

xAP-0436 100ug
EUR 280

Mouse Monoclonal anti-Human IL-8 Antibody

xAP-0437 100ug
EUR 280

Anti-Human IL-8 Rabbit Polyclonal Antibody

TA328221 100 µg Ask for price

Human Interleukin 8 (IL-8) CLIA Kit

abx195916-96tests 96 tests
EUR 990

Human IL-8 -Interleukin 8- CLIA Kit

E-CL-H0048-24Tests 24 Tests
EUR 180
Description: Sandwich

Human IL-8 -Interleukin 8- CLIA Kit

E-CL-H0048-48Tests 48 Tests
EUR 546
Description: Sandwich

Human IL-8 -Interleukin 8- CLIA Kit

E-CL-H0048-96Tests 96 Tests
EUR 682
Description: Sandwich

Human IL-8 -Interleukin 8- CLIA Kit

E-CL-H0048-96Tests10 96 Tests *10
EUR 6820
Description: Sandwich

Human IL-8 -Interleukin 8- CLIA Kit

E-CL-H0048-96Tests5 96 Tests *5
EUR 3410
Description: Sandwich

mouse anti-human IL-8 mAb(Q10)

E4A09D07-Q10 50ug
EUR 275
Description: Biotin-Conjugated, FITC-Conjugated , AF350 Conjugated , AF405M-Conjugated ,AF488-Conjugated, AF514-Conjugated ,AF532-Conjugated, AF555-Conjugated ,AF568-Conjugated , HRP-Conjugated, AF405S-Conjugated, AF405L-Conjugated , AF546-Conjugated, AF594-Conjugated , AF610-Conjugated, AF635-Conjugated , AF647-Conjugated , AF680-Conjugated , AF700-Conjugated , AF750-Conjugated , AF790-Conjugated , APC-Conjugated , PE-Conjugated , Cy3-Conjugated , Cy5-Conjugated , Cy5.5-Conjugated , Cy7-Conjugated Antibody

mouse anti-human IL-8 mAb(Q36)

E4A09D07-Q36 50ug
EUR 275
Description: Biotin-Conjugated, FITC-Conjugated , AF350 Conjugated , AF405M-Conjugated ,AF488-Conjugated, AF514-Conjugated ,AF532-Conjugated, AF555-Conjugated ,AF568-Conjugated , HRP-Conjugated, AF405S-Conjugated, AF405L-Conjugated , AF546-Conjugated, AF594-Conjugated , AF610-Conjugated, AF635-Conjugated , AF647-Conjugated , AF680-Conjugated , AF700-Conjugated , AF750-Conjugated , AF790-Conjugated , APC-Conjugated , PE-Conjugated , Cy3-Conjugated , Cy5-Conjugated , Cy5.5-Conjugated , Cy7-Conjugated Antibody

Rabbit anti-Human IL-8 mAb (CAP)

RM17646 100μg Ask for price

Rabbit anti-Human IL-8 mAb (DET)

RM17647 100μg Ask for price

Rabbit anti-Human IL-8 mAb (CAP)

RM17648 100μg Ask for price

Rabbit anti-Human IL-8 mAb (DET)

RM17649 100μg Ask for price

Human Interleukin 8,IL-8 ELISA KIT

201-12-0090 96 tests
EUR 528
Description: A quantitative ELISA kit for measuring Human in samples from biological fluids.

Human IL-8(Interleukin 8) ELISA Kit

EH0205 96T
EUR 571.5
Description: Method of detection: Double Antibody, Sandwich ELISA;Reacts with: Homo sapiens;Sensitivity: 18.75pg/ml

Human IL-8(Interleukin 8) ELISA Kit

EKF57074-48T 48T
EUR 396.9

Human IL-8(Interleukin 8) ELISA Kit

EKF57074-5x96T 5x96T
EUR 2693.25

Human IL-8(Interleukin 8) ELISA Kit

EKF57074-96T 96T
EUR 567

Human IL-8 (Interleukin 8) ELISA Kit

EKE60046-5x96T 5x96T
EUR 2667.6

Human IL-8 (Interleukin 8) ELISA Kit

EKE60046-96T 96T
EUR 561.6

Human Interleukin 8,IL-8 ELISA KIT

EKC40086-48T 48T
EUR 328.86

Human Interleukin 8,IL-8 ELISA KIT

EKC40086-5x96T 5x96T
EUR 2231.55

Human Interleukin 8,IL-8 ELISA KIT

EKC40086-96T 96T
EUR 469.8

Human Interleukin 8(IL-8) Elisa Kit

EK710269 96 Wells
EUR 0.77

Human IL-8(Interleukin 8) ELISA Kit

E39EH0205 96T
EUR 595

Human Interleukin 8(IL-8) Elisa Kit

EK610269 96 Wells
EUR 0.1

Characterization of Anti-Inflammatory and Antioxidant Constituents from Scutellaria baicalensis Utilizing LC-MS Coupled with a Bioassay Technique

An efficient and beforehand demonstrated screening technique for energetic constituents in pure <em>merchandise</em> utilizing LC-MS coupled with a bioassay was reported in our earlier research.
With this, the present investigation tried to determine bioactive constituents of <i>Scutellaria baicalensis</i> via LC-MS coupled with a bioassay.
Peaks at broadly 17-20 and 24-25 min on the MS chromatogram displayed an inhibitory impact on NO manufacturing in lipopolysaccharide-induced BV2 microglia cells.
Equally, peaks at roughly 17-19 and 22 min confirmed antioxidant exercise with an 2,2′-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) (ABTS)/2,2-diphenyl-1- picrylhydrazyl (DPPH) assay.
For affirmation of LC-MS coupled with a bioassay, 9 compounds (<b>1</b>-<b>9</b>) have been remoted from an MeOH extract of <i>S. baicalensis</i>. As we predicted, compounds <b>1</b>, <b>8</b>, and <b>9</b> considerably lowered lipopolysaccharide (LPS)-induced NO manufacturing in BV2 cells.
Likewise, compounds <b>5</b>, <b>6</b>, and <b>8</b> exhibited free radical-scavenging actions with the ABTS/DPPH assay. As well as, the structural similarity of the principle elements was confirmed by analyzing the whole extract and EtOAc fractions via <em>molecular</em> networking.
Total, the outcomes recommend that the strategy comprised of LC-MS coupled with a bioassay can successfully predict energetic compounds with out an isolation course of, and the outcomes of <em>molecular</em> networking predicted that different elements across the energetic compound node can also be energetic.

Polymer-Derived Heteroatom-Doped Porous Carbon Supplies

Heteroatom-doped porous carbon supplies (HPCMs) have discovered in depth functions in adsorption/separation, natural catalysis, sensing, and power conversion/storage.
The even handed alternative of carbon precursors is essential for the manufacture of HPCMs with particular usages and maximization of their capabilities. On this regard, polymers as precursors have demonstrated nice promise due to their versatile molecular and nanoscale constructions, modulatable chemical composition, and wealthy processing strategies to generate textures that, together with correct solid-state chemistry, could be maintained all through carbonization.
This Overview comprehensively surveys the progress in polymer-derived practical HPCMs by way of the right way to produce and management their porosities, heteroatom doping results, and morphologies and their associated use.
First, we summarize and talk about artificial approaches, together with laborious and delicate templating strategies in addition to direct synthesis methods using polymers to manage the pores and/or heteroatoms in HPCMs. Second, we summarize the heteroatom doping results on the thermal stability, digital and optical properties, and floor chemistry of HPCMs.
Particularly, the heteroatom doping impact, which includes each single-type heteroatom doping and codoping of two or extra kinds of heteroatoms into the carbon community, is mentioned.
Contemplating the significance of the morphologies of HPCMs of their utility spectrum, potential decisions of appropriate polymeric precursors and methods to exactly regulate the morphologies of HPCMs are offered.
Lastly, we present our perspective on the right way to predefine the constructions of HPCMs through the use of polymers to comprehend their potential functions within the present fields of power era/conversion and environmental remediation.
We imagine that these analyses and deductions are helpful for a systematic understanding of polymer-derived carbon supplies and can function a supply of inspiration for the design of future HPCMs.

