Description
RP2-Serpin-B10 is a polyclonal antibody made to the serine proteinase inhibitor PI-10. The antibody is made to a synthetic peptide based on the reactive center loop area of human serpin-B10. The antibody has been peptide-affinity purified, concentrated to 1.0 mg/ml, with the addition of 0.05% sodium azide as preservative and 50% glycerol as cryoprotectant.
Use
Serpin-B10, also known as Bomapin, Bone Marrow-Associated Serpin, PI-10, Proteinase Inhibitor-10, is a serine proteinase inhibitor of the ovalbumin-like B clade of serpins. Serpin-B10 was first discovered in human bone marrow in a search for serpins similar to serpin-B6. Serpin-B10 was identified in lymphocytes, and was elevated in chronic myeloid leukemia and chronic myelomonocytic leukemia cells. The monocytic cell lines THP-1 and AML-193 also showed elevated serpin-B10 expression. Serpin-B10 is similar to PI-9, also found in blood marrow cells, but serpin-B10 seems to be more restricted in distribution. Serpin-B10 has been shown to inhibit thrombin and trypsin in-vitro, and to inhibit tumor necrosis factor-(alpha) induced cell death. The mode of action seems similar to serpin-B9, which prevents cell-mediated cell death by inhibiting granzyme-B, although serpin-B10 has not been implicated in granzyme-B inhibition. Most leukemia cells and many tumor cells produce PI-9, leading to speculation that PI-9 may help protect tumor cells from destruction by NK and CTL cells, and this may be true of serpin-B10 as well. Like serpin-B6 and serpin-B8, serpin-B10 lacks a signal sequence, and is found mainly in the cytoplasm and nucleus, although it can be detected outside of cells and in serum. Most of the serpins (SERine Proteinase Inhibitors) are serine proteinase inhibitors; although not all serine proteinase inhibitors are serpins, and visa versa. The overall structural shape of the B clade of serpins most resembles ovalbumin, which is not considered to be a serine proteinase inhibitor. The serpins share a reactive center loop motif: a substrate bait loop which, when cleaved, confers a remarkable molecular shift in the serpin molecule, and traps the enzyme. This mousetrap method works because the uncleaved serpin molecule is in tension, and cleaving the loop allows a more energetically favorable state to exist. The cleavage site in serpin-B10 is Arg362-Ile362 of the 397 amino acid sequence. The original sequence described was 397 amino acids in length, with predicted mass of 42.4 kDa and pI of 5.74. A recommended starting concentration for Western blots is 1:1,000 when using colorimetric substrates such as BCIP/NBT, and 1:5,000 for chemiluminescent substrates. Higher concentrations of antibody may be needed for samples from more distantly related species FOR RESEARCH USE ONLY; NOT FOR USE IN HUMANS.
Storage
The undiluted antibody solution is stable for approximately 12 at -20C.
