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
Immunogen Information
Immunogen
Recombinant protein of human SERPINB8
Swissprot
P50452
Synonyms
CAP 2CAP-2CAP2Cytoplasmic antiproteinase 2OTTHUMP00000067000OTTHUMP00000067001Peptidase inhibitor 8PI 8PI-8PI8Protease inhibitor 8 (ovalbumin type)Serine (or cysteine) proteinase inhibitor clade B (ovalbumin) member 8Serpin B8Serpin peptidase
Gene Accession
BC034528
Applications
Reactivity
Human
Tested Applications
IHC,ELISA
Conjugation
Unconjugated
Dilution
IHC 1:30-1:150
Concentration
0.6 mg/mL
Storage Buffer
PBS with 0.05% sodium azide and 50% glycerol, PH7.4