Anti-Human VEGFR-1/Flt-1 Antibody

102-PA20 200 µg
EUR 173.25
Description: Endothelial cells express three different vascular endothelial growth factor (VEGF) receptors, belonging to the family of receptor tyrosine kinases (RTKs). They are named VEGFR-1 (Flt-1), VEGFR-2 (KDR/Flk-1), VEGFR-3 (Flt-4). Their expression is almost exclusively restricted to endothelial cells, but VEGFR-1 can also be found on monocytes, dendritic cells and on trophoblast cells. The flt-1 gene was first described in 1990. The receptor contains seven immunoglobulin-like extracellular domains, a single transmembrane region and an intracellular splited tyrosine kinase domain. Compared to VEGFR-2 the Flt-1 receptor has a higher affinity for VEGF but a weaker signaling activity. VEGFR-1 thus leads not to proliferation of endothelial cells, but mediates signals for differentiation. Interestingly a naturally occuring soluble variant of VEGFR-1 (sVEGFR-1) was found in HUVEC supernatants in 1996, which is generated by alternative splicing of the flt-1 mRNA.

Anti-Human VEGFR-1/Flt-1 Antibody

102-PABi20 50 µg
EUR 157.5
Description: Endothelial cells express three different vascular endothelial growth factor (VEGF) receptors, belonging to the family of receptor tyrosine kinases (RTKs). They are named VEGFR-1 (Flt-1), VEGFR-2 (KDR/Flk-1), VEGFR-3 (Flt-4). Their expression is almost exclusively restricted to endothelial cells, but VEGFR-1 can also be found on monocytes, dendritic cells and on trophoblast cells. The flt-1 gene was first described in 1990. The receptor contains seven immunoglobulin-like extracellular domains, a single transmembrane region and an intracellular splited tyrosine kinase domain. Compared to VEGFR-2 the Flt-1 receptor has a higher affinity for VEGF but a weaker signaling activity. VEGFR-1 thus leads not to proliferation of endothelial cells, but mediates signals for differentiation. Interestingly a naturally occuring soluble variant of VEGFR-1 (sVEGFR-1) was found in HUVEC supernatants in 1996, which is generated by alternative splicing of the flt-1 mRNA.

Mouse anti VEGFR-3/Flt-4 (#1) (human)

101-M36 100ug
EUR 297.6

Mouse anti VEGFR-1/Flt-1-Biotin (#EWF) (human)

101-MBi28 50ug
EUR 297.6

VEGFR-1 / FLT-1 Antibody

abx239393-100ug 100 ug
EUR 577.2

VEGFR-1/FLT-1 antibody

E39-09393 100ug/100ul
EUR 225
Description: Available in various conjugation types.

VEGFR-1/FLT-1 antibody

CAF50629-100ug 100ug
EUR 312

Anti-Mouse VEGFR-1/Flt-1 Antibody

103-M31 100 µg
EUR 399
Description: Vascular Endothelial Growth Factor (VEGF or VEGF-A) family members are major mediators of vasculogenesis and angiogenesis. Specifically, biological activities attributed to VEGFs include: mitogenic activity on endothelial cells, increased permeability of endothelial cells to proteins, stimulation of monocyte migration across endothelial cells and angiogenic activity. Three VEGF family receptors have been described: Flt-1 (fms-like tyrosine kinase) also known as VEGF R1, KDR (kinase-insert domain-containing receptor) also known as Flk-1 and VEGF R2, and Flt-4 also known as VEGF R3. The three receptors contain seven extracellular immunoglobulin-like domains and share substantial sequence homology. In addition, neuropilin-1, a neuronal receptor, also acts as a co-receptor for VEGF when expressed on vascular endothelial cells, endothelial cell progenitors and monocytes. VEGF R1 is expressed primarily on endothelial cells but is also found on human peripheral blood monocytes. Through its endothelial mitogenic and hyperpermeability activities, VEGF influences a variety of immune functions related to wound healing and blood protein traffic across endothelial barriers.

Mouse anti VEGFR-3/Flt-4-Biotin (#1) (human)

101-MBi36 50ug
EUR 297.6

Recombinant Human FLT-1/VEGFR-1 Protein

RP01137 50μg
EUR 308.75

Rabbit anti VEGFR-3/Flt-4 (human)

102-PA22AG 50ug
EUR 240

Rabbit anti VEGFR-3/Flt-4 (human)

102-PA22S 100ug
EUR 240

Anti-Human VEGFR-1/Flt-1 (Peptide), soluble Antibody

102-PA21S 100 µg
EUR 126
Description: Endothelial cells express three different vascular endothelial growth factor (VEGF) receptors, belonging to the family of receptor tyrosine kinases (RTKs). They are named VEGFR-1 (Flt-1), VEGFR-2 (KDR/Flk-1), VEGFR-3 (Flt-4). Their expression is almost exclusively restricted to endothelial cells, but VEGFR-1 can also be found on monocytes, dendritic cells and on trophoblast cells. The flt-1 gene was first described in 1990. The receptor contains seven immunoglobulin-like extracellular domains, a single transmembrane region and an intracellular splited tyrosine kinase domain. Compared to VEGFR-2 the Flt-1 receptor has a higher affinity for VEGF but a weaker signaling activity. VEGFR-1 thus leads not to proliferation of endothelial cells, but mediates signals for differentiation. Interestingly a naturally occuring soluble variant of VEGFR-1 (sVEGFR-1) was found in HUVEC supernatants in 1996, which is generated by alternative splicing of the flt-1 mRNA.

Rabbit Anti-Human VEGFR-1 Flt-1 (Peptide), soluble

102-PA21 100ug
EUR 240

Active Recombinant Human FLT-1/VEGFR-1 Protein

RP01188 5 μg
EUR 32.5

Human FLT-1/VEGFR-1 Control/blocking peptide #1

FLT11-P 100 ug
EUR 196.8

Anti-Hu/Mo VEGFR-1/Flt-1, Antagonistic Antibody

mV1004.1m-h-m 100 µg
EUR 645.75
Description: Endothelial cells express three different vascular endothelial growth factor (VEGF) receptors, belonging to the family of receptor tyrosine kinases (RTKs). They are named VEGFR-1 (Flt-1), VEGFR-2 (KDR/Flk-1), VEGFR-3 (Flt-4). Their expression is almost exclusively restricted to endothelial cells, but VEGFR-1 can also be found on monocytes, dendritic cells and on trophoblast cells. The flt-1 gene was first described in 1990. The receptor contains seven immunoglobulin-like extracellular domains, a single transmembrane region and an intracellular splited tyrosine kinase domain. Compared to VEGFR-2 the Flt-1 receptor has a higher affinity for VEGF but a weaker signaling activity. VEGFR-1 thus leads not to proliferation of endothelial cells, but mediates signals for differentiation. Interestingly a naturally occuring soluble variant of VEGFR-1 (sVEGFR-1) was found in HUVEC supernatants in 1996, which is generated by alternative splicing of the flt-1 mRNA. The antibody will bind near the ligand binding site of the receptor and has antagonistic activity by blocking the binding of natural ligands.

