|Pim-1 (C93F2) Rabbit mAb 3247
|Pim-2 (D1D2) Rabbit mAb 4730
|40, 38, 34
|Pim-3 (D17C9) Rabbit mAb 4165
|H M R
|Phospho-Bad (Ser112) (40A9) Rabbit mAb 5284
|H M R Mk
|Bad (D24A9) Rabbit mAb 9239
|H M R Mk
|Anti-rabbit IgG, HRP-linked Antibody 7074
Monoclonal antibody is produced by immunizing animals with a synthetic peptide corresponding to residues surrounding Val160 of human Pim-1, Cys266 of human Pim-2, Ser275 of human Pim-3, Ser112 of mouse Bad, and Pro102 of human Bad, respectively.
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).
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