SERPINA12 Polyclonal Antibody

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Product Description

In direct ELISAs and Western blots, less than 1% cross-reactivity with recombinant human (rh) Serpin A1, rhSerpin A3, rhSerpin F1, and recombinant mouse Serpin E1 is observed. Reconstitute at 0.2 mg/mL in sterile PBS. Vaspin is a newly described adipocytokine expressed predominantly in visceral white adipose tissues. Structure analysis of vaspin predicts the presence of three beta-sheets, nine alpha-helices, and one central loop, which are distinctive structural features of Serpin family members. The serpins are irreversible ("suicidal") serine-protease inhibitors, characterized by having more than 30% sequence homology with alpha1-antitrypsin and a conserved tertiary structure, which contains an exposed reactive center loop that acts as a pseudo-substrate for the target proteinase. Members of this family play an important role in a number of fundamental biological processes, including blood coagulation, fibrinolysis, complement activation, angiogenesis, inflammation, and tumor suppression. In humans, the serpins represent approximately 2% of total serum proteins, of which 70% is alpha1-antitrypsin. Vaspin exhibits 40.2% sequence identity with alpha1-antitrypsin. Yet, its protease inhibitory activity is still unknown. Vaspin mRNA expression in visceral fat is pos