Biotinylated Recombinant Human FLT-1/VEGFR-1 Protein

RP02100 500μg
EUR 2843.75

Rabbit Anti-human FLT-1/VEGFR-1 IgG #1, aff pure

FLT11-A 100 ul
EUR 578.4

Human VEGFR-1/Flt-1 (D5), soluble Recombinant Protein

S01-011 5 µg
EUR 73.5
Description: Recombinant human soluble Vascular Endothelial Growth Factor Receptor-1 domain D1-5 (sVEGFR-1(D5)) is a 70 kDa protein. The baculovirus generated, recombinant human sVEGFR-1 is produced as a non-chimeric protein in a monomeric form. The soluble receptor protein contains only the first 5 extracellular domains, which contain all the information necessary for high affinity ligand binding. The receptor monomers have a mass of approximately 70 kDa. Endothelial cells express three different vascular endothelial growth factor (VEGF) receptors, belonging to the family of receptor tyrosine kinases (RTKs). They are named VEGFR-1 (Flt-1), VEGFR-2 (KDR/Flk-1), VEGFR-3 (Flt-4). Their expression is almost exclusively restricted to endothelial cells, but VEGFR-1 can also be found on monocytes, dendritic cells and on trophoblast cells. The flt-1 gene was first described in 1990. The receptor contains seven immunoglobulin-like extracellular domains, a single transmembrane region and an intracellular splited tyrosine kinase domain. Compared to VEGFR-2 the Flt-1 receptor has a higher affinity for VEGF but a weaker signaling activity. VEGFR-1 thus leads not to proliferation of endothelial cells, but mediates signals for differentiation. Interestingly a naturally occuring soluble variant of VEGFR-1 (sVEGFR-1) was found in HUVEC supernatants in 1996, which is generated by alternative splicing of the flt-1 mRNA. The biological functions of sVEGFR-1 still are not clear, but it seems to be an endogenous regulator of angiogenesis, binding VEGF with the same affinity as the full-length receptor.

Human VEGFR-1/Flt-1 (D5), soluble Recombinant Protein

S01-012 20 µg
EUR 157.5
Description: Recombinat human soluble Vascular Endothelial Growth Factor Receptor-1 domain D1-5 (sVEGFR-1(D5)) is a 70 kDa protein containing amino acid residues. The baculovirus generated, recombinant human sVEGFR-1 is produced as a non-chimeric protein in a monomeric form. The soluble receptor protein contains only the first 5 extracellular domains, which contain all the information necessary for high affinity ligand binding. The receptor monomers have a mass of approximately 70 kDa. Endothelial cells express three different vascular endothelial growth factor (VEGF) receptors, belonging to the family of receptor tyrosine kinases (RTKs). They are named VEGFR-1 (Flt-1), VEGFR-2 (KDR/Flk-1), VEGFR-3 (Flt-4). Their expression is almost exclusively restricted to endothelial cells, but VEGFR-1 can also be found on monocytes, dendritic cells and on trophoblast cells. The flt-1 gene was first described in 1990. The receptor contains seven immunoglobulin-like extracellular domains, a single transmembrane region and an intracellular split tyrosine kinase domain. Compared to VEGFR-2 the Flt-1 receptor has a higher affinity for VEGF but a weaker signaling activity. VEGFR-1 thus leads not to proliferation of endothelial cells, but mediates signals for differentiation. Interestingly a naturally occuring soluble variant of VEGFR-1 (sVEGFR-1) was found in HUVE supernatants in 1996, which is generated by alternative splicing of the flt-1 mRNA. The biological functions of sVEGFR-1 still are not clear, but it seems to be an endogenous regulator of angiogenesis, binding VEGF with the same affinity as the full-length receptor.

Human VEGFR-1/Flt-1 (D4), soluble Recombinant Protein

S01-013 5 µg
EUR 103.95
Description: Recombinant Human soluble Vascular Endothelial Growth Factor Receptor-1 domain D1-4 (sVEGFR-1(D4)) is produced as a non-chimeric protein in a monomeric form. The soluble receptor protein contains only the first 4 extracellular domains, which contain all the information necessary for binding of VEGF. The receptor monomers have a mass of approximately 55 kDa containing 457 amino acid residues. Endothelial cells express three different vascular endothelial growth factor (VEGF) receptors, belonging to the family of receptor tyrosine kinases (RTKs). They are named VEGFR-1 (Flt-1), VEGFR-2 (KDR/Flk-1), VEGFR-3 (Flt-4). Their expression is almost exclusively restricted to endothelial cells, but VEGFR-1 can also be found on monocytes, dendritic cells and on trophoblast cells. The flt-1 gene was first described in 1990. The receptor contains seven immunoglobulin-like extracellular domains, a single transmembrane region and an intracellular split tyrosine kinase domain. Compared to VEGFR-2 the Flt-1 receptor has a higher affinity for VEGF but a weaker signaling activity. VEGFR-1 thus leads not to proliferation of endothelial cells, but mediates signals for differentiation. Interestingly a naturally occuring soluble variant of VEGFR-1 (sVEGFR-1) was found in HUVEC supernatants in 1996, which is generated by alternative splicing of the flt-1 mRNA. The biological functions of sVEGFR-1 still are not clear, but it seems to be an endogenous regulator of angiogenesis, binding VEGF with the same affinity as the full-length receptor.

Human VEGFR-1/Flt-1 (D4), soluble Recombinant Protein

S01-014 20 µg
EUR 199.5
Description: Recombinant Human soluble Vascular Endothelial Growth Factor Receptor-1 domain D1-4 (sVEGFR-1(D4)) is produced as a non-chimeric protein in a monomeric form. The soluble receptor protein contains only the first 4 extracellular domains, which contain all the information necessary for binding of VEGF. The receptor monomers have a mass of approximately 55 kDa containing 457 amino acid residues. Endothelial cells express three different vascular endothelial growth factor (VEGF) receptors, belonging to the family of receptor tyrosine kinases (RTKs). They are named VEGFR-1 (Flt-1), VEGFR-2 (KDR/Flk-1), VEGFR-3 (Flt-4). Their expression is almost exclusively restricted to endothelial cells, but VEGFR-1 can also be found on monocytes, dendritic cells and on trophoblast cells. The flt-1 gene was first described in 1990. The receptor contains seven immunoglobulin-like extracellular domains, a single transmembrane region and an intracellular split tyrosine kinase domain. Compared to VEGFR-2 the Flt-1 receptor has a higher affinity for VEGF but a weaker signaling activity. VEGFR-1 thus leads not to proliferation of endothelial cells, but mediates signals for differentiation. Interestingly a naturally occuring soluble variant of VEGFR-1 (sVEGFR-1) was found in HUVEC supernatants in 1996, which is generated by alternative splicing of the flt-1 mRNA. The biological functions of sVEGFR-1 still are not clear, but it seems to be an endogenous regulator of angiogenesis, binding VEGF with the same affinity as the full-length receptor.

