Background：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
仕様
Synonyms：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
Host：Rabbit
Reactivity：Human
Applications：IHC,ELISA
Concentration：0.6mg/mL
Immunogen：Recombinant protein of human SERPINB8
Purification Method：Affinity purification
Clonality：Polyclonal
Conjugation：Unconjugated
Buffer：PBS with 0.05％ sodium azide, 50％ glycerol, PH7.3
