SERPINB8 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 well-conserved a 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-8 (PI8; SERPINB8) 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]

SERPINB8: Belongs to the serpin family. Ov-serpin subfamily. 2 isoforms of the human protein are produced by alternative splicing

Protein type: Inhibitor

Chromosomal Location of Human Ortholog: 18q22.1

Cellular Component: cytosol; extracellular space

Molecular Function: protein binding; serine-type endopeptidase inhibitor activity