Human VEGFR-1/Flt-1 (D3), soluble Recombinant Protein

S01-015 5 µg
EUR 103.95
Description: Recombinant human soluble Vascular Endothelial Growth Factor Receptor-1 domain D1-3 (sVEGFR-1(D3)) is produced as a non-chimeric protein in a monomeric form. The soluble receptor protein contains only the first 3 extracellular domains, which contain all the information necessary for binding of VEGF. The receptor monomers have a mass of approximately 45 kDa containing 352 amino acid residues. Endothelial cells express three different vascular endothelial growth factor (VEGF) receptors, belonging to the family of receptor tyrosine kinases (RTKs). They are named VEGFR-1 (Flt-1), VEGFR-2 (KDR/Flk-1), VEGFR-3 (Flt-4). Their expression is almost exclusively restricted to endothelial cells, but VEGFR-1 can also be found on monocytes, dendritic cells and on trophoblast cells. The flt-1 gene was first described in 1990. The receptor contains seven immunoglobulin-like extracellular domains, a single transmembrane region and an intracellular splited tyrosine kinase domain. Compared to VEGFR-2 the Flt-1 receptor has a higher affinity for VEGF but a weaker signaling activity. VEGFR-1 thus leads not to proliferation of endothelial cells, but mediates signals for differentiation. Interestingly a naturally occuring soluble variant of VEGFR-1 (sVEGFR-1) was found in HUVEC supernatants in 1996, which is generated by alternative splicing of the flt-1 mRNA. The biological functions of sVEGFR-1 still are not clear, but it seems to be an endogenous regulator of angiogenesis, binding VEGF with the same affinity as the full-length receptor.

Human VEGFR-1/Flt-1 (D3), soluble Recombinant Protein

S01-016 20 µg
EUR 199.5
Description: Recombinant human soluble Vascular Endothelial Growth Factor Receptor-1 domain D1-3 (sVEGFR-1(D3)) is produced as a non-chimeric protein in a monomeric form. The soluble receptor protein contains only the first 3 extracellular domains, which contain all the information necessary for binding of VEGF. The receptor monomers have a mass of approximately 45 kDa containing 352 amino acid residues. Endothelial cells express three different vascular endothelial growth factor (VEGF) receptors, belonging to the family of receptor tyrosine kinases (RTKs). They are named VEGFR-1 (Flt-1), VEGFR-2 (KDR/Flk-1), VEGFR-3 (Flt-4). Their expression is almost exclusively restricted to endothelial cells, but VEGFR-1 can also be found on monocytes, dendritic cells and on trophoblast cells. The flt-1 gene was first described in 1990. The receptor contains seven immunoglobulin-like extracellular domains, a single transmembrane region and an intracellular splited tyrosine kinase domain. Compared to VEGFR-2 the Flt-1 receptor has a higher affinity for VEGF but a weaker signaling activity. VEGFR-1 thus leads not to proliferation of endothelial cells, but mediates signals for differentiation. Interestingly a naturally occuring soluble variant of VEGFR-1 (sVEGFR-1) was found in HUVEC supernatants in 1996, which is generated by alternative splicing of the flt-1 mRNA. The biological functions of sVEGFR-1 still are not clear, but it seems to be an endogenous regulator of angiogenesis, binding VEGF with the same affinity as the full-length receptor.

Human VEGFR-1/Flt-1 (native), soluble Recombinant Protein

S01-009 5 µg
EUR 73.5
Description: Recombinant human soluble Vascular Endothelial Growth Factor Receptor-1 (sVEGFR-1) is the naturally occurring form and was cloned from total RNA of human umbilical vein endothelial cells. The recombinant mature sVEGFR-1 is a glycosylated monomeric protein with a mass of approximately 96 kDa. The soluble receptor precursor protein consists of the first 6 extracellular domains (Met1-His688) containing the unique 31 amino acids residues at the C-terminus. Endothelial cells express three different vascular endothelial growth factor (VEGF) receptors, belonging to the family of receptor tyrosine kinases (RTKs). They are named VEGFR-1 (Flt-1), VEGFR-2 (KDR/Flk-1), and VEGFR-3 (Flt-4). Their expression is almost exclusively restricted to endothelial cells, but VEGFR-1 can also be found on monocytes, dendritic cells and on trophoblast cells. The flt-1 gene was first described in 1990. The receptor contains seven immunoglobulin-like extracellular domains, a single transmembrane region and an intracellular split tyrosine kinase domain. Compared to VEGFR-2 the Flt-1 receptor has a higher affinity for VEGF but a weaker signaling activity. VEGFR-1 thus leads not to proliferation of endothelial cells, but mediates signals for differentiation. Interestingly, a naturally occurring soluble variant of VEGFR-1 (sVEGFR-1) was found in HUVEC supernatants in 1996, which is generated by alternative splicing of the flt-1 mRNA. The biological functions of sVEGFR-1 still are not clear, but it seems to be an endogenous regulator of angiogenesis, binding VEGF with the same affinity as the full-length receptor.

Human VEGFR-1/Flt-1 (native), soluble Recombinant Protein

S01-010 20 µg
EUR 157.5
Description: Recombinant human soluble Vascular Endothelial Growth Factor Receptor-1 (sVEGFR-1) is the naturally occurring form and was cloned from total RNA of human umbilical vein endothelial cells. The recombinant mature sVEGFR-1 is a glycosylated monomeric protein with a mass of approximately 96 kDa. The soluble receptor protein consists of the first 6 extracellular domains (Met1-His688) containing the unique 31 amino acids residues at the C-terminus. Endothelial cells express three different vascular endothelial growth factor (VEGF) receptors, belonging to the family of receptor tyrosine kinases (RTKs). They are named VEGFR-1 (Flt-1), VEGFR-2 (KDR/Flk-1), and VEGFR-3 (Flt-4). Their expression is almost exclusively restricted to endothelial cells, but VEGFR-1 can also be found on monocytes, dendritic cells and on trophoblast cells. The flt-1 gene was first described in 1990. The receptor contains seven immunoglobulin-like extracellular domains, a single transmembrane region and an intracellular split tyrosine kinase domain. Compared to VEGFR-2 the Flt-1 receptor has a higher affinity for VEGF but a weaker signaling activity. VEGFR-1 thus leads not to proliferation of endothelial cells, but mediates signals for differentiation. Interestingly, a naturally occurring soluble variant of VEGFR-1 (sVEGFR-1) was found in HUVEC supernatants in 1996, which is generated by alternative splicing of the flt-1 mRNA. The biological functions of sVEGFR-1 still are not clear, but it seems to be an endogenous regulator of angiogenesis binding VEGF with the same affinity as the full-length receptor.

Anti-Human VEGFR-3/FLT-4 Antibody

101-M37 100 µg
EUR 199.5
Description: VEGFR-1 (Flt-1), VEGFR-2 (KDR/Flk 1) and VEGFR-3 (FLT-4) belong to the class III subfamily of receptor tyrosine kinases (RTKs). All three receptors contain seven immunoglobulin-like repeats in their extracellular domains and kinase insert domains in their intracellular regions. The expression of VEGFR-1 to -3 is almost exclusively restricted to hematopoietic precursor cells, vascular and lymphatic endothelial cells and to the monocyte/macrophage lineage. These receptors play essential roles in vasculogenesis, hematopoiesis, angiogenesis and lymphangiogenesis. The VEGFR-3 cDNA encodes a 1298 amino acid (aa) residue precursor protein with a 24 aa residue signal peptide. Mature VEGFR-3 is composed of a 751 aa residue extracellular domain, a 22 aa residue transmembrane domain and a 482 aa residue cytoplasmic domain. Both VEGF-C and VEGF-D have been shown to bind and activate VEGF R3 (Flt-4). The Flt-4 gene is widely expressed in the early embryo but becomes restricted to the lymphatic endothelial a latter stage of development. It is important for lymphangiogenesis.

