Pim-1 Antibody

2907:

Western Blotting

Pim-1 Antibody recognizes endogenous levels of total Pim-1 protein. This antibody does not cross-react with other Pim proteins.

Polyclonal antibodies are produced by immunizing animals with a synthetic peptide corresponding to residues at the carboxy terminus of human Pim-1. Antibodies were purified by protein A and peptide affinity chromatography.

Western Blotting

Western blot analysis of extracts from K562, Raji and NK-92 cell lines using Pim-1 Antibody.

Western Blotting

Western blot analysis of recombinant Pim-1, -2 and -3 (5 ng) using Pim-1 Antibody.

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).

The corresponding pim-1 gene encodes a pair of proteins through use of different translation initiation sites. Both larger 44 kDa (Pim-1L) and smaller 33 kDa (Pim-1S) proteins are active kinases, but differ in stability (13).

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. Saris, C.J. et al. (1991) EMBO J 10, 655-64.

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• 7071 Phototope^® -HRP Western Blot Detection System, Anti-rabbit IgG, HRP-linked Antibody
• 7074 Anti-rabbit IgG, HRP-linked Antibody
• 7720 Prestained Protein Marker, Broad Range (Premixed Format)
• 7727 Biotinylated Protein Ladder Detection Pack
• 7003 20X LumiGLO^® Reagent and 20X Peroxide

For Research Use Only. Not For Use In Diagnostic Procedures.