抗体

抗VEGFR2/激酶插入区受体单克隆抗体

MA1040

100μg/vial

315美元

单克隆

小鼠

未共轭

激酶插入区受体-1

人类, 大鼠

抗VEGFR2/激酶插入区受体单克隆抗体

315美元

100μg/vial

单克隆

激酶插入区受体-1

小鼠

人类

免疫组化

免疫组化(冰冻切片), 1-2µg/毫升, 人类

Other applications have not been tested. Optimal dilutions should be determined by end users.

Boster Bio Anti-VEGFR2/KDR Monoclonal Antibody catalog # MA1040. Tested in IHC applications. This antibody reacts with Human.

Adding 1 ml of PBS buffer will yield a concentration of 100 μg/ml.

激酶插入区受体

O08775

Recombinant human extracellular domain of VEGFR-2 (KDR).

冻干

Mouse ascites fluid, 1.2% sodium acetate, 2mg BSA, with 0.01mg NaN3 as preservative.

腹水

No cross reactivity with other proteins

小鼠IgG1

Store at -20˚C for one year from date of receipt. After reconstitution, at 4˚C for one month. It can also be aliquotted and stored frozen at -20˚C for six months. Avoid repeated freeze-thaw cycles.

Add 1ml of PBS buffer will yield a concentration of 100ug/ml.

血管内皮生长因子受体2

Vascular endothelial growth factor receptor 2; VEGFR-2; 2.7.10.1; Fetal liver kinase 1; FLK-1; Protein-tyrosine kinase receptor flk-1; CD309; Kdr; Flk1;

血管内皮生长因子受体2

150394分子量

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 may function as decoy receptors for VEGFA, VEGFC and/or VEGFD. 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 (By similarity).

Cell membrane ; Single-pass type I membrane protein. Cytoplasm. Nucleus. Cytoplasmic vesicle. Early endosome. Cell junction. Endoplasmic reticulum. Detected on caveolae-enriched lipid rafts at the cell surface. Is recycled from the plasma membrane to endosomes and back again. Phosphorylation triggered by VEGFA binding promotes internalization and subsequent degradation. VEGFA binding triggers internalization and translocation to the nucleus. Localized with RAP1A at cell-cell junctions. Colocalizes with ERN1 and XBP1 in the endoplasmic reticulum in endothelial cells in a vascular endothelial growth factor (VEGF)-dependent manner (By similarity).

Expressed in the post-pubertal mammary glands.

Boster recommends HRP Conjugated anti-Mouse IgG Super Vision Assay Kit (SV0001-1) for IHC(F).

Belongs to the protein kinase superfamily. Tyr protein kinase family. CSF-1/PDGF receptor subfamily.

VEGF, a homodimeric glycoprotein of relative molecular mass 45,000, is the only mitogen that specifically acts on endothelial cells. The importance of VEGF and its receptor system in tumor growth and intervention in this system may provide promising approaches to cancer therapy. VEGF receptor 2 is a member of a receptor tyrosine kinase family. Like other growth factor receptors, upon ligand binding VEGF receptor 2 dimerises and is autophosphorylated on multiple tyrosine residues.

Angiogenesis, Cancer, Cancer Metabolism, Cardiovascular, Growth Factors, Growth Factors/Hormones, Hematopoietic Progenitors, Host Virus Interaction, Interspecies Interaction, Invasion/Microenvironment, Metabolism, Metabolism Processes, Microbiology, Oncoproteins, Oncoproteins/Suppressors, Pathways And Processes, Protein Phosphorylation, Receptor Tyrosine Kinases, Response To Hypoxia, Signal Transduction, Stem Cells, Surface Molecules, Tyrosine Kinases