Recombinant Human PIM2 protein is a Human Full Length protein, in the 1 to 311 aa range, expressed in Escherichia coli, with >85% purity and suitable for SDS-PAGE, MS.
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Application SDS-PAGE | Reactivity Reacts | Dilution info - | Notes - |
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Proto-oncogene with serine/threonine kinase activity involved in cell survival and cell proliferation. Exerts its oncogenic activity through: the regulation of MYC transcriptional activity, the regulation of cell cycle progression, the regulation of cap-dependent protein translation and through survival signaling by phosphorylation of a pro-apoptotic protein, BAD. Phosphorylation of MYC leads to an increase of MYC protein stability and thereby an increase transcriptional activity. The stabilization of MYC exerted by PIM2 might explain partly the strong synergism between these 2 oncogenes in tumorigenesis. Regulates cap-dependent protein translation in a mammalian target of rapamycin complex 1 (mTORC1)-independent manner and in parallel to the PI3K-Akt pathway. Mediates survival signaling through phosphorylation of BAD, which induces release of the anti-apoptotic protein Bcl-X(L)/BCL2L1. Promotes cell survival in response to a variety of proliferative signals via positive regulation of the I-kappa-B kinase/NF-kappa-B cascade; this process requires phosphorylation of MAP3K8/COT. Promotes growth factor-independent proliferation by phosphorylation of cell cycle factors such as CDKN1A and CDKN1B. Involved in the positive regulation of chondrocyte survival and autophagy in the epiphyseal growth plate.
Serine/threonine-protein kinase pim-2, Pim-2h, PIM2
Recombinant Human PIM2 protein is a Human Full Length protein, in the 1 to 311 aa range, expressed in Escherichia coli, with >85% purity and suitable for SDS-PAGE, MS.
pH: 8
Constituents: 10% Glycerol (glycerin, glycerine), 0.58% Sodium chloride, 0.32% Tris HCl
ab181913 was purified by using conventional chromatography techniques.
Proto-oncogene with serine/threonine kinase activity involved in cell survival and cell proliferation. Exerts its oncogenic activity through: the regulation of MYC transcriptional activity, the regulation of cell cycle progression, the regulation of cap-dependent protein translation and through survival signaling by phosphorylation of a pro-apoptotic protein, BAD. Phosphorylation of MYC leads to an increase of MYC protein stability and thereby an increase transcriptional activity. The stabilization of MYC exerted by PIM2 might explain partly the strong synergism between these 2 oncogenes in tumorigenesis. Regulates cap-dependent protein translation in a mammalian target of rapamycin complex 1 (mTORC1)-independent manner and in parallel to the PI3K-Akt pathway. Mediates survival signaling through phosphorylation of BAD, which induces release of the anti-apoptotic protein Bcl-X(L)/BCL2L1. Promotes cell survival in response to a variety of proliferative signals via positive regulation of the I-kappa-B kinase/NF-kappa-B cascade; this process requires phosphorylation of MAP3K8/COT. Promotes growth factor-independent proliferation by phosphorylation of cell cycle factors such as CDKN1A and CDKN1B. Involved in the positive regulation of chondrocyte survival and autophagy in the epiphyseal growth plate.
Belongs to the protein kinase superfamily. CAMK Ser/Thr protein kinase family. PIM subfamily.
Autophosphorylated.
PIM2 also known as Pim-2 proto-oncogene encodes a serine/threonine kinase with a molecular weight of approximately 34 kDa. This protein is expressed in various tissues with higher levels in hematopoietic and lymphoid systems. PIM2 kinase activity increases under certain cellular stress conditions and it functions by phosphorylating substrates involved in cell survival proliferation and apoptosis regulation. As a member of the PIM kinase family it shares functional characteristics with its relatives PIM1 and PIM3.
The actions of PIM2 influence cell cycle progression and survival. It does not form a complex but interacts with several other proteins. PIM2 phosphorylates important substrates such as BAD and 4E-BP1 which impacts the cellular translation machinery and apoptotic pathways. Through these interactions PIM2 contributes to cellular responses to growth factors and various stress signals promoting cell survival even in low nutrient or hypoxic conditions.
In the PI3K/AKT and MYC signaling pathways PIM2 has important roles. PIM2 contributes by regulating the stability and activity of MYC a transcription factor vital for cancer cell metabolism. In the PI3K/AKT pathway PIM2 activity works synergistically with AKT to enhance pro-survival and proliferative signals. These actions link PIM2 with both cellular growth and survival pathways often cooperating with proteins like mTOR and BAD to modulate downstream effects.
Aberrant PIM2 expression has been associated with several malignancies including leukemia and multiple myeloma. The elevated PIM2 levels in cancer cells often correlate with resistance to apoptosis contributing to tumor progression. In these contexts PIM2 interacts with oncogenic proteins such as MYC and mTOR establishing a network that supports the survival and growth of tumor cells. Targeting PIM2 directly or its associated pathways offers potential therapeutic strategies for these cancers.
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15% SDS-PAGE analysis of ab181913 (3μg).
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