Render Target: STATIC
Render Timestamp: 2024-12-20T12:03:40.203Z
Commit: f2d32940205a64f990b886d724ccee2c9935daff
XML generation date: 2024-08-01 15:25:47.118
Product last modified at: 2024-12-17T18:54:43.923Z
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PDP - Template Name: Polyclonal Antibody
PDP - Template ID: *******59c6464

K48-linkage Specific Polyubiquitin Antibody #4289

Filter:
  • WB

    Supporting Data

    REACTIVITY All
    SENSITIVITY Endogenous
    MW (kDa)
    SOURCE Rabbit
    Application Key:
    • WB-Western Blotting 
    Species Cross-Reactivity Key:
    • All-All Species Expected 

    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

    K48-linkage Specific Polyubiquitin Antibody detects polyubiquitin chains formed by Lys48 residue linkage. Antibody demonstrates slight cross-reactivity with linear polyubiquitin chain. No cross-reactivity observed with monoubiquitin or polyubiquitin chains formed by specific linkage to different lysine residues.

    Species Reactivity:

    All Species Expected

    Source / Purification

    Polyclonal antibodies are produced by immunizing animals with a synthetic peptide corresponding to the Lys48 branch the human diubiquitin chain. 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).

    Substrate proteins are linked to ubiquitin using seven distinct ubiquitin lysine residues (Lys6, Lys11, Lys27, Lys29, Lys33, Lys48 and Lys63). Formation of a polyubiquitin chain occurs when a lysine residue of ubiquitin is linked to the carboxy-terminal glycine of another ubiquitin. Proteins polyubiquinated at specific lysine residues display a tendency to be targeted for different processes; K48-linked polyubiquitin chains mainly target proteins for proteasomal degradation while K63-linked polyubiquitin regulates protein function, subcellular localization, or protein-protein interactions (8).
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