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Pim-2 Antibody #4723

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Inquiry Info. # 4723

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    Supporting Data

    REACTIVITY H
    SENSITIVITY Endogenous
    MW (kDa) 40, 38, 34
    SOURCE Rabbit
    Application Key:
    • WB-Western Blotting 
    Species Cross-Reactivity Key:
    • H-Human 

    Product Information

    Product Usage Information

    Application Dilution
    Western Blotting 1:1000

    Storage

    Supplied in 10 mM sodium HEPES (pH 7.5), 150 mM NaCl, 100 µg/ml BSA and 50% glycerol. Store at –20°C. Do not aliquot the antibody.

    Protocol

    Specificity / Sensitivity

    Pim-2 Antibody detects endogenous levels of total Pim-2 protein. The antibody does not cross-react with other Pim family members.

    Species Reactivity:

    Human

    The antigen sequence used to produce this antibody shares 100% sequence homology with the species listed here, but reactivity has not been tested or confirmed to work by CST. Use of this product with these species is not covered under our Product Performance Guarantee.

    Species predicted to react based on 100% sequence homology:

    Monkey

    Source / Purification

    Polyclonal antibodies are produced by immunizing animals with a synthetic peptide corresponding to residues surrounding Gln287 of human Pim-2. Antibodies were purified by peptide affinity chromatography.

    Background

    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 has also been observed in certain cancers (17,18).
    1. Mikkers, H. et al. (2004) Mol Cell Biol 24, 6104-15.
    2. Selten, G. et al. (1986) Cell 46, 603-11.
    3. Meeker, T.C. et al. (1987) J Cell Biochem 35, 105-12.
    4. Dautry, F. et al. (1988) J Biol Chem 263, 17615-20.
    5. Möröy, T. et al. (1993) Proc Natl Acad Sci USA 90, 10734-8.
    6. Lilly, M. and Kraft, A. (1997) Cancer Res 57, 5348-55.
    7. Leverson, J.D. et al. (1998) Mol Cell 2, 417-25.
    8. Winn, L.M. et al. (2003) Cell Cycle 2, 258-62.
    9. Pasqualucci, L. et al. (2001) Nature 412, 341-6.
    10. Kim, O. et al. (2004) Oncogene 23, 1838-44.
    11. Aho, T.L. et al. (2004) FEBS Lett 571, 43-9.
    12. Yan, B. et al. (2003) J Biol Chem 278, 45358-67.
    13. van der Lugt, N.M. et al. (1995) EMBO J. 14, 2536-2544.
    14. Breuer, M.L. et al. (1989) EMBO J. 8, 743-748.
    15. Fox, C.J. et al. (2003) Genes Dev. 17, 1841-1854.
    16. White, E. (2003) Genes Dev. 17, 1813-1816.
    17. Cohen, A.M. et al. (2004) Leuk. Lymphoma 45, 951-955.
    18. Dai, H. et al. (2005) Prostate 65, 276-286.
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