产品描述：

background: May modulates insulin action conceivably only in the presence of its yet undefined target proteases in white adipose tissues.

Serpins are the largest and most diverse family of protease inhibitors. Most serpins control proteolytic cascades, certain

serpins do not inhibit enzymes, but instead perform diverse functions such as storage (ovalbumin, in egg white), hormone

carriage proteins (thyroxine-binding globulin, cortisol-binding globulin) and tumor suppressor genes (maspin). Most inhibitory

serpins target chymotrypsin-like serine proteases. These enzymes are defined by the presence of a nucleophilic serine residue

in their catalytic site. Some serpins inhibit other classes of protease. A number of such serpins have been shown to target

cysteine proteases. These enzymes differ from serine proteases in that they are defined by the presence of a nucleophilic

cysteine residue, rather than a serine residue, in their catalytic site.

SerpinA12, also known as OL-64, Visceral adipose tissue-derived serine protease inhibitor, Vaspin, Visceral adipose-specific

serpin and SERPINA12, is a secreted protein which belongs to the serpin family. SerpinA12 / Vaspin is expressed in visceral

adipose tissues. It may modulates insulin action conceivably only in the presence of its yet undefined target proteases in white

adipose tissues. SerpinA12 / Vaspin may be the compensatory molecule in the pathogenesis of metabolic syndrome and

SerpinA12 / Vaspin recombinant protein or vaspin-mimicking agents such as vaspin analogs, antibodies or small molecule

agents may be the link to drug discovery and development.