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]).1) Rose, J.E., et al. Mol. Med. 16 (7-8), 247-253 (2010) :
Immunogen
This SERPINB8 antibody is generated from rabbits immunized with a KLH conjugated synthetic peptide between 274-301 amino acids from the C-terminal region of human SERPINB8.
Western blot analysis in Jurkat cell line lysates (35ug/lane).
Application Notes
For WB starting dilution is: 1:1000
Additional Information
Form
Liquid
Storage Instructions
Store at 4˚C for three months and -20˚C, stable for up to one year. As with all antibodies care should be taken to avoid repeated freeze thaw cycles. Antibodies should not be exposed to prolonged high temperatures.