Anti-Human VEGFR-3/FLT-4 Antibody

101-M38 100 µg
EUR 399
Description: Receptor tyrosine Kinase VEGFR-3, also known as FLT4, together with VEGFR1 (Flt1) and VEGFR2 (KDR/Flk-1), are the receptors for vascular endothelial growth factors (VEGF). The VEGFR family belongs to the class II subfamily of receptor tyrosine kinases (RTKs), containing a large extracellular region which is composed of seven Ig-like domains (D1–D7), a single transmembrane (TM) helix and cytoplasmic region with a tyrosine kinase activity. In VEGFR-3, the fifth Ig homology domain is proteolytically cleaved which results in polypeptides which remain linked by two disulfide bonds. VEGFR-3 is widely expressed on all endothelial cells in early embryogenesis, while, in adult tissues, VEGFR-3 expression disappears from the vascular endothelial cells and is observed only on the lymphatic endothelium. VEGF-C and VEGF-D activation of VEGFR-3 plays an important role in the formation of the lymphatic vessel system.

Anti-Human VEGFR-3/FLT-4 Antibody

101-M870 100 µg
EUR 399
Description: Receptor tyrosine Kinase VEGFR-3, also known as FLT4, together with VEGFR1 (Flt1) and VEGFR2 (KDR/Flk-1), are the receptors for vascular endothelial growth factors (VEGF). The VEGFR family belongs to the class II subfamily of receptor tyrosine kinases (RTKs), containing a large extracellular region which is composed of seven Ig-like domains (D1–D7), a single transmembrane (TM) helix and cytoplasmic region with a tyrosine kinase activity. In VEGFR-3, the fifth Ig homology domain is proteolytically cleaved which results in polypeptides which remain linked by two disulfide bonds. VEGFR-3 is widely expressed on all endothelial cells in early embryogenesis, while, in adult tissues, VEGFR-3 expression disappears from the vascular endothelial cells and is observed only on the lymphatic endothelium. VEGF-C and VEGF-D activation of VEGFR-3 plays an important role in the formation of the lymphatic vessel system.

Anti-Human VEGFR-3/FLT-4 Antibody

102-PA22 200 µg
EUR 147
Description: Receptor tyrosine Kinase VEGFR-3, also known as FLT4, together with VEGFR1 (FIT1) and VEGFR2 (KDR/Flk-1), are the receptors for vascular endothelial growth factors (VEGF). The VEGFR family belongs to the class II subfamily of receptor tyrosine kinases (RTKs), containing a large extracellular region which is composed of seven Ig-like domains (D1–D7), a single transmembrane (TM) helix and cytoplasmic region with a tyrosine kinase activity. In VEGFR-3, the fifth Ig homology domain is proteolytically cleaved which results in polypeptides remain linked by two disulfide bonds. VEGFR-3 is widely expressed on all endothelia cells in early embryogenesis, while, in adult tissues, VEGFR-3 expression disappears from the vascular endothelial cells and is observed only on the lymphatic endothelium. VEGF-C and VEGF-D activation of VEGFR-3 plays an important role in the formation of the lymphatic vessel system.

Anti-Human VEGFR-3/FLT-4 Antibody

102-PABi22 50 µg
EUR 157.5
Description: Receptor tyrosine Kinase VEGFR-3, also known as FLT4, together with VEGFR1 (FIT1) and VEGFR2 (KDR/Flk-1), are the receptors for vascular endothelial growth factors (VEGF). The VEGFR family belongs to the class II subfamily of receptor tyrosine kinases (RTKs), containing a large extracellular region which is composed of seven Ig-like domains (D1–D7), a single transmembrane (TM) helix and cytoplasmic region with a tyrosine kinase activity. In VEGFR-3, the fifth Ig homology domain is proteolytically cleaved which results in polypeptides remain linked by two disulfide bonds. VEGFR-3 is widely expressed on all endothelia cells in early embryogenesis, while, in adult tissues, VEGFR-3 expression disappears from the vascular endothelial cells and is observed only on the lymphatic endothelium. VEGF-C and VEGF-D activation of VEGFR-3 plays an important role in the formation of the lymphatic vessel system.

Human VEGFR-1/Flt-1 (D3)-His, soluble Recombinant Protein

S01-080 50 µg
EUR 378
Description: Recombinant human soluble Vascular Endothelial Growth Factor Receptor-1 domain D1-3 (sVEGFR-1(D3)) is produced as a non-chimeric protein in a monomeric form. The soluble receptor protein contains only the first 3 extracellular domains, which contain all the information necessary for binding of VEGF. The receptor monomers have a mass of approximately 45 kDa containing 352 amino acid residues. Endothelial cells express three different vascular endothelial growth factor (VEGF) receptors, belonging to the family of receptor tyrosine kinases (RTKs). They are named VEGFR-1 (Flt-1), VEGFR-2 (KDR/Flk-1), VEGFR-3 (Flt-4). Their expression is almost exclusively restricted to endothelial cells, but VEGFR-1 can also be found on monocytes, dendritic cells and on trophoblast cells. The flt-1 gene was first described in 1990. The receptor contains seven immunoglobulin-like extracellular domains, a single transmembrane region and an intracellular splited tyrosine kinase domain. Compared to VEGFR-2 the Flt-1 receptor has a higher affinity for VEGF but a weaker signaling activity. VEGFR-1 thus leads not to proliferation of endothelial cells, but mediates signals for differentiation. Interestingly a naturally occuring soluble variant of VEGFR-1 (sVEGFR-1) was found in HUVEC supernatants in 1996, which is generated by alternative splicing of the flt-1 mRNA. The biological functions of sVEGFR-1 still are not clear, but it seems to be an endogenous regulator of angiogenesis, binding VEGF with the same affinity as the full-length receptor.

Mouse Monoclonal Anti-human FLT-1/VEGFR-1 IgG, aff pure

FLT12-M 100 ug
EUR 578.4

Mouse Monoclonal Anti-human FLT-1/VEGFR-1 IgG, aff pure

FLT14-M 100 ug
EUR 578.4

VEGFR-3/Flt-4

JP27779 96
EUR 611

Anti-Mouse VEGFR-3/FLT-4 Antibody

103-M36 100 µg
EUR 246.75
Description: VEGFR-3, also known as FLT4, is a member of the Tyr protein kinase family. The extracellular portion of VEGFR-3 contains 7 immunoglobulin (Ig)-like domains and the cytoplasmic portion contains a protein kinase domain. FLT4 regulates angiogenesis and lymphangiogenesis, its ligands are VEGF-C and D and its binding is mediated by the 2nd and 3rd Ig-like domains of FLT4. During fetal development VEGFR-3 is expressed on endothelial cells, however, in the adult mice, the vascular endothelial cells lose VEGFR-3 expression, but the lymphatic endothelium expresses it constitutively. In addition, VEGFR-3 expression can be induced in tumors with active angiogenesis.

