PIM2 blocking peptide

PIM2 Antibody (C-term) Blocking Peptide

• Synonyms: PIM2; PIM2 Antibody (C-term) Blocking Peptide; Serine/threonine-protein kinase pim-2; Pim-2h; PIM2 blocking peptide

• Specificity: The synthetic peptide sequence used to generate the antibody was selected from the C-term region of human PIM2. A 10 to 100 fold molar excess to antibody is recommended. Precise conditions should be optimized for a particular assay.
• Form/Format: The synthetic peptide was lyophilized with 100% acetonitrile and is supplied as a powder. Reconstitute with 0.1 ml deionized water for a final concentration of 1 mg/ml.
• Sequence Length: 311

• Tissue Location: Highly expressed in hematopoietic tissues, in leukemic and lymphoma cell lines, testis, small intestine, colon and colorectal adenocarcinoma cells. Weakly expressed in normal liver, but highly expressed in hepatocellular carcinoma tissues
• Preparation and Storage: Maintain refrigerated at 2-8 degree C for up to 6 months. For long term storage store at -20 degree C.

Related Product Information for PIM2 blocking peptide

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. Isoform 1 is less active in this respect. 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.

NCBI and Uniprot Product Information

• NCBI GI #: 20139243
• NCBI GeneID: 11040
• UniProt Accession #: Q9P1W9; Q99739; A8K4G6
• Molecular Weight: 34,190 Da
• NCBI Official Full Name: Serine/threonine-protein kinase pim-2
• NCBI Official Synonym Full Names: Pim-2 proto-oncogene, serine/threonine kinase
• NCBI Official Symbol: PIM2
• NCBI Protein Information: serine/threonine-protein kinase pim-2
• UniProt Protein Name: Serine/threonine-protein kinase pim-2
• Protein Family: Serine/threonine-protein kinase
• UniProt Gene Name: PIM2
• UniProt Entry Name: PIM2_HUMAN

NCBI Description

This gene encodes a protooncogene that acts as a serine/threonine protein kinase. Studies determined the encoded protein functions to prevent apoptosis and to promote cell survival.[provided by RefSeq, Nov 2009]

Uniprot Description

Pim2: a Ca(2 )/calmodulin-dependent protein kinase of the PIM family. Highly expressed in hematopoietic tissues, in leukemic and lymphoma cell lines, testis, small intestine, colon and colorectal adenocarcinoma cells.

Protein type: Protein kinase, CAMK; Kinase, protein; Protein kinase, Ser/Thr (non-receptor); Oncoprotein; EC 2.7.11.1; CAMK group; PIM family

Chromosomal Location of Human Ortholog: Xp11.23

Cellular Component: cytoplasm

Molecular Function: protein binding; protein serine/threonine kinase activity

Biological Process: cell proliferation; G1/S transition of mitotic cell cycle; male meiosis; negative regulation of apoptosis; negative regulation of cell proliferation; positive regulation of autophagy; positive regulation of I-kappaB kinase/NF-kappaB cascade; positive regulation of transcription, DNA-dependent; protein amino acid autophosphorylation; protein amino acid phosphorylation; protein stabilization; regulation of mitotic cell cycle; response to virus