Anti-VEGFR2 Antibody, Highly Galactosylated (CAT#: BioBet-GA-039ZP) Datasheet

VEGFR2

vascular endothelial growth factor receptor 2

Kinase Insert Domain Receptor, Kinase Insert Domain Receptor (A Type III Receptor Tyrosine Kinase), Vascular Endothelial Growth Factor Receptor 2, Protein-Tyrosine Kinase Receptor Flk-1, Fetal Liver Kinase 1, EC 2.7.10.1, VEGFR2, FLK1, Tyrosine Kinase Growth Factor Receptor;

Plasma membrane, Extracellular region or secreted Cytosol, Endosome, Nucleus, ER

Its related pathways are Cell adhesion_Plasmin signaling and Signaling by GPCR.

Tyrosine protein kinase acts as a cell surface receptor for VEGFA, VEGFC and VEGFD. It plays an important role in the regulation of angiogenesis, vascular development, vascular permeability and embryonic hematopoiesis. Promote the proliferation, survival, migration and differentiation of endothelial cells. Promote the reorganization of the actin cytoskeleton. Isomers lacking transmembrane domains, such as Isomer 2 and Isomer 3, may act as decoy receptors for VEGFA, VEGFC, and/or VEGFD. As a negative regulator of VEGFA and VEGFC-mediated lymphangiogenesis, Isoform 2 plays an important role by limiting the amount of free VEGFA and/or VEGFC and preventing them from binding to FLT4. Regulation of FLT1 and FLT4 signals by forming heterodimers. The combination of angiogenesis factor and isoform 1 leads to the activation of multiple signal cascades. The activation of PLCG1 leads to the production of cell signaling molecules triglyceride and inositol 1,4,5-triphosphate and the activation of protein kinase c, which mediates the activation of MAPK1/ERK2, MAPK3/ERK1 and map kinase signaling pathways, and AKT1 signaling Activation of the pathway. Mediates the phosphorylation of PIK3R1, which is the regulatory subunit of phosphatidylinositol 3-kinase, recombines the actin cytoskeleton and activates PTK2/FAK1. The induction of NOS2 and NOS3 mediated by vegfa causes endothelial cells to produce the signal molecule nitric oxide (NO). Phosphorylate PLCG1. Promote the phosphorylation of FYN, NCK1, NOS3, PIK3R1, PTK2/FAK1 and SRC.

1.N-glycosylated. 2.Ubiquitinated. Tyrosine phosphorylation of the receptor promotes its poly-ubiquitination, leading to its degradation via the proteasome or lysosomal proteases. 3. Autophosphorylated on tyrosine residues upon ligand binding. Autophosphorylation occurs intrans, i.e. one subunit of the dimeric receptor phosphorylates tyrosine residues on the other subunit. Phosphorylation at Tyr-951 is important for interaction with SH2D2A/TSAD and VEGFA-mediated reorganization of the actin cytoskeleton. Phosphorylation at Tyr-1175 is important for interaction with PLCG1 and SHB. Phosphorylation at Tyr-1214 is important for interaction with NCK1 and FYN. Dephosphorylated by PTPRB. Dephosphorylated by PTPRJ at Tyr-951, Tyr-996, Tyr-1054, Tyr-1059, Tyr-1175 and Tyr-1214. 4.The inhibitory disulfide bond between Cys-1024 and Cys-1045 may serve as a specific molecular switch for H(2)S-induced modification that regulates VEGFR2 function.

Protein Based Therapies
Monoclonal antibody (mAb)

IgG1

BioBet-GA-039ZP

Human

Human

Ramucirumab (LY3009806, IMC-1121B, trade name Cyramza) is a human monoclonal antibody (IgG1) against vascular endothelial growth factor receptor 2 (VEGFR2). The drug was developed by ImClone Systems Inc. and used to treat solid tumors, including adenocarcinoma of the advanced stomach or gastroesophageal junction.

Advanced Gastric Cancer
Advanced gastro-esophageal junction adenocarcinoma
Refractory, metastatic Colorectal cancer
Refractory, metastatic Non small cell lung cancer

Advanced Gastric Cancer
Advanced gastro-esophageal junction adenocarcinoma
Refractory, metastatic Colorectal cancer
Refractory, metastatic Non small cell lung cancer