protein

VEGFR2-Fc Vascular Endothelial Growth Factor Receptor-2 Fc Chimera Human Recombinant Protein

PROTP35968-2

2 ug, 10 ug, 1 mg

Enabled

VEGFR2-Fc Vascular Endothelial Growth Factor Receptor-2 Fc Chimera Human Recombinant Protein

KDR

Sample: 2ug / $153 Regular: 10ug / $230 Bulk: 1mg / $4483

No

KDR fusion protein was lyophilized from a concentrated (1mg/ml) sterile solution containing 1xPBS pH-7.2.

Soluble VEGFR2 Fc Human Recombinant fused with the Fc part of human IgG1 produced in baculovirus is a disulfide-linked homodimeric, glycosylated, polypeptide containing 968 amino acids and having a molecular mass of 145 kDa. The soluble receptor protein contains only the first 7 extracellular domains, which contain all the information necessary for ligand binding.

Soluble VEGFR2 Fc Human Recombinant fused with the Fc part of human IgG145 kDa. The soluble receptor protein contains only the first 7 extracellular domains, which contain all the information necessary for ligand binding.

Introduction . 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. 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 occuring, secreted forms of VEGFR-2 have so far been reported. The binding of VEGF165 to VEGFR-2 is dependent on heparin.

Amino Acid Sequence ASVGLPSVSL DLPRLSIQKD ILTIKANTTL QITCRGQRDL DWLWPNNQSG SEQRVEVTEC SDGLFCKTLT IPKVIGNDTG AYKCFYRETD LASVIYVYVQ DYRSPFIASV SDQHGVVYIT ENKNKTVVIP CLGSISNLNV SLCARYPEKR FVPDGNRISW DSKKGFTIPS YMISYAGMVF CEAKINDESY QSIMYIVVVV GYRIYDVVLS PSHGIELSVG EKLVLNCTAR TELNVGIDFN WEYPSSKHQH KKLVNRDLKT QSGSEMKKFL STLTIDGVTR SDQGLYTCAA SSGLMTKKNS TFVRVHEKPF VAFGSGMESL VEATVGERVR IPAKYLGYPP PEIKWYKNGI PLESNHTIKA GHVLTIMEVS ERDTGNYTVI LTNPISKEKQ SHVVSLVVYV PPQIGEKSLI SPVDSYQYGT TQTLTCTVYA IPPPHHIHWY WQLEEECANE PSQAVSVTNP YPCEEWRSVE DFQGGNKIEV NKNQFALIEG KNKTVSTLVI QAANVSALYK CEAVNKVGRG ERVISFHVTR GPEITLQPDM QPTEQESVSL WCTADRSTFE NLTWYKLGPQ PLPIHVGELP TPVCKNLDTL WKLNATMFSN STNDILIMEL KNASLQDQGD YVCLAQDRKT KKRHCVVRQL TVLERVAPTI TGNLENQTTS IGESIEVSCT ASGNPPPQIM WFKDNETLVE DSGIVLKDGN RNLTIRRVRK EDEGLYTCQA CSVLGCAKVE AFFIIEGANA SDKTHTCPPC PAPELLGGPS VFLFPPKPKD TLMISRTPEV TCVVVDVSHE DPEVKFNWYV DGVEVHNAKT KPREEQYNST YRVVSVLTVL HQDWLNGKEY KCKVSNKALP APIEKTISKA KGQPREPQVY TLPPSREEMT KNQVSLTCLV KGFYPSDIAV EWESNGQPEN NYKTTPPMLD SDGSFFLYSK LTVDKSRWQQ GNVFSCSVMH EALHNHYTQK SLSLSPGK. Biological Activity The activity of sVEGFR2/Fc was determined by its ability to inhibit the VEGF-dependent proliferation of human umbilical vein endothelial cells.

2 ug, 10 ug, 1 mg

P35968

No

Sterile Filtered White lyophilized (freeze-dried) powder.

Greater than 90.0% as determined by SDS-PAGE.

Store in -20 C for long term storage. After reconstitution, store in 4 C for short term usage within a few days. Avoid freeze-thaw cycles.

Cell Culture

Recombinant protein fun image

Vascular endothelial growth factor receptor 2;VEGFR-2;2.7.10.1;Fetal liver kinase 1;FLK-1;Kinase insert domain receptor;KDR;Protein-tyrosine kinase receptor flk-1;CD309;KDR;FLK1, VEGFR2;

Vascular endothelial growth factor receptor 2

Tyrosine-protein kinase that acts as a cell-surface receptor for VEGFA, VEGFC and VEGFD. Plays an essential role in the regulation of angiogenesis, vascular development, vascular permeability, and embryonic hematopoiesis. Promotes proliferation, survival, migration and differentiation of endothelial cells. Promotes reorganization of the actin cytoskeleton. Isoforms lacking a transmembrane domain, such as isoform 2 and isoform 3, may function as decoy receptors for VEGFA, VEGFC and/or VEGFD. Isoform 2 plays an important role as negative regulator of VEGFA- and VEGFC-mediated lymphangiogenesis by limiting the amount of free VEGFA and/or VEGFC and preventing their binding to FLT4. Modulates FLT1 and FLT4 signaling by forming heterodimers. Binding of vascular growth factors to isoform 1 leads to the activation of several signaling cascades. Activation of PLCG1 leads to the production of the cellular signaling molecules diacylglycerol and inositol 1,4,5-trisphosphate and the activation of protein kinase C. Mediates activation of MAPK1/ERK2, MAPK3/ERK1 and the MAP kinase signaling pathway, as well as of the AKT1 signaling pathway. Mediates phosphorylation of PIK3R1, the regulatory subunit of phosphatidylinositol 3-kinase, reorganization of the actin cytoskeleton and activation of PTK2/FAK1. Required for VEGFA-mediated induction of NOS2 and NOS3, leading to the production of the signaling molecule nitric oxide (NO) by endothelial cells. Phosphorylates PLCG1. Promotes phosphorylation of FYN, NCK1, NOS3, PIK3R1, PTK2/FAK1 and SRC.

Cell junction

Detected in cornea (at protein level). Widely expressed.

Insect Cells.

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