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Render Timestamp: 2024-09-26T11:04:49.837Z
Commit: 60a5021c3a47fc24d1656fb463e2c3c41a1ad145
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PDP - Template Name: Polyclonal Antibody
PDP - Template ID: *******59c6464

Phospho-Pim-1 (Tyr218) Antibody #4721

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  • WB
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Inquiry Info. # 4721

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    Supporting Data

    REACTIVITY H M R
    SENSITIVITY Endogenous
    MW (kDa) 33
    SOURCE Rabbit
    Application Key:
    • WB-Western Blotting 
    Species Cross-Reactivity Key:
    • H-Human 
    • M-Mouse 
    • R-Rat 

    Product Information

    Product Usage Information

    Application Dilution
    Western Blotting 1:1000

    Storage

    Supplied in 10 mM sodium HEPES (pH 7.5), 150 mM NaCl, 100 µg/ml BSA and 50% glycerol. Store at –20°C. Do not aliquot the antibody.

    Protocol

    Specificity / Sensitivity

    Phospho-Pim-1 (Tyr218) Antibody detects endogenous levels of Pim-1 protein when phosphorylated at Tyr218. The phosphorylation site is also conserved with Tyr221 of Pim-3.

    Species Reactivity:

    Human, Mouse, Rat

    Source / Purification

    Polyclonal antibodies are produced by immunizing animals with a synthetic peptide corresponding to residues surrounding tyrosine 218 of Pim-1. Antibodies are purified by protein A and peptide affinity chromatography.

    Background

    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).
    For Research Use Only. Not For Use In Diagnostic Procedures.
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