Anti-Mouse VEGFR-3/FLT-4 Antibody

103-M38 100 µg
EUR 399
Description: Receptor tyrosine kinase VEGFR-3, also known as Flt-4, together with VEGFR-1 (Flt-1) and VEGFR-2 (KDR/Flk-1), are the receptors for vascular endothelial growth factors (VEGF). The VEGFR family belongs to the class II subfamily of receptor tyrosine kinases (RTKs), containing a large extracellular region which is composed of seven Ig-like domains (D1–D7), a single transmembrane (TM) helix and cytoplasmic region with a tyrosine kinase activity. In VEGFR-3, the fifth Ig homology domain is proteolytically cleaved which results in polypeptides remaining linked by two disulfide bonds. VEGFR-3 is widely expressed on all endothelial cells in early embryogenesis, while, in adult tissues, VEGFR-3 expression disappears from the vascular endothelial cells and is observed only on the lymphatic endothelium. VEGF-C and VEGF-D activation of VEGFR-3 plays an important role in the formation of the lymphatic vessel system.

Human VEGFR-3 / Flt-4 GENLISA ELISA

KBH0215 1 x 96 wells
EUR 286

Human VEGFR-1/Flt-1(D7)-Fc Chimera, soluble Recombinant Protein

SFC-005 10 µg
EUR 57.75
Description: Recombinant human soluble Vascular Endothelial Growth Factor Receptor-1 (sVEGFR-1(D7)) was fused with the Fc part of human IgG1. The recombinant mature sVEGFR-1(D7)/Fc is a disulfide-linked homodimeric protein. The sVEGFR-1(D7)/Fc monomers have a mass of approximately 130 kDa. The soluble receptor protein consists of all 7 extracellular domains (Met1-Thr751), which contain all the information necessary for high affinity ligand binding. Endothelial cells express three different vascular endothelial growth factor (VEGF) receptors, belonging to the family of receptor tyrosine kinases (RTKs). They are named VEGFR-1 (Flt-1), VEGFR-2 (KDR/Flk-1), and VEGFR-3 (Flt-4). Their expression is almost exclusively restricted to endothelial cells, but VEGFR-1 can also be found on monocytes. All VEGF-receptors have seven immunoglobulin-like extracellular domains, a single transmembrane region and an intracellular split tyrosine kinase domain. VEGFR-2 has a lower affinity for VEGF than the Flt-1 receptor, but a higher signalling activity. Mitogenic activity in endothelial cells is mainly mediated by VEGFR-2 leading to their proliferation. Differential splicing of the flt-1 gene leads to the formation of a secreted, soluble variant of VEGFR-1 (sVEGFR-1). No naturally occurring, secreted forms of VEGFR-2 have so far been reported. The binding of VEGF165 to VEGFR-2 is dependent on heparin.

Human VEGFR-1/Flt-1(D7)-Fc Chimera, soluble Recombinant Protein

SFC-006 50 µg
EUR 168
Description: Recombinant human soluble Vascular Endothelial Growth Factor Receptor-1 (sVEGFR-1(D7)) was fused with the Fc part of human IgG1. The recombinant mature sVEGFR-1(D7)/Fc is a disulfide-linked homodimeric protein. The sVEGFR-1(D7)/Fc monomers have a mass of approximately 130 kDa. The soluble receptor protein consists of all 7 extracellular domains (Met1-Thr751), which contain all the information necessary for high affinity ligand binding. Endothelial cells express three different vascular endothelial growth factor (VEGF) receptors, belonging to the family of receptor tyrosine kinases (RTKs). They are named VEGFR-1 (Flt-1), VEGFR-2 (KDR/Flk-1), and VEGFR-3 (Flt-4). Their expression is almost exclusively restricted to endothelial cells, but VEGFR-1 can also be found on monocytes. All VEGF-receptors have seven immunoglobulin-like extracellular domains, a single transmembrane region and an intracellular split tyrosine kinase domain. VEGFR-2 has a lower affinity for VEGF than the Flt-1 receptor, but a higher signalling activity. Mitogenic activity in endothelial cells is mainly mediated by VEGFR-2 leading to their proliferation. Differential splicing of the flt-1 gene leads to the formation of a secreted, soluble variant of VEGFR-1 (sVEGFR-1). No naturally occurring, secreted forms of VEGFR-2 have so far been reported. The binding of VEGF165 to VEGFR-2 is dependent on heparin.

Rabbit Anti-Mouse FLT-1/VEGFR-1 (279-299aa) IgG, aff pure

FLT15-A 100 ul
EUR 578.4

Human VEGFR-3/FLT-4/Fc Chimera, soluble

SFC-010 50ug
EUR 378

Rabbit Anti-Mouse FLT-4/VEGFR-3 IgG #1, aff pure

FLT41-A 100 ug
EUR 578.4

Active Recombinant Human VEGFR-3/FLT-4 Protein

RP00123 10 μg
EUR 175.5

Human VEGFR-3/FLT-4, soluble Recombinant Protein

S01-017 10 µg
EUR 103.95
Description: Recombinant human soluble Vascular Endothelial Growth Factor Receptor-3 (sVEGFR-3/FLT-4) was fused with a carboxy-terminal 6X histidine-tag. The recombinant mature sVEGFR-3/FLT-4 is a glycosylated monomeric protein. The sVEGFR-3/FLT-4 monomers have a mass of approximately 120 kDa. The soluble receptor protein consists of all 7 extracellular domains (Met1-Glu774). All three VEGF receptors belong to the class III subfamily of receptor tyrosine kinases (RTKs) characterised by the seven immunoglobulin-like loops in the extracellular domain. The expression of VEGFR-1 to -3 is almost exclusively restricted to hematopoietic precursor cells, vascular and lymphatic endothelial cells and to the monocyte/macrophage lineage. They play key roles in vasculogenesis, hematopoiesis, angiogenesis and lymphangiogenesis. The FLT-4 cDNA encodes a 1298 amino acid (aa) residue precursor protein with a 23aa residue signal peptide. Mature VEGFR-3/FLT-4 is composed of a 751aa residue extracellular domain, a 22aa transmembrane domain and a 482aa residue cytoplasmic domain. Both VEGF family members VEGF-C and VEGF-D have been shown to bind and activate VEGFR-3/FLT-4. The Flt-4 gene is widely expressed in the early embryo but becomes restricted to the lymphatic endothelial a latter stages of development. It is important for lymphangiogenesis.

Human VEGFR-3/FLT-4, soluble Recombinant Protein

S01-017S 5 µg
EUR 63
Description: Recombinant human soluble Vascular Endothelial Growth Factor Receptor-3 (sVEGFR-3/FLT-4) was fused with a carboxy-terminal 6X histidine-tag. The recombinant mature sVEGFR-3/FLT-4 is a glycosylated monomeric protein. The sVEGFR-3/FLT-4 monomers have a mass of approximately 120 kDa. The soluble receptor protein consists of all 7 extracellular domains (Met1-Glu774). All three VEGF receptors belong to the class III subfamily of receptor tyrosine kinases (RTKs) characterised by the seven immunoglobulin-like loops in the extracellular domain. The expression of VEGFR-1 to -3 is almost exclusively restricted to hematopoietic precursor cells, vascular and lymphatic endothelial cells and to the monocyte/macrophage lineage. They play key roles in vasculogenesis, hematopoiesis, angiogenesis and lymphangiogenesis. The FLT-4 cDNA encodes a 1298 amino acid (aa) residue precursor protein with a 23aa residue signal peptide. Mature VEGFR-3/FLT-4 is composed of a 751aa residue extracellular domain, a 22aa transmembrane domain and a 482aa residue cytoplasmic domain. Both VEGF family members VEGF-C and VEGF-D have been shown to bind and activate VEGFR-3/FLT-4. The Flt-4 gene is widely expressed in the early embryo but becomes restricted to the lymphatic endothelial a latter stages of development. It is important for lymphangiogenesis.

