Render Target: STATIC
Render Timestamp: 2024-11-22T11:02:04.200Z
Commit: 5c4accf06eb7154018ba3f54329c7590f97f534a
XML generation date: 2024-08-01 15:28:43.904
Product last modified at: 2024-11-14T13:00:18.178Z
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PDP - Template Name: Polyclonal Antibody
PDP - Template ID: *******59c6464

SirT4 Antibody #69786

Filter:
  • WB

    Supporting Data

    REACTIVITY H M R Mk
    SENSITIVITY Endogenous
    MW (kDa) 29-33
    SOURCE Rabbit
    Application Key:
    • WB-Western Blotting 
    Species Cross-Reactivity Key:
    • H-Human 
    • M-Mouse 
    • R-Rat 
    • Mk-Monkey 

    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

    SirT4 Antibody recognizes endogenous levels of total SirT4 protein.

    Species Reactivity:

    Human, Mouse, Rat, Monkey

    Source / Purification

    Polyclonal antibodies are produced by immunizing animals with a synthetic peptide corresponding to residues surrounding Gly235 of human SirT4 protein. Antibodies are purified by peptide affinity chromatography.

    Background

    The Silent Information Regulator (SIR2) family of genes is a highly conserved group of genes that encode nicotinamide adenine dinucleotide (NAD)-dependent protein deacetylases, initially classified as Class III histone deacetylases. The first discovered and best characterized of these genes is Saccharomyces cerevisiae Sir2, which is involved in silencing of mating type loci, telomere maintenance, DNA damage response, and cell aging (1). SirT4, a mammalian homolog of Sir2, is localized to the mitochondria and has been implicated in the regulation of cell metabolism, oxidative stress, genomic stability, and aging (2,3). In addition to deacetylase activity, multiple additional enzymatic activities have been attributed to SirT4, including protein deacylation, ADP-ribosylation, and NAD-dependent protein lipoamidase activity. SirT4 regulates the metabolism of glutamine, lipids, and glucose through direct deacetylation of malonyl CoA decarboxylase (MCD) (4), ADP-ribosylation of glutamine dehydrogenase (5), and hydrolysis of the lipoamide cofactors from the E2 component dihydrolipoyllysine acetyltransferase (DLAT) of the pyruvate dehydrogenase complex (PDHC) (6). SirT4 is a tumor suppressor protein, and expression is reduced or lost in a large number of cancers, resulting in the acceleration of tumor morbidity and metastasis (2,3).
    For Research Use Only. Not For Use In Diagnostic Procedures.
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