Mouse Anti-Human VEGFR-1/Flt-1
MBS690109-005mg	MyBiosource	0.05mg	EUR 450

Mouse Anti-Human VEGFR-1/Flt-1
MBS690109-5x005mg	MyBiosource	5x0.05mg	EUR 1725

Mouse Anti-Human VEGFR-1/Flt-1
MBS690355-01mg	MyBiosource	0.1mg	EUR 450

Mouse Anti-Human VEGFR-1/Flt-1
MBS690355-5x01mg	MyBiosource	5x0.1mg	EUR 1725

Mouse Anti-Human VEGFR-1/Flt-1
MBS690361-01mg	MyBiosource	0.1mg	EUR 450

Mouse Anti-Human VEGFR-1/Flt-1
MBS690361-5x01mg	MyBiosource	5x0.1mg	EUR 1725

Mouse Anti-Human VEGFR-1/Flt-1
MBS690384-005mg	MyBiosource	0.05mg	EUR 430

Mouse Anti-Human VEGFR-1/Flt-1
MBS690384-5x005mg	MyBiosource	5x0.05mg	EUR 1645

Mouse Anti-Human VEGFR-1/Flt-1
MBS690483-005mg	MyBiosource	0.05mg	EUR 430

Mouse Anti-Human VEGFR-1/Flt-1
MBS690483-5x005mg	MyBiosource	5x0.05mg	EUR 1645

Mouse Anti-Human VEGFR-1/Flt-1
MBS690832-01mg	MyBiosource	0.1mg	EUR 430

Mouse Anti-Human VEGFR-1/Flt-1
MBS690832-5x01mg	MyBiosource	5x0.1mg	EUR 1645

anti- VEGFR-1/FLT-1 antibody
FNab09393	FN Test	100µg	EUR 606.3
Description: Antibody raised against VEGFR-1/FLT-1

Anti-Human VEGFR-1/Flt-1 Antibody
101-MBi24	ReliaTech	50 µg	EUR 246.75
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.

Anti-Human VEGFR-1/Flt-1 Antibody
101-MBi30	ReliaTech	50 µg	EUR 189
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-PA20	ReliaTech	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	ReliaTech	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-1/Flt-1-Biotin (#EWF) (human)
101-MBi28	Angio Proteomie	50ug	EUR 297.6

Human VEGFR-1/Flt-1 (D5), soluble
MBS691664-002mg	MyBiosource	0.02mg	EUR 380

Human VEGFR-1/Flt-1 (D5), soluble
MBS691664-5x002mg	MyBiosource	5x0.02mg	EUR 1410

Human VEGFR-1/Flt-1 (D5), soluble
MBS691669-0005mg	MyBiosource	0.005mg	EUR 265

Human VEGFR-1/Flt-1 (D5), soluble
MBS691669-5x0005mg	MyBiosource	5x0.005mg	EUR 890

Human VEGFR-1/Flt-1 (D3), soluble
MBS691717-002mg	MyBiosource	0.02mg	EUR 450

Human VEGFR-1/Flt-1 (D3), soluble
MBS691717-5x002mg	MyBiosource	5x0.02mg	EUR 1725

Human VEGFR-1/Flt-1 (D4), soluble
MBS691847-0005mg	MyBiosource	0.005mg	EUR 310

Human VEGFR-1/Flt-1 (D4), soluble
MBS691847-5x0005mg	MyBiosource	5x0.005mg	EUR 1110

Human VEGFR-1/Flt-1 (D3), soluble
MBS692000-0005mg	MyBiosource	0.005mg	EUR 310

Human VEGFR-1/Flt-1 (D3), soluble
MBS692000-5x0005mg	MyBiosource	5x0.005mg	EUR 1110

Human VEGFR-1/Flt-1 (D4), soluble
MBS692119-002mg	MyBiosource	0.02mg	EUR 450

Human VEGFR-1/Flt-1 (D4), soluble
MBS692119-5x002mg	MyBiosource	5x0.02mg	EUR 1725

Human VEGFR-1/Flt-1 (native), soluble
MBS691505-0005mg	MyBiosource	0.005mg	EUR 265

Human VEGFR-1/Flt-1 (native), soluble
MBS691505-5x0005mg	MyBiosource	5x0.005mg	EUR 890

Human VEGFR-1/Flt-1 (native), soluble
MBS691991-002mg	MyBiosource	0.02mg	EUR 380

Human VEGFR-1/Flt-1 (native), soluble
MBS691991-5x002mg	MyBiosource	5x0.02mg	EUR 1410

Mouse anti VEGFR-3/Flt-4-Biotin (#1) (human)
101-MBi36	Angio Proteomie	50ug	EUR 297.6

VEGFR-1 / FLT-1 Antibody
abx239393-100ug	Abbexa	100 ug	EUR 577.2

VEGFR-1/FLT-1 antibody
E39-09393	EnoGene	100ug/100ul	EUR 225
Description: Available in various conjugation types.

VEGFR-1/FLT-1 antibody
CAF50629-100ug	Biomatik Corporation	100ug	EUR 312

Anti-Mouse VEGFR-1/Flt-1 Antibody
103-M31	ReliaTech	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.

