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]

CAP 2;
CAP-2;
CAP2;
Cytoplasmic antiproteinase 2;
OTTHUMP00000067000;
OTTHUMP00000067001;
Peptidase inhibitor 8;
PI 8;
PI-8;
PI8;
Protease inhibitor 8 (ovalbumin type);
Serine (or cysteine) proteinase inhibitor clade B (ovalbumin) member 8;
Serpin B8;
Serpin peptidase inhibitor clade B (ovalbumin) member 8;
Serpinb8;
SPB8_HUMAN.

Human,Mouse,Rat,Dog,Cow,Horse,Rabbit,GuineaPig,Cat

WB

WB 1:500-2000

43kD

5271

P50452

https://www.uniprot.org/uniprotkb/P50452

Cytoplasm.

KLH conjugated synthetic peptide derived from human SerpinB8

Rabbit

Polyclonal

IgG

affinity purified by Protein A

Liquid

0.01M TBS (pH7.4) with 1% BSA, 0.02% Proclin300 and 50% Glycerol.

Shipped at 4℃. Store at -20℃ for one year. Avoid repeated freeze/thaw cycles.