KDR (Y1175) Antibody
Affinity Purified Rabbit Polyclonal Antibody (Pab)
- SPECIFICATION
- CITATIONS
- PROTOCOLS
- BACKGROUND
Application ![]()
| FC, WB, E |
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Primary Accession | P35968 |
Reactivity | Human, Mouse |
Host | Rabbit |
Clonality | Polyclonal |
Isotype | Rabbit IgG |
Calculated MW | 151527 Da |
Antigen Region | 1153-1182 aa |
Gene ID | 3791 |
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Other Names | Vascular endothelial growth factor receptor 2, VEGFR-2, Fetal liver kinase 1, FLK-1, Kinase insert domain receptor, KDR, Protein-tyrosine kinase receptor flk-1, CD309, KDR, FLK1, VEGFR2 |
Target/Specificity | This KDR antibody is generated from rabbits immunized with a KLH conjugated synthetic peptide between 1153-1182 amino acids from human KDR. |
Dilution | WB~~1:1000 FC~~1:10~50 |
Format | Purified polyclonal antibody supplied in PBS with 0.09% (W/V) sodium azide. This antibody is purified through a protein A column, followed by peptide affinity purification. |
Storage | Maintain refrigerated at 2-8°C for up to 2 weeks. For long term storage store at -20°C in small aliquots to prevent freeze-thaw cycles. |
Precautions | KDR (Y1175) Antibody is for research use only and not for use in diagnostic or therapeutic procedures. |
Name | KDR (HGNC:6307) |
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Synonyms | FLK1, VEGFR2 |
Function | 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. |
Cellular Location | Cell junction. Endoplasmic reticulum. Cell membrane. Note=Localized with RAP1A at cell-cell junctions (By similarity). Colocalizes with ERN1 and XBP1 in the endoplasmic reticulum in endothelial cells in a vascular endothelial growth factor (VEGF)-dependent manner (PubMed:23529610). {ECO:0000250, ECO:0000269|PubMed:23529610} [Isoform 2]: Secreted. |
Tissue Location | Detected in cornea (at protein level). Widely expressed. |

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Provided below are standard protocols that you may find useful for product applications.
Background
KDR is a major growth factor for endothelial cells. This protein encodes one of the two receptors of the KDR. This receptor, known as kinase insert domain receptor, is a type III receptor tyrosine kinase. It functions as the main mediator of VEGF-induced endothelial proliferation, survival, migration, tubular morphogenesis and sprouting. The signalling and trafficking of this receptor are regulated by multiple factors, including Rab GTPase, P2Y purine nucleotide receptor, integrin alphaVbeta3, T-cell protein tyrosine phosphatase, etc..
References
Huang, D., et al. Cancer Res. 70(3):1053-1062(2010)
Sentilhes, L., et al. J. Neuropathol. Exp. Neurol. 69(2):111-128(2010)
Lamalice, L., et al. J. Biol. Chem. 281(45):34009-34020(2006)
Meyer, R.D., et al. J. Biol. Chem. 277(30):27081-27087(2002)

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