Human Integrin α5β1 Protein, Triton X-100 Formulation

Nonreduced SDS-PAGE of 15 mg on 5-15% polyacrylamide slab gel and staining with Coomassie shows only two main bands at 110 kDa (beta1 subunit) and 155 kDa (alpha5 subunit).A weak band at 205 kDa is due to dimerization of the b1 subunit (Belkin et al., 1996)

Electrophoresis and Immunoblotting control. Due to the existance of reduction sensitive sites within the integrin subunits, it is recommended that gels be run under non-reducing conditions for best results. Under non-reducing conditions, the alpha5 subunit will migrate at 155 kDa while the beta1 subunit will migrate at 110 kDa.

Function: Liposomes containing Integrin alpha5/beta1 adhere to surfaces coated with fibronectin in an RGD-dependent fashion.

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Integrin a5/b1 purified from smooth muscle and placental tissue under nondenaturing conditions by affinity chromatography on fibronectin-Sepharose (Belkin, 1990).



Two main protein bands corresponding to a5 (145 kD) and beta1 (120 kD) subunits are seen in silver stained 7.5%

polyacrylamide gels under nonreduced conditions. Minor protein band at the 210 kD corresponding to beta1 subunit disulfide dimmer, which is formed during electrophoresis and disappears after reduction.

Product Source: Human smooth muscle and placental tissue.

Purified protein in 20 mM Tris-HCl, pH 7.5, 150 mM NaCl, 2 mM MgCl2 containing 0.2% Triton X-100. No preservatives. Source material for the enclosed purified human proteins, Integrin alpha5beta1, has been tested for antibodies to HIV, HCV, and HbsAg and found to be negative by an approved test.

Maintain at -70°C in undiluted aliquots. Avoid repeated freeze/thaw cycles.

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