Product Pathways - Lymphocyte Signaling
Pim-2 (D1D2) Rabbit mAb #4730
|4730S||100 µl (10 western blots)||---||In Stock||---|
|4730||carrier free and custom formulation / quantity||email request|
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|W||1:1000||Human||Endogenous||40, 38, 34||Rabbit|
Species cross-reactivity is determined by western blot.
Applications Key: W=Western Blotting, IP=Immunoprecipitation
Specificity / Sensitivity
Pim-2 (D1D2) Rabbit mAb detects endogenous levels of total Pim-2 protein. The antibody does not cross-react with other Pim family members.
Source / Purification
Monoclonal antibody is produced by immunizing animals with a synthetic peptide corresponding to residues surrounding Cys266 of human Pim-2.
Western blot analysis of extracts from K-562, Raji and KARPAS-620 cell lines using Pim-2 (D1D2) Rabbit mAb.
Pim proteins (Pim-1, Pim-2 and Pim-3) are oncogene-encoded serine/threonine kinases (1). Pim-1, a serine/threonine kinase highly expressed in hematopoietic cells, plays a critical role in the transduction of mitogenic signals and is rapidly induced by a variety of growth factors and cytokines (1-4). Pim-1 cooperates with c-Myc in lymphoid cell transformation and protects cells from growth factor withdrawal and genotoxic stress-induced apoptosis (5,6). Pim-1 also enhances the transcriptional activity of c-Myb through direct phosphorylation within the c-Myb DNA binding domain as well as phosphorylation of the transcriptional coactivator p100 (7,8). Hypermutations of the Pim-1 gene are found in B-cell diffuse large cell lymphomas (9). Phosphorylation of Pim-1 at Tyr218 by Etk occurs following IL-6 stimulation and correlates with an increase in Pim-1 activity (10). Various Pim substrates have been identified; Bad is phosphorylated by both Pim-1 and Pim-2 at Ser112 and this phosphorylation reverses Bad-induced cell apoptosis (11,12).
Pim-2 is highly homologous to Pim-1 with similar oncogenic functions (13,14). Three isoforms of Pim-2 can be generated from alternative start sites which run at 34, 38, and 40 kDa (13). Pim-2 leads to resistance to a variety of apoptotic stimuli and its expression is negatively regulated by growth factor withdrawal (15,16). Increased levels of Pim-2 have also been observed in certain cancers (17,18).
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- Meeker, T.C. et al. (1987) J Cell Biochem 35, 105-12.
- Dautry, F. et al. (1988) J Biol Chem 263, 17615-20.
- Möröy, T. et al. (1993) Proc Natl Acad Sci USA 90, 10734-8.
- Lilly, M. and Kraft, A. (1997) Cancer Res 57, 5348-55.
- Leverson, J.D. et al. (1998) Mol Cell 2, 417-25.
- Winn, L.M. et al. (2003) Cell Cycle 2, 258-62.
- Pasqualucci, L. et al. (2001) Nature 412, 341-6.
- Kim, O. et al. (2004) Oncogene 23, 1838-44.
- Aho, T.L. et al. (2004) FEBS Lett 571, 43-9.
- Yan, B. et al. (2003) J Biol Chem 278, 45358-67.
- van der Lugt, N.M. et al. (1995) EMBO J 14, 2536-44.
- Breuer, M.L. et al. (1989) EMBO J 8, 743-8.
- Fox, C.J. et al. (2003) Genes Dev 17, 1841-54.
- White, E. (2003) Genes Dev 17, 1813-6.
- Cohen, A.M. et al. (2004) Leuk Lymphoma 45, 951-5.
- Dai, H. et al. (2005) Prostate 65, 276-86.
- Gómez-Abad, C. et al. (2011) Blood 118, 5517-27. Applications: Western Blotting, IHC-P (paraffin).
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