Human VEGFR-3/FLT-4, soluble Recombinant Protein

S01-018 50 µg
EUR 210
Description: Recombinant human soluble Vascular Endothelial Growth Factor Receptor-3 (sVEGFR-3/FLT-4) was fused with a carboxy-terminal 6X histidine-tag. The recombinant mature sVEGFR-3/FLT-4 is a glycosylated monomeric protein. The sVEGFR-3/FLT-4 monomers have a mass of approximately 120 kDa. The soluble receptor protein consists of all 7 extracellular domains (Met1-Glu774). All three VEGF receptors belong to the class III subfamily of receptor tyrosine kinases (RTKs) characterised by the seven immunoglobulin-like loops in the extracellular domain. The expression of VEGFR-1 to -3 is almost exclusively restricted to hematopoietic precursor cells, vascular and lymphatic endothelial cells and to the monocyte/macrophage lineage. They play key roles in vasculogenesis, hematopoiesis, angiogenesis and lymphangiogenesis. The FLT-4 cDNA encodes a 1298 amino acid (aa) residue precursor protein with a 23 aa residue signal peptide. Mature VEGFR-3/FLT-4 is composed of a 751 aa residue extracellular domain, a 22 aa transmembrane domain and a 482aa residue cytoplasmic domain. Both VEGF family members VEGF-C and VEGF-D have been shown to bind and activate VEGFR-3/FLT-4. The Flt-4 gene is widely expressed in the early embryo but becomes restricted to the lymphatic endothelial a latter stages of development. It is important for lymphangiogenesis.

FLT-1/VEGFR1 Human, Antibody

GWB-BE9645 0.1 mg Ask for price

Rat Monoclonal anti-Mouse VEGFR-3 (FLT-4) Antibody

xAP-0836 100ug
EUR 280

Mouse FLT-4/VEGFR-3 Control/blocking peptide #1

FLT41-P 100 ug
EUR 196.8

Human FLT-4/VEGFR-3 control/blocking peptide #2

FLT42-P 100 ug
EUR 196.8

Rabbit Anti-Human FLT-4/VEGFR-3 IgG #2, aff pure

FLT42-A 100 ug
EUR 578.4

Mouse VEGFR-1/Flt-1(D7)-Fc Chimera, soluble Recombinant Protein

SFC-M05 10 µg
EUR 57.75
Description: Recombinant human soluble Vascular Endothelial Growth Factor Receptor-1 (sVEGFR-1D1-7) was fused with the Fc part of human IgG1. The recombinant mature sVEGFR-1D1-7/Fc is a disulfide-linked homodimeric protein. The sVEGFR-1D1-7/Fc monomers have a mass of approximately 130 kDa. The soluble receptor protein consists of all 7 extracellular domains (Met1-Thr751), which contain all the information necessary for high affinity ligand binding. Endothelial cells express three different vascular endothelial growth factor (VEGF) receptors, belonging to the family of receptor tyrosine kinases (RTKs). They are named VEGFR-1 (Flt-1), VEGFR-2 (KDR/Flk-1), and VEGFR-3 (Flt-4). Their expression is almost exclusively restricted to endothelial cells, but VEGFR-1 can also be found on monocytes. All VEGF-receptors have seven immunoglobulin-like extracellular domains, a single transmembrane region and an intracellular split tyrosine kinase domain. VEGFR-2 has a lower affinity for VEGF than the Flt-1 receptor, but a higher signalling activity. Mitogenic activity in endothelial cells is mainly mediated by VEGFR-2 leading to their proliferation. Differential splicing of the flt-1 gene leads to the formation of a secreted, soluble variant of VEGFR-1 (sVEGFR-1). No naturally occurring, secreted forms of VEGFR-2 have so far been reported. The binding of VEGF165 to VEGFR-2 is dependent on heparin.

Mouse VEGFR-1/Flt-1(D7)-Fc Chimera, soluble Recombinant Protein

SFC-M06 50 µg
EUR 168
Description: Recombinant human soluble Vascular Endothelial Growth Factor Receptor-1 (sVEGFR-1D1-7) was fused with the Fc part of human IgG1. The recombinant mature sVEGFR-1D1-7/Fc is a disulfide-linked homodimeric protein. The sVEGFR-1D1-7/Fc monomers have a mass of approximately 130 kDa. The soluble receptor protein consists of all 7 extracellular domains (Met1-Thr751), which contain all the information necessary for high affinity ligand binding. Endothelial cells express three different vascular endothelial growth factor (VEGF) receptors, belonging to the family of receptor tyrosine kinases (RTKs). They are named VEGFR-1 (Flt-1), VEGFR-2 (KDR/Flk-1), and VEGFR-3 (Flt-4). Their expression is almost exclusively restricted to endothelial cells, but VEGFR-1 can also be found on monocytes. All VEGF-receptors have seven immunoglobulin-like extracellular domains, a single transmembrane region and an intracellular split tyrosine kinase domain. VEGFR-2 has a lower affinity for VEGF than the Flt-1 receptor, but a higher signaling activity. Mitogenic activity in endothelial cells is mainly mediated by VEGFR-2 leading to their proliferation. Differential splicing of the flt-1 gene leads to the formation of a secreted, soluble variant of VEGFR-1 (sVEGFR-1). No naturally occurring, secreted forms of VEGFR-2 have so far been reported. The binding of VEGF165 to VEGFR-2 is dependent on heparin.

Human VEGFR1/Flt-1 ELISA KIT

E42EH-249 96T/48T Ask for price

Human VEGFR-1/Flt1 ELISA Kit

EHV0045 96Tests
EUR 625.2

Human VEGFR-3/FLT-4/Fc Chimera, soluble Recombinant Protein

SFC-009 10 µg
EUR 73.5
Description: Recombinant human soluble Vascular Endothelial Growth Factor Receptor-3 (sVEGFR-3) was fused with the Fc part of human IgG1. The recombinant mature sVEGFR-3/Fc is a disulfide-linked homodimeric protein. The sVEGFR-3/Fc monomers have a mass of approximately 130 kDa. The soluble receptor protein consists of all 7 extracellular domains (Met1-Glu774). All three VEGF receptors belong to the class III subfamily of receptor tyrosine kinases (RTKs) characterised by the seven immunoglobulin-like loops in the extracellular domain. The expression of VEGFR-1 to -3 is almost exclusively restricted to hematopoietic precursor cells, vascular and lymphatic endothelial cells and to the monocyte/macrophage lineage. They play key roles in vasculogenesis, hematopoiesis, angiogenesis and lymphangiogenesis. The VEGFR-3/FLT-4 cDNA encodes a 1298 amino acid (aa) residue precursor protein with a 23aa residue signal peptide. Mature VEGFR-3/FLT-4 is composed of a 751aa residue extracellular domain, a 22aa transmembrane domain and a 482aa residue cytoplasmic domain. Both VEGF family members VEGF-C and VEGF-D have been shown to bind and activate VEGFR-3/FLT-4. The FLT-4 gene is widely expressed in the early embryo but becomes restricted to the lymphatic endothelial at latter stages of development. It is important for lymphangiogenesis.

