Render Target: SSR
Render Timestamp: 2024-12-19T21:29:55.089Z
Commit: f2d32940205a64f990b886d724ccee2c9935daff
XML generation date: 2024-08-01 15:28:36.047
Product last modified at: 2024-12-14T01:00:11.202Z
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PDP - Template Name: Polyclonal Antibody
PDP - Template ID: *******59c6464

PGK1 Antibody #68540

Filter:
  • WB

    Supporting Data

    REACTIVITY H M R
    SENSITIVITY Endogenous
    MW (kDa) 43
    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

    PGK1 Antibody recognizes endogenous levels of total PGK1 protein.

    Species Reactivity:

    Human, Mouse, Rat

    Source / Purification

    Polyclonal antibodies are produced by immunizing animals with a synthetic peptide corresponding to residues surrounding Thr298 of human PGK1 protein. Antibodies are purified by protein A and peptide affinity chromatography.

    Background

    PGK1 (phosphoglycerate kinase) is an essential enzyme in the glycolysis pathway (1). It catalyzes the reversible phospho-transfer reaction from 1,3-diphosphoglycerate to ADP to form ATP and 3-phosphoglycerate. The expression of PGK1 is upregulated in many cancer types and plays an important role in cancer cell proliferation and metastasis (2-5). PGK1 can also function as a protein kinase. ERK can phosphorylate PGK1 at Ser203. This phosphorylation changes PGK1 conformation and leads to its translocation from cytoplasm to mitochondria. There it interacts and phosphorylates PDHK1 (pyruvate dehydrogenase kinase isomerase 1), which leads to PDHK1 inhibition, blocks pyruvate to coenzyme A conversion, and promotes cytosolic lactate concentration (6). Acetylated PGK1 can phosphorylate Beclin1 to induce autophagy (7). PGK1 is activated by autophosphorylation at Tyr324. PTEN can dephosphorylate PGK1 at this site to downregulate its activity. In cancer cells, loss of PTEN enhances PGK1 activity and promotes glycolysis and tumor growth (8).
    For Research Use Only. Not For Use In Diagnostic Procedures.
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