The Phospho-Pim1 (Tyr309) Antibody (PAC024089) is a valuable tool for researchers studying the Pim1 protein, a serine/threonine protein kinase involved in cell proliferation and survival. This antibody, produced in rabbits, specifically targets the phosphorylated form of Pim1 at tyrosine 309 and is highly reactive with human samples. It has been validated for use in Western blot applications, allowing for the detection and analysis of phosphorylated Pim1 in various cell types.Pim1 is known to play a crucial role in signaling pathways that regulate cell growth and survival, making it a promising target for cancer research. The phosphorylation of Pim1 at tyrosine 309 has been linked to its activity and function, making this antibody a valuable tool for investigating the role of Pim1 in cancer development and progression.
Understanding the phosphorylation status of Pim1 can provide insight into its function and potential as a therapeutic target in cancer treatment.Overall, the Phospho-Pim1 (Tyr309) Antibody is a reliable tool for researchers interested in studying the role of Pim1 in cancer and other diseases. Its specificity for the phosphorylated form of Pim1 makes it a valuable asset for detecting and analyzing Pim1 activity in cellular pathways, offering new opportunities for research and drug development in the field of oncology.
Antibody Name:
Phospho-Pim1 (Tyr309) Antibody (PACO24089)
Antibody SKU:
PACO24089
Size:
100ul
Host Species:
Rabbit
Tested Applications:
ELISA, WB
Recommended Dilutions:
ELISA:1:2000-1:10000, WB:1:500-1:1000
Species Reactivity:
Human, Mouse, Rat
Immunogen:
Peptide sequence around phosphorylation site of tyrosine 309(A-A-V(p)-W-S) derived from Human Pim-1.
Form:
Liquid
Storage Buffer:
Rabbit IgG in phosphate buffered saline (without Mg2+ and Ca2+), pH 7.4, 150mM NaCl, 0.02% sodium azide and 50% glycerol.
Purification Method:
Antibodies were produced by immunizing rabbits with synthetic phosphopeptide and KLH conjugates. Antibodies were purified by affinity-chromatography using epitope-specific phosphopeptide. Non-phospho specific antibodies were removed by chromatogramphy using non-phosphopeptide.
Clonality:
Polyclonal
Isotype:
IgG
Conjugate:
Non-conjugated
Western blot analysis of extracts from HUVEC cells treated with PMA using Pim-1 (Phospho-Tyr309) Antibody.The lane on the right is treated with the antigen-specific peptide.
Background:
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.
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 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 ().
