Pim-3 (D17C9) Rabbit mAb

4165:

Immunoprecipitation, Western Blotting

Pim-3 (D17C9) Rabbit mAb detects endogenous levels of total Pim-3 protein. It does not cross-react with other Pim family members.

Monoclonal antibody is produced by immunizing animals with a synthetic peptide corresponding to residues surrounding Ser275 of human Pim-3.

Western Blotting

Western blot analysis of extracts from COS-7 cells, untransfected () or transfected with a mouse Pim-3 construct (+), using Pim-3 (D17C9) Rabbit mAb.

Western Blotting

Western blot analysis of recombinant Pim-1, 2, and 3 using Pim-3 (D17C9) Rabbit mAb.

Western Blotting

Western blot analysis of extracts from various cell lines using Pim-3 (D17C9) 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-3, originally named Kid-1, was identified as a protein induced by depolarization in PC-12 cells (13). Like other family members, Pim-3 can phosphorylate Bad to inhibit Bad-mediated apoptosis (14). Aberrant expression of Pim-3 has been observed in a number of types of cancer, including liver, pancreas, colon and gastric cancer (14-17).

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. Feldman, J.D. et al. (1998) J Biol Chem 273, 16535-43.
14. Li, Y.Y. et al. (2006) Cancer Res 66, 6741-7.
15. Fujii, C. et al. (2005) Int J Cancer 114, 209-18.
16. Popivanova, B.K. et al. (2007) Cancer Sci 98, 321-8.
17. Zheng, H.C. et al. (2008) J Cancer Res Clin Oncol 134, 481-8.

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