SERPINA12. also known as vaspin (visceral adipose tissue-derived serpin), is a member of the serine protease inhibitor (serpin) family. It is primarily secreted by adipose tissue and has been implicated in metabolic regulation, insulin sensitivity, and inflammatory processes. SERPINA12 functions by inhibiting target proteases, particularly kallikrein 7 (KLK7), which may influence extracellular matrix remodeling and metabolic homeostasis. Its expression is associated with obesity, type 2 diabetes, and cardiovascular diseases, though its precise mechanisms remain under investigation.
Antibodies targeting SERPINA12 are critical tools for studying its physiological and pathological roles. They enable detection and quantification of SERPINA12 in tissues and biological fluids (e.g., serum) via techniques like ELISA, Western blotting, or immunohistochemistry. Such antibodies also facilitate research into its interaction with proteases and receptors, as well as its potential as a biomarker for metabolic disorders. Commercial SERPINA12 antibodies are typically raised in hosts like rabbits or mice, using recombinant protein fragments as immunogens. Validation includes specificity checks using knockout controls or blocking peptides.
Recent studies explore therapeutic applications, such as modulating SERPINA12 levels to improve insulin resistance or mitigate inflammation. However, cross-reactivity with other serpins and tissue-specific expression patterns require careful antibody characterization. Overall, SERPINA12 antibodies remain pivotal in unraveling its dual role as both a protective adipokine and a disease-associated mediator.