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]).
Target |
SERPINB8 |
Reactivity |
Human |
Host |
Rabbit |
Clonality |
Polyclonal |
Tested Applications |
WB |
Recommended dilutions |
Optimal dilutions/concentrations should be determined by the end user. |
Immunogen |
KLH-conjugated synthetic peptide between 274-301 amino acids from the C-terminal region of human SERPINB8. |
Purification |
Purified through a protein A column, followed by peptide affinity purification. |
Isotype |
IgG |
Conjugation |
Unconjugated |
Storage |
Aliquot and store at -20 °C. Avoid repeated freeze/thaw cycles. |
Swiss Prot |
P50452
|
Buffer |
PBS containing 0.09% sodium azide. |
UNSPSC Code |
12352203 |
Availability |
Shipped within 5-10 working days. |
Note |
This product is for research use only. |