Anti-Integrin αVβ3 Antibody, clone LM609, Alexa Fluor^™ 555 Conjugate

Evaluated by Immunocytochemistry in HepG2 cells.

Immunocytochemistry Analysis: A 1:100 dilution of this antibody detected Integrin αVβ3 in HepG2 cells.

Anti-Integrin αVβ3 Antibody, clone LM609, Alexa Fluor^™ 555 Conjugate is an antibody against Integrin αVβ3 for use in Immunocytochemistry.

Immunocytochemistry Analysis: A 1:100 dilution from a representative lot detected Integrin αVβ3 in HeLa cells.
The unconjugated antibody (Cat. No. MAB1976) is shown to be suitable also for functional assay, flow cytometry, immunofluorescence, immunohistochemistry, and immunoprecipitation applications.

Reacts with the vitronectin receptor alphaVbeta3 complex, an RGD-directed adhesion receptor. LM609 has been demonstrated to block adhesion of a human melanoma cell line (M21) to vitronectin, fibrinogen and von Willebrand factor, as well as to a synthetic RGD containing peptide (Cheresh, D.A., and Spiro R.C. (1987). J Biol Chem. 262(36):17703-11; Cheresh, D.A. (1987). Proc. Natl. Acad. Sci. U.S.A. 84(18):6471-6475). In chick chorioallentoic membranes, LM609 was shown to block angiogenesis induced by bFGF and TNFalpha but had no effect on pre-existing vessels (Brooks, P.C., et al. (1994). Science. 264(5158):569-571). While LM609 does block cell attachment to RGD containing ligands, it does not interact directly with the RGD binding site. Instead, LM609 appears to be an allosteric inhibitor of integrin alphaVbeta3, which binds to a conformational epitope resulting from the post-translational association of the alphaV and beta3 subunits.

Integrin alpha-V (CD51, Vitronectin receptor subunit alpha; UniProt P06756) and Integrin beta-3 (CD61, GPIIIa, Platelet membrane glycoprotein IIIa; UniProt P05106) are encoded by the ITGAV (MSK8, VNRA; Gene ID 3685) and ITGB3 (GP3A; Gene ID 3690) gene, respectively, in human. The integrin family of cell adhesion receptors consists of at least 16 membrane-associated heterodimers, composed of an alpha and a beta subunit that associate in a non-covalent manner. The structure and functional diversity of the integrin family are based upon the pairing abilities of the individual alpha and beta subunits. Key to these molecular interactions between the integrin receptors and their respective ligands is the recognition of the Arg-Gly-Asp (RGD) sequence, known to be present in the extracellular matrix components fibronectin, vitronectin, collagen, fibrinogen, and von Willebrand factor. The involvement of integrins in vascular proliferation, adhesion, and wound repair has been well documented. The adhesion receptor, integrin alphaVbeta3, appears to be selectively expressed on growing blood vessels and has been identified as a marker of angiogenic vascular tissue. Due to its involvement in angiogenesis, integrin alphaVbeta3 is among of the most studied integrin receptors.

~116 kDa observed

Purified adhesion receptor from the human melanoma cell line M21 (Cheresh, D.A., and Spiro R.C. (1987). J. Biol. Chem. 262(36):17703-11).

Concentration: Please refer to lot specific datasheet.

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