VEGFR-1/Flt1/ Rat VEGFR- 1/ Flt1 ELISA Kit

ELA-E0147r 96 Tests
EUR 1063.2

Anti-VEGFR-1/FLT-1 antibody

PAab09393 100 ug
EUR 426

FLT-1/ VEGFR1 AB1

GWB-91AE5A 0.5 ml Ask for price

VEGFR1 / Flt-1(FLT1/659) Antibody

BNC040659-100 100uL
EUR 238.8
Description: Primary antibody against VEGFR1 / Flt-1(FLT1/659), CF405S conjugate, Concentration: 0.1mg/mL

VEGFR1 / Flt-1(FLT1/659) Antibody

BNC040659-500 500uL
EUR 652.8
Description: Primary antibody against VEGFR1 / Flt-1(FLT1/659), CF405S conjugate, Concentration: 0.1mg/mL

VEGFR1 / Flt-1(FLT1/658) Antibody

BNC810658-100 100uL
EUR 238.8
Description: Primary antibody against VEGFR1 / Flt-1(FLT1/658), CF680R conjugate, Concentration: 0.1mg/mL

VEGFR1 / Flt-1(FLT1/658) Antibody

BNC810658-500 500uL
EUR 652.8
Description: Primary antibody against VEGFR1 / Flt-1(FLT1/658), CF680R conjugate, Concentration: 0.1mg/mL

VEGFR1 / Flt-1(FLT1/659) Antibody

BNC810659-100 100uL
EUR 238.8
Description: Primary antibody against VEGFR1 / Flt-1(FLT1/659), CF680R conjugate, Concentration: 0.1mg/mL

VEGFR1 / Flt-1(FLT1/659) Antibody

BNC810659-500 500uL
EUR 652.8
Description: Primary antibody against VEGFR1 / Flt-1(FLT1/659), CF680R conjugate, Concentration: 0.1mg/mL

VEGFR1 / Flt-1(FLT1/659) Antibody

BNC940659-100 100uL
EUR 238.8
Description: Primary antibody against VEGFR1 / Flt-1(FLT1/659), CF594 conjugate, Concentration: 0.1mg/mL

VEGFR1 / Flt-1(FLT1/659) Antibody

BNC940659-500 500uL
EUR 652.8
Description: Primary antibody against VEGFR1 / Flt-1(FLT1/659), CF594 conjugate, Concentration: 0.1mg/mL

VEGFR1 / Flt-1(FLT1/659) Antibody

BNC880659-100 100uL
EUR 238.8
Description: Primary antibody against VEGFR1 / Flt-1(FLT1/659), CF488A conjugate, Concentration: 0.1mg/mL

VEGFR1 / Flt-1(FLT1/659) Antibody

BNC880659-500 500uL
EUR 652.8
Description: Primary antibody against VEGFR1 / Flt-1(FLT1/659), CF488A conjugate, Concentration: 0.1mg/mL

VEGFR1 / Flt-1(FLT1/658) Antibody

BNC800658-100 100uL
EUR 238.8
Description: Primary antibody against VEGFR1 / Flt-1(FLT1/658), CF680 conjugate, Concentration: 0.1mg/mL

VEGFR1 / Flt-1(FLT1/658) Antibody

BNC800658-500 500uL
EUR 652.8
Description: Primary antibody against VEGFR1 / Flt-1(FLT1/658), CF680 conjugate, Concentration: 0.1mg/mL

VEGFR1 / Flt-1(FLT1/659) Antibody

BNC800659-100 100uL
EUR 238.8
Description: Primary antibody against VEGFR1 / Flt-1(FLT1/659), CF680 conjugate, Concentration: 0.1mg/mL

VEGFR1 / Flt-1(FLT1/659) Antibody

BNC800659-500 500uL
EUR 652.8
Description: Primary antibody against VEGFR1 / Flt-1(FLT1/659), CF680 conjugate, Concentration: 0.1mg/mL

VEGFR1 / Flt-1(FLT1/658) Antibody

BNC430658-100 100uL
EUR 238.8
Description: Primary antibody against VEGFR1 / Flt-1(FLT1/658), CF543 conjugate, Concentration: 0.1mg/mL

VEGFR1 / Flt-1(FLT1/658) Antibody

BNC430658-500 500uL
EUR 652.8
Description: Primary antibody against VEGFR1 / Flt-1(FLT1/658), CF543 conjugate, Concentration: 0.1mg/mL

VEGFR1 / Flt-1(FLT1/659) Antibody

BNC430659-100 100uL
EUR 238.8
Description: Primary antibody against VEGFR1 / Flt-1(FLT1/659), CF543 conjugate, Concentration: 0.1mg/mL

VEGFR1 / Flt-1(FLT1/659) Antibody

BNC430659-500 500uL
EUR 652.8
Description: Primary antibody against VEGFR1 / Flt-1(FLT1/659), CF543 conjugate, Concentration: 0.1mg/mL

VEGFR1 / Flt-1(FLT1/659) Antibody

BNC400659-100 100uL
EUR 238.8
Description: Primary antibody against VEGFR1 / Flt-1(FLT1/659), CF640R conjugate, Concentration: 0.1mg/mL

VEGFR1 / Flt-1(FLT1/659) Antibody

BNC400659-500 500uL
EUR 652.8
Description: Primary antibody against VEGFR1 / Flt-1(FLT1/659), CF640R conjugate, Concentration: 0.1mg/mL

VEGFR1 / Flt-1(FLT1/658) Antibody

BNC050658-100 100uL
EUR 238.8
Description: Primary antibody against VEGFR1 / Flt-1(FLT1/658), CF405M conjugate, Concentration: 0.1mg/mL

VEGFR1 / Flt-1(FLT1/658) Antibody

BNC050658-500 500uL
EUR 652.8
Description: Primary antibody against VEGFR1 / Flt-1(FLT1/658), CF405M conjugate, Concentration: 0.1mg/mL

VEGFR1 / Flt-1(FLT1/659) Antibody

BNC050659-100 100uL
EUR 238.8
Description: Primary antibody against VEGFR1 / Flt-1(FLT1/659), CF405M conjugate, Concentration: 0.1mg/mL

VEGFR1 / Flt-1(FLT1/659) Antibody

BNC050659-500 500uL
EUR 652.8
Description: Primary antibody against VEGFR1 / Flt-1(FLT1/659), CF405M conjugate, Concentration: 0.1mg/mL

VEGFR1 / Flt-1(FLT1/659) Antibody

BNC470659-100 100uL
EUR 238.8
Description: Primary antibody against VEGFR1 / Flt-1(FLT1/659), CF647 conjugate, Concentration: 0.1mg/mL

VEGFR1 / Flt-1(FLT1/659) Antibody

BNC470659-500 500uL
EUR 652.8
Description: Primary antibody against VEGFR1 / Flt-1(FLT1/659), CF647 conjugate, Concentration: 0.1mg/mL

VEGFR1 / Flt-1(FLT1/658) Antibody

BNC550658-100 100uL
EUR 238.8
Description: Primary antibody against VEGFR1 / Flt-1(FLT1/658), CF555 conjugate, Concentration: 0.1mg/mL

VEGFR1 / Flt-1(FLT1/658) Antibody

BNC550658-500 500uL
EUR 652.8
Description: Primary antibody against VEGFR1 / Flt-1(FLT1/658), CF555 conjugate, Concentration: 0.1mg/mL