Serpin Peptidase Inhibitor, Clade B (Ovalbumin), Member 10 (SERPINB10) Antibody – Rabbit Polyclonal

The superfamily of high molecular weight serine proteinase inhibitors (serpins) regulate a diverse set of intracellular and extracellular processes such as complement activation, fibrinolysis, coagulation, cellular differentiation, tumor suppression, apoptosis, and cell migration. Serpins are characterized by a well-conserved tertiary structure that consists of 3 beta sheets and 8 or 9 alpha helices (Huber and Carrell, 1989 [PubMed 2690952]). A critical portion of the molecule, the reactive center loop connects beta sheets A and C. Protease inhibitor-10 (PI10; SERPINB10) is a member of the ov-serpin subfamily, which, relative to the archetypal serpin PI1 (MIM 107400), is characterized by a high degree of homology to chicken ovalbumin, lack of N- and C-terminal extensions, absence of a signal peptide, and a serine rather than an asparagine residue at the penultimate position (summary by Bartuski et al., 1997 [PubMed 9268635]).[supplied by OMIM, Jan 2010]

SERPINB10: Protease inhibitor that may play a role in the regulation of protease activities during hematopoiesis and apoptosis induced by TNF. May regulate protease activities in the cytoplasm and in the nucleus. Belongs to the serpin family. Ov-serpin subfamily.

Protein type: Inhibitor

Chromosomal Location of Human Ortholog: 18q21.3

Cellular Component: extracellular space; cytoplasm; nucleus

Molecular Function: serine-type endopeptidase inhibitor activity