Recombinant Human Vaspin/SerpinA12 Protein (His Tag) (Active)

Cat. No : CDRP-00768

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Target Information
Target Name	Vaspin/SerpinA12
Synonyms	Serpin A12; OL-64; Vaspin; Visceral Adipose-Specific Serpin; SERPINA12
UniProt ID	P43652
Accession	NP_776249.1

Product Details
Expression Host	HEK293 Cells
Species	Human
Tag	C-His
Molar Mass	46.5 kDa
Sequence	Met 1-Thr 661

Background
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 secretedprotein which belongs to theserpin 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.

Background

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 secretedprotein which belongs to theserpin 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.

Properties
Purity	>95% as determined by reducing SDS-PAGE.
Formulation	Lyophilized from sterile PBS, pH7.4.
Reconstitution	Please refer to the printed manual for detailed information.
Shipping	This product is provided as lyophilized powder which is shipped with ice packs.
Storage	Generally, lyophilized proteins are stable for up to 12 months when stored at -20 to -80 °C. Reconstituted protein solution can be stored at 4-8 °C for 2-7 days. Aliquots of reconstituted samples are stable at < -20 °C for 3 months.

! For research use only. Not intended for any clinical use.