Integrin alphaV beta5 was purified from human placenta by affinity chromatography using immobilized monoclonal antibodies to alphaV beta5 integrin. Two bands are identified with silver stain, corresponding to alphaV (145kDa) and beta5 (90kDa) subunits under nonreducing conditions. Product was tested and found negative for HIV, HBsAg, syphilis, and hepatitis. Integrin alphaV beta5 interacts with vitronectin in ELISA.
Application
Electrophoresis
Immunoblotting (nonreduced conditions)
Ligand Binding studies.
Optimal working dilutions must be determined by end user.
Physical form
Purified protein in 20 mM Tris-HCl, pH 7.5, 150 mM NaCl, 2 mM MgCl, 0.2% Triton X-100, with no preservatives.
Preparation Note
Maintain at -70°C in undiluted aliquots. Avoid repeated freeze/ thaw cycles.
Analysis Note
Two main protein bands corresponding to aV (145 kD) and β5 (90 kD) subunits are seen in silver stained gel under non-reduced conditions.
Legal Information
CHEMICON is a registered trademark of Merck KGaA, Darmstadt, Germany
Disclaimer
Unless otherwise stated in our catalog or other company documentation accompanying the product(s), our products are intended for research use only and are not to be used for any other purpose, which includes but is not limited to, unauthorized commercial uses, in vitro diagnostic uses, ex vivo or in vivo therapeutic uses or any type of consumption or application to humans or animals.
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Caulollins from Caulobacter crescentus, a pair of partially unstructured proteins of betagamma-crystallin superfamily, gain structure upon binding calcium.
The Journal of cell biology, 111(5 Pt 1), 2159-2170 (1990-11-01)
A membrane glycoprotein complex was isolated and purified from human smooth muscle by detergent solubilization and affinity chromatography on collagen-Sepharose. The complex was identified as VLA-1 integrin and consisted of two subunits of 195 and 130 kD in SDS-PAGE. Liposomes
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