|Calculated MW||61.0 kDa|
|Other Names||PIM, Serine/threonine-protein kinase Pim-2|
|Source||Baculovirus (Sf9 insect cells)|
|Storage||-80°C; Recombinant protein in storage buffer (50 mM Tris-HCl, pH 7.5, 150 mM NaCl, 0.25 mM DTT, 0.1 mM EGTA, 0.1 mM EDTA, 0.1 mM PMSF, 25% glycerol).|
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Provided below are standard protocols that you may find useful for product applications.
Baytel et al. identified a deduced 334-amino acid sequence of the clone, which showed 90% identity with the mouse Pim2 protein. Like mouse Pim2, the human protein appears to be a serine threonine kinase. Northern blot analysis detected 2 PIM2 transcripts in all tissues tested, but most abundantly in hematopoietic tissues, spleen, thymus, and peripheral blood leukocytes, as well as in testis, small intestine, and colon. It was also highly expressed in human leukemic and lymphoma cell lines and a colorectal adenocarcinoma cell line. The results suggested a role for PIM2 in proliferating cells as well as during meiosis (1). Yan et al investigated potential functions for the pim family of kinases in factor-dependent murine hematopoietic cells and indicate that pim-2 functions similarly to pim-1 as a pro-survival kinase and suggest that BAD is a legitimate PIM-2 substrate (2). Hammerman et al concluded that the transcriptional induction of Pim-2 initiated a novel NF-kappaB activation pathway that regulates cell survival (3).
Baytel D.,et al.Biochim. Biophys. Acta 1442:274-285(1998).
Ota T.,et al.Nat. Genet. 36:40-45(2004).
Ishida N.,et al.Submitted (MAY-2000) to the EMBL/GenBank/DDBJ databases.
Ross M.T.,et al.Nature 434:325-337(2005).
Leong W.F.,et al.Cell. Microbiol. 8:565-580(2006).
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