Anti-PIM1 Antibody Picoband® Fluoro647 Conjugated

Proto-oncogene serine/threonine-protein kinase Pim-1 is an enzyme that in humans is encoded by the PIM1 gene. It is mapped to 6p21.2. Primarily expressed in spleen, thymus, bone marrow, prostate, oral epithelial, hippocampus and fetal liver cells, Pim-1 has also been found to be highly expressed in cell cultures isolated from human tumors. Pim-1 is mainly involved in cell cycle progression, apoptosis and transcriptional activation, as well as more general signal transduction pathways. It has been found a physiologic role of the PIM1 oncogene during hematopoietic development and a deregulation of the gene in various leukemias. PIM1 also has a role in cardioprotection downstream of AKT activation.

A synthetic peptide corresponding to a sequence at the C-terminus of human PIM1, different from the related mouse sequence by seven amino acids and from the related rat sequence by two amino acids.

Cancer, Chromatin Remodeling, Epigenetics and Nuclear Signaling, Hematopoietic Progenitors, Oncoproteins, Oncoproteins/Suppressors, Protein Phosphorylation, Ser/Thr Kinases, Serine/Threonine Kinases, Signal Transduction, Stem Cells

Proto-oncogene with serine/threonine kinase activity involved in cell survival and cell proliferation and thus providing a selective advantage in tumorigenesis. Exerts its oncogenic activity through: the regulation of MYC transcriptional activity, the regulation of cell cycle progression and by phosphorylation and inhibition of proapoptotic proteins (BAD, MAP3K5, FOXO3) . Phosphorylation of MYC leads to an increase of MYC protein stability and thereby an increase of transcriptional activity. The stabilization of MYC exerted by PIM1 might explain partly the strong synergism between these two oncogenes in tumorigenesis. Mediates survival signaling through phosphorylation of BAD, which induces release of the anti-apoptotic protein Bcl- X (L) /BCL2L1. Phosphorylation of MAP3K5, an other proapoptotic protein, by PIM1, significantly decreases MAP3K5 kinase activity and inhibits MAP3K5-mediated phosphorylation of JNK and JNK/p38MAPK subsequently reducing caspase-3 activation and cell apoptosis. Stimulates cell cycle progression at the G1-S and G2-M transitions by phosphorylation of CDC25A and CDC25C. Phosphorylation of CDKN1A, a regulator of cell cycle progression at G1, results in the relocation of CDKN1A to the cytoplasm and enhanced CDKN1A protein stability. Promote cell cycle progression and tumorigenesis by down-regulating expression of a regulator of cell cycle progression, CDKN1B, at both transcriptional and post- translational levels. Phosphorylation of CDKN1B, induces 14-3-3- proteins binding, nuclear export and proteasome-dependent degradation. May affect the structure or silencing of chromatin by phosphorylating HP1 gamma/CBX3. Acts also as a regulator of homing and migration of bone marrow cells involving functional interaction with the CXCL12-CXCR4 signaling axis. .

1. Amson, R., Sigaux, F., Przedborski, S., Flandrin, G., Givol, D., Telerman, A. The human protooncogene product p33pim is expressed during fetal hematopoiesis and in diverse leukemias. Proc. Nat. Acad. Sci. 86: 8857-8861, 1989. 2. Bachmann M, Möröy T (April 2005) . The serine/threonine kinase Pim-1. Int. J. Biochem. Cell Biol. 37 (4) : 726–30. 3. Muraski, J. A., Rota, M., Misao, Y., Fransioli, J., Cottage, C., Gude, N., Esposito, G., Delucchi, F., Arcarese, M., Alvarez, R., Siddiqi, S., Emmanuel, G. N., and 13 others. Pim-1 regulates cardiomyocyte survival downstream of Akt. Nature Med. 13: 1467-1475, 2007. Note: Erratum: Nature Med. 14: 350 only, 2008.