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Render Timestamp: 2024-11-26T11:16:47.758Z
Commit: d79925545b26f8827f92d145dadc6f0527debdb1
XML generation date: 2024-08-01 15:27:14.980
Product last modified at: 2024-05-30T07:07:19.533Z
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PDP - Template Name: Polyclonal Antibody
PDP - Template ID: *******59c6464

Phospho-Ubiquitin (Ser65) Antibody #37642

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    Supporting Data

    REACTIVITY H
    SENSITIVITY Endogenous
    MW (kDa)
    SOURCE Rabbit
    Application Key:
    • WB-Western Blotting 
    • IP-Immunoprecipitation 
    Species Cross-Reactivity Key:
    • H-Human 

    Product Information

    Product Usage Information

    Application Dilution
    Western Blotting 1:1000
    Immunoprecipitation 1:200

    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-Ubiquitin (Ser65) Antibody recognizes endogenous levels of ubiquitin protein only when phosphorylated at Ser65.

    Species Reactivity:

    Human

    The antigen sequence used to produce this antibody shares 100% sequence homology with the species listed here, but reactivity has not been tested or confirmed to work by CST. Use of this product with these species is not covered under our Product Performance Guarantee.

    Species predicted to react based on 100% sequence homology:

    Mouse, Rat

    Source / Purification

    Polyclonal antibodies are produced by immunizing animals with a synthetic phospho-peptide corresponding to residues surrounding Ser65 of human ubiquitin protein. Antibodies are purified by protein A and peptide affinity chromatography.

    Background

    Ubiquitin is a conserved polypeptide unit that plays an important role in the ubiquitin-proteasome pathway. Ubiquitin can be covalently linked to many cellular proteins by the ubiquitination process, which targets proteins for degradation by the 26S proteasome. Three components are involved in the target protein-ubiquitin conjugation process. Ubiquitin is first activated by forming a thiolester complex with the activation component E1; the activated ubiquitin is subsequently transferred to the ubiquitin-carrier protein E2, then from E2 to ubiquitin ligase E3 for final delivery to the epsilon-NH2 of the target protein lysine residue (1-3). The ubiquitin-proteasome pathway has been implicated in a wide range of normal biological processes and in disease-related abnormalities. Several proteins such as IκB, p53, cdc25A, and Bcl-2 have been shown to be targets for the ubiquitin-proteasome process as part of regulation of cell cycle progression, differentiation, cell stress response, and apoptosis (4-7).

    Ubiquitin is phosphorlated at Ser65 by PINK1, leading to activation of the E3 ubiquitin ligase Parkin (8, 9). PINK1 accumulates on depolarized mitochondria, resulting in phosphorylation of ubiquitin and activation of Parkin, which then triggers the mitophagy pathway to clear damaged mitochondria. Loss-of-function mutations in PINK1 and Parkin result in early onset Parkinson's disease (10, 11).
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