Integrin alphaV, beta3, Recombinant, Human

Integrin alphaVbeta3 together with aIIb-beta3, constitutes the only known beta3 Integrins (1-3). The non-covalent heterodimer of 170kD alphaV/CD51 and 93kD beta3/CD61 subunits show wide expression, notably by endothelial cells and osteoclasts (2-4). Each subunit has a transmembrane sequence and a short cytoplasmic tail connected to the cytoskeleton. Active cell surface alphaVbeta3 adheres to matrix proteins including vitronectin, fibronectin, fibrinogen and thrombospondin (2, 3). The ligand binding site of alphaVbeta3 is in the N-terminal head region, formed by interaction of the beta3 vWFA domain with the alphaV beta-propeller structure (4). The alphaV subunit contributes a thigh and a calf region, while the beta3 subunit contains a PSI domain and four cysteine-rich I-EGF folds. The alphaV subunit domains termed thigh, calf-1 and calf-2 generate a пїЅkneeпїЅ region that is bent when the alphaVbeta3 is in its constitutively inactive state. Activation, either by пїЅinside outпїЅ signaling or by Mg2+ or Mn2+ binding, extends the Integrin to expose its ligand binding site (1, 4). Two splice variants of beta3 (b and c) diverge over the last 21 amino acids (aa) and lack cytoplasmic phosphorylation sites (5, 6). Another beta3 splice variant diverges after the vWFA domain, producing a soluble 60kD form in platelets and endothelial cells (7). Alpha Vbeta3 is essential for the maturation of osteoclasts and their binding and resorption of bone; it also, however, promotes their apoptosis (8, 9). M-CSF R and alphaVbeta3 share signaling pathways during osteoclastogenesis, and deletion of either molecule causes osteopetrosis (8, 9). Also cell entry of several viruses is mediated by alphaVbeta3 (4,10). The 962aa human alphaV ECD11 shares 92-95% aa sequence identity with mouse, rat and bovine alphaV while the 685 aa human beta3 ECD12 shares 95% aa identity with equine and canine, and 89-92% aa identity with mouse, rat and porcine beta3.\n\nThe extracellular domain of human Integrin alphaV subunit (Phe31-Val992; Accession # NP_002201) and the extracellular domain of beta3 subunit (Gly27-Asp718; Accession # AAA52589) were co-expressed in Chinese Hamster Ovary cells.\n\nActivity: \nMeasured by its ability in functional ELISA. Immobilized recombinant human Vitronectin at 1ug/ml can bind rhIntegrin aVb3 with apparent Kd <10nM. \n\nApplications: \nSuitable for use in ELISA and Western Blot. Band observed at 110-155kD under reducing conditions. Other applications not tested.\n\nRecommended Dilutions:\nOptimal dilutions to be determined by the researcher.\n\nStorage and Stability:\nLyophilized powder may be stored at -20 degrees C. Stable for 12 months at -20 degrees C. Reconstitute with sterile PBS. Aliquot to avoid repeated freezing and thawing. Store at -20 degrees C. For maximum recovery of product, centrifuge the original vial after thawing and prior to removing the cap. Further dilutions can be made in assay buffer.

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SPECIFICATIONS

Catalog Number

I7661-37E9

Size

50ug

Applications

ELISA, WB

Reactivities

Hum

Form

Supplied as a lyophilized powder from 50mM Tris, pH 7.4, 150mM sodium chloride, 0.5mM calcium chloride. Reconstitute with 500ul sterile PBS.

Purity

(same/more than)90%, as determined by SDS-PAGE under reducing conditions and visualized by silver stain. Endotoxin: (same/less than) 1EU per ug.

References

1. Hynes, R.O., Cell 110: 673-687 (2002). 2. Serini, G., et al., Exp. Cell Res. 312: 651-658 (2006). 3. Ross, F.P. and Teitelbaum, S.L., Immunol. Rev. 208: 88-105 (2005). 4. Xiong, J., et al., Science 294: 339-345 (2001). 5. Kumar, C.S., et al., J. Biol. Chem. 272: 16,390-16,397 (1987). 6. van Kuppevelt, H., et al., Proc. Natl. Acad. Sci. USA 86: 5415-5418 (1989). 7. Djaffar, I., et al., Biochem. J. 300: 67-74 (1994). 8. McHugh, K.P., et al., J. Clin. Invest. 105: 433-440 (2000). 9. Faccio, R., et al., J. Clin. Invest. 111: 749-758 (2003). 10. Chu, J.J., and Ng, M., J. Biol. Chem. 279: 54,533-54,541 (2004). 11. Suzuki, S., et al., J. Biol. Chem. 262: 14,060-14,085 (1987). 12. Fitzgerald, L.A., et al., J. Biol. Chem. 262: 3936-3939 (1987).