Render Target: STATIC
Render Timestamp: 2024-12-20T12:10:01.510Z
Commit: f2d32940205a64f990b886d724ccee2c9935daff
XML generation date: 2024-12-17 23:02:08.204
Product last modified at: 2024-12-18T21:00:09.059Z
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PDP - Template Name: Monoclonal Antibody
PDP - Template ID: *******c5e4b77
R Recombinant
Recombinant: Superior lot-to-lot consistency, continuous supply, and animal-free manufacturing.

Phospho-Ubiquitin (Ser57) (F1I4R) Rabbit mAb #88056

Filter:
  • WB

    Supporting Data

    REACTIVITY H
    SENSITIVITY Transfected Only
    MW (kDa)
    Source/Isotype Rabbit IgG
    Application Key:
    • WB-Western Blotting 
    Species Cross-Reactivity Key:
    • H-Human 

    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, 50% glycerol, and less than 0.02% sodium azide. Store at –20°C. Do not aliquot the antibody.

    Protocol

    Specificity / Sensitivity

    Phospho-Ubiquitin (Ser57) (F1I4R) Rabbit mAb recognizes transfected levels of ubiquitin protein only when phosphorylated at Ser57. This antibody detects bands of unknown origin between 80-90 kDa in some conditions.

    Species Reactivity:

    Human

    Source / Purification

    Monoclonal antibody is produced by immunizing animals with a synthetic phosphopeptide corresponding to residues surrounding Ser57 of human ubiquitin protein.

    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).

    Regulation of ubiquitin homeostasis is mediated by phosphorylation at Ser57, with mutation at Ser57 conferring increased rates of endocytic trafficking and ubiquitin turnover (8). Moreover, phosphorylation of Ser57 has been shown to function in the oxidative stress response in Saccharomyces cerevisiae (9). In vitro kinase assays have demonstrated that kinases in the MARK and SIK families can phosphorylate ubiquitin at Ser57 (9).
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