PRODUCT NO 01-INT-5

PACKAGE SIZE 50 µg

DESCRIPTION

Triton X-100. No preservatives.

Human placenta.

Integrin aVß3 was purified from human placenta by affinity chromatography using

immobilized monoclonal antibodies to aVß3 integrin. A tissue detergent extract, which was

applied to the column. 7.5 % SDS-PAGE by the method of Laemmli gives two major protein

bands, corresponding to aV subunit (145 kDa) and ß3 subunit (92 kDa) when visualized by

silver stain (2-2.5 µg protein/lane nonreduced). A minor protein band (170 kDa) corresponds

to the ß3 dimer, similar to an occurrence of the ß1 dimer upon purification of ß1 integrins. In

some cases a ß3 trimer is visible at 260 kDa. After reduction, with protein quantities of

1.5-4 µg protein/lane, three major protein bands are apparent, corresponding to ß3 integrin

subunit (110 kDa), heavy aV chain (125 kDa) and light aV chain (25 kDa). A minor band at

200 kDa region is presumed to be the reduced ß3 dimer, consistent with previous

publications describing a 230 kDa ß1 reduced dimer for ß1 integrin purifications. Faint bands

at 80 kDa and 55 kDa correspond to minor degradation products of ß3. Two faint bands

identified at 210 and 220 kDa, which may correspond to the aV dimer. It is expected that this

preparation of aVß3 integrin will also interact with other aVß3 binding proteins in an RGDdependent

fashion.

Maintain at –70 °C in undiluted aliquots. Avoid repeated freeze/ thaw cycles. Source material

for the enclosed purified human proteins, Integrin aVß3, a5ß1 and a1ß1, has been tested for

antibodies to HIV, and for HCV , and HbsAg and found to be negative by an approved test.

Electrophoresis and Immunoblotting control. Also useful for in vitro binding experiments

with metalloproteinase MMP-2. This format of aVß3 is appropriate for functional

evaluations.

Belkin, V.M., et al. J. Cell Biol. (1990) 111: 2159-2170

Belkin, V.M., et al. Biochem. and Mol. Biol. Inter. (1996) 40: 53-60.

Petela, R., et al. Methods Enzymol. (1987) 144: 475- 489.