|Application ||IHC-P, IF, IP, IHC-Fr, Flo, Func|
|Dilution||Func, IHC-P (10 µg/ml),|
|Other Names||Integrin alpha-V, Vitronectin receptor subunit alpha, CD51, Integrin alpha-V heavy chain, Integrin alpha-V light chain, ITGAV, MSK8, VNRA|
|Target/Specificity||Recognizes human CD51.|
|Reconstitution & Storage||Long term: -20°C; Short term: +4°C; Avoid freeze-thaw cycles.|
|Precautions||ITGAV/Integrin Alpha V/CD51 Antibody is for research use only and not for use in diagnostic or therapeutic procedures.|
|Function||The alpha-V (ITGAV) integrins are receptors for vitronectin, cytotactin, fibronectin, fibrinogen, laminin, matrix metalloproteinase-2, osteopontin, osteomodulin, prothrombin, thrombospondin and vWF. They recognize the sequence R-G-D in a wide array of ligands. ITGAV:ITGB3 binds to fractalkine (CX3CL1) and may act as its coreceptor in CX3CR1-dependent fractalkine signaling (PubMed:23125415). ITGAV:ITGB3 binds to NRG1 (via EGF domain) and this binding is essential for NRG1-ERBB signaling (PubMed:20682778). ITGAV:ITGB3 binds to FGF1 and this binding is essential for FGF1 signaling (PubMed:18441324). ITGAV:ITGB3 binds to IGF1 and this binding is essential for IGF1 signaling (PubMed:19578119). ITGAV:ITGB3 binds to PLA2G2A via a site (site 2) which is distinct from the classical ligand-binding site (site 1) and this induces integrin conformational changes and enhanced ligand binding to site 1 (PubMed:18635536, PubMed:25398877). ITGAV:ITGB3 and ITGAV:ITGB6 act as a receptor for fibrillin-1 (FBN1) and mediate R-G-D-dependent cell adhesion to FBN1 (PubMed:12807887, PubMed:17158881).|
|Cellular Location||Membrane; Single-pass type I membrane protein. Cell junction, focal adhesion|
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Provided below are standard protocols that you may find useful for product applications.
The alpha-V (ITGAV) integrins are receptors for vitronectin, cytotactin, fibronectin, fibrinogen, laminin, matrix metalloproteinase-2, osteopontin, osteomodulin, prothrombin, thrombospondin and vWF. They recognize the sequence R-G-D in a wide array of ligands. In case of HIV-1 infection, the interaction with extracellular viral Tat protein seems to enhance angiogenesis in Kaposi's sarcoma lesions.
Suzuki S.,et al.J. Biol. Chem. 262:14080-14085(1987).
Sims M.A.,et al.Cytogenet. Cell Genet. 89:268-271(2000).
Ota T.,et al.Nat. Genet. 36:40-45(2004).
Totoki Y.,et al.Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
Hillier L.W.,et al.Nature 434:724-731(2005).
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