Recombinant Human FLT-1/VEGFR-1 Protein
RP01137	Abclonal	50μg	EUR 308.75

Recombinant Human FLT-1/VEGFR-1 Protein
RP02099	Abclonal	100μg	EUR 205.47

Human VEGFR-1/Flt-1 (D3)-His, soluble
MBS692528-005mg	MyBiosource	0.05mg	EUR 725

Human VEGFR-1/Flt-1 (D3)-His, soluble
MBS692528-5x005mg	MyBiosource	5x0.05mg	EUR 2965

Rabbit anti VEGFR-3/Flt-4 (human)
102-PA22AG	Angio Proteomie	50ug	EUR 240

Rabbit anti VEGFR-3/Flt-4 (human)
102-PA22S	Angio Proteomie	100ug	EUR 240

Anti-Human VEGFR-3/FLT-4 (#1) Antibody
MBS4158541-01mg	MyBiosource	0.1mg	EUR 920

Anti-Human VEGFR-3/FLT-4 (#1) Antibody
MBS4158541-5x01mg	MyBiosource	5x0.1mg	EUR 3880

Anti-Human VEGFR-1/Flt-1 (Peptide), soluble Antibody
102-PA21S	ReliaTech	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	Angio Proteomie	100ug	EUR 240

Human VEGFR-1/Flt-1(D7)-Fc Chimera, soluble
MBS691483-005mg	MyBiosource	0.05mg	EUR 395

Human VEGFR-1/Flt-1(D7)-Fc Chimera, soluble
MBS691483-5x005mg	MyBiosource	5x0.05mg	EUR 1490

Human VEGFR-1/Flt-1(D7)-Fc Chimera, soluble
MBS691782-001mg	MyBiosource	0.01mg	EUR 245

Human VEGFR-1/Flt-1(D7)-Fc Chimera, soluble
MBS691782-5x001mg	MyBiosource	5x0.01mg	EUR 805

Active Recombinant Human FLT-1/VEGFR-1 Protein
RP01188	Abclonal	5 μg	EUR 32.5

Human FLT-1/VEGFR-1 Control/blocking peptide #1
FLT11-P	Alpha Diagnostics	100 ug	EUR 196.8

Biotinylated Recombinant Human FLT-1/VEGFR-1 Protein
RP02100	Abclonal	500μg	EUR 2843.75

Anti-Human VEGFR-l/Flt-1 (#EWC) Antibody
MBS4158536-01mg	MyBiosource	0.1mg	EUR 920

Anti-Human VEGFR-l/Flt-1 (#EWC) Antibody
MBS4158536-5x01mg	MyBiosource	5x0.1mg	EUR 3880

Anti-Human VEGFR-l/Flt-1 (#EIC) Antibody
MBS4158537-01mg	MyBiosource	0.1mg	EUR 920

Anti-Human VEGFR-l/Flt-1 (#EIC) Antibody
MBS4158537-5x01mg	MyBiosource	5x0.1mg	EUR 3880

Anti-Human VEGFR-l/Flt-1 (#EWF) Antibody
MBS4158538-01mg	MyBiosource	0.1mg	EUR 920

Anti-Human VEGFR-l/Flt-1 (#EWF) Antibody
MBS4158538-5x01mg	MyBiosource	5x0.1mg	EUR 3880

Human VEGFR-1/Flt-1 (D5), soluble Recombinant Protein
S01-011	ReliaTech	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	ReliaTech	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	ReliaTech	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	ReliaTech	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	ReliaTech	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	ReliaTech	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	ReliaTech	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	ReliaTech	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.

Rabbit Anti-human FLT-1/VEGFR-1 IgG #1, aff pure
FLT11-A	Alpha Diagnostics	100 ul	EUR 578.4

Anti-Hu/Mo VEGFR-1/Flt-1, Antagonistic Antibody
mV1004.1m-h-m	ReliaTech	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.

Human VEGFR-1/Flt-1 (D3)-His, soluble Recombinant Protein
S01-080	ReliaTech	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.

Human VEGFR-3/FLT-4, soluble
MBS691602-001mg	MyBiosource	0.01mg	EUR 310

Human VEGFR-3/FLT-4, soluble
MBS691602-5x001mg	MyBiosource	5x0.01mg	EUR 1110

Human VEGFR-3/FLT-4, soluble
MBS691970-005mg	MyBiosource	0.05mg	EUR 465

Human VEGFR-3/FLT-4, soluble
MBS691970-5x005mg	MyBiosource	5x0.05mg	EUR 1805

Human VEGFR-3/FLT-4, soluble
MBS692181-0005mg	MyBiosource	0.005mg	EUR 250

Human VEGFR-3/FLT-4, soluble
MBS692181-5x0005mg	MyBiosource	5x0.005mg	EUR 835

Anti-Human VEGFR-l/Flt-1 (#EWF) Biotin Antibody
MBS4158553-005mg	MyBiosource	0.05mg	EUR 920

Anti-Human VEGFR-l/Flt-1 (#EWF) Biotin Antibody
MBS4158553-5x005mg	MyBiosource	5x0.05mg	EUR 3880

Anti-Human VEGFR-3/FLT-4 (CL 1) Biotin Antibody
MBS4158555-005mg	MyBiosource	0.05mg	EUR 920

Anti-Human VEGFR-3/FLT-4 (CL 1) Biotin Antibody
MBS4158555-5x005mg	MyBiosource	5x0.05mg	EUR 3880

Mouse Anti-Human VEGFR-3/FLT-4
MBS690017-01mg	MyBiosource	0.1mg	EUR 450

Mouse Anti-Human VEGFR-3/FLT-4
MBS690017-5x01mg	MyBiosource	5x0.1mg	EUR 1725

Mouse Anti-Human VEGFR-3/FLT-4
MBS690153-01mg	MyBiosource	0.1mg	EUR 450

Mouse Anti-Human VEGFR-3/FLT-4
MBS690153-5x01mg	MyBiosource	5x0.1mg	EUR 1725

Mouse Anti-Human VEGFR-3/FLT-4
MBS690532-005mg	MyBiosource	0.05mg	EUR 450

Mouse Anti-Human VEGFR-3/FLT-4
MBS690532-5x005mg	MyBiosource	5x0.05mg	EUR 1725