Native human integrin αVβ3 (CD51 / CD61) heterodimer, affinity-purified from human source tissue and supplied as a ready-to-use protein solution, 10 µg. In cation-supplemented buffer the heterodimer adopts its functional, cation-dependent conformation and binds the full panel of physiological RGD ligands (vitronectin, fibronectin, fibrinogen, osteopontin, thrombospondin, bone sialoprotein, MMP-2, LAP-TGFβ, tenascin) as well as cyclic RGD mimetics of the cilengitide class. αVβ3 — the “vitronectin receptor” — sits at the centre of tumour angiogenesis, osteoclast-mediated bone resorption, vascular smooth-muscle migration and wound-healing re-epithelialisation, and this preparation supplies it as a defined, soluble, isolated receptor for assays that must separate αVβ3-specific signal from mixed cell-based readouts. Companion integrins for selectivity panels: cat. 476 (αVβ5), cat. 638 (α5β1) and cat. 126 (α1β1).
SPECIFICATIONS
Catalogue number: 357 | Product: Integrin αVβ3 (human)
Source: human tissue; affinity-purified native heterodimer
Composition: αV (CD51) / β3 (CD61) heterodimer
Format: protein solution, ready for direct use | Package size: 10 µg
Cation dependence: activity requires divalent cations; typical assay buffer 50 mM Tris-HCl pH 7.4, 150 mM NaCl, 2 mM MgCl2, 1 mM MnCl2
Key ligands: vitronectin, fibronectin, fibrinogen, osteopontin, thrombospondin, bone sialoprotein, MMP-2, LAP-TGFβ, tenascin; cyclic RGD peptides (cilengitide / RGDfV class)
STORAGE
Supplied as a solution, ready for direct use; no reconstitution required.
Store at −20 °C or lower on receipt; aliquot before freezing.
Avoid repeated freeze-thaw cycles. Thaw on ice and dilute into cation-supplemented buffer immediately before use.
APPLICATIONS
- Quartz-crystal-microbalance (QCM) and surface-plasmon-resonance (SPR) binding studies — typical working concentration ~20 µg/mL in Tris / NaCl / Mg2+ / Mn2+ buffer flowed over RGD-functionalised sensor surfaces for label-free affinity and kinetic measurement.
- Drug-discovery screening of αVβ3 antagonists: cyclic RGD peptides, small-molecule RGD mimetics and antibody-based vitronectin-receptor inhibitors. Pair with cat. 476 for an αVβ3-vs-αVβ5 selectivity panel, and add cat. 638 for full RGD-integrin cross-reactivity profiling.
- Solid-phase (ELISA-format) receptor-binding assays: coat, block, then quantify binding of biotinylated RGD ligands, RGD-presenting peptides, anti-integrin antibodies or candidate inhibitors.
- Characterisation of photo-, redox- and pH-activatable RGD ligands: caged-RGD, photoswitchable-RGD and stimuli-responsive RGD-presenting surfaces and hydrogels.
- Reference receptor for vitronectin / fibronectin / fibrinogen binding studies where αVβ3 engagement must be demonstrated specifically.
- Immunogen for raising anti-αVβ3 (anti-CD51 / anti-CD61) antibodies and for epitope mapping of heterodimer-specific monoclonals.
APPLICATION HIGHLIGHTS — HIGH-VALUE RESEARCH NICHES
- Tumour angiogenesis: the drug-targeted endothelial RGD receptor behind the cilengitide class of antagonists.
- Osteoclast biology and anti-resorptive drug discovery: the original αVβ3 therapeutic target.
- Biomaterials and tissue engineering: defined-receptor readout for RGD-functionalised, photopatterned and gradient surfaces.
- Label-free biosensing: benchmark receptor input for QCM and SPR method development.
- Integrin-selectivity profiling across the RGD-binding integrin family.
REFERENCES
Wirkner M., Weis S., San Miguel V., Álvarez M., Gropeanu R.A., Salierno M., Sartoris A., Unger R.E., Kirkpatrick C.J., del Campo A. (2011) Photoactivatable caged cyclic RGD peptide for triggering integrin binding and cell adhesion to surfaces. ChemBioChem 12(17): 2623–2629. doi:10.1002/cbic.201100437.
