Render Target: SSR
Render Timestamp: 2025-03-06T19:11:47.460Z
Commit: 9fc0f116116d9da247dc8ddd4e5fe811153412e1
XML generation date: 2024-08-01 15:26:30.520
Product last modified at: 2025-02-13T21:30:15.057Z
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PDP - Template Name: Polyclonal Antibody
PDP - Template ID: *******59c6464

HERPUD1 Antibody #26730

Filter:
  • WB

    Supporting Data

    REACTIVITY H M R Mk
    SENSITIVITY Endogenous
    MW (kDa) 54
    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

    HERPUD1 Antibody recognizes endogenous levels of total HERPUD1 protein. This antibody also cross-reacts with unidentified proteins of 30 kDa and 48 kDa. This antibody does not cross-react with HERPUD2 protein.

    Species Reactivity:

    Human, Mouse, Rat, Monkey

    Source / Purification

    Polyclonal antibodies are produced by immunizing animals with a synthetic peptide corresponding to residues near the amino terminus of human HERPUD1 protein. Antibodies are purified by protein A and peptide affinity chromatography.

    Background

    The homocysteine-responsive, ER-resident ubiquitin-like domain member 1 protein (HERPUD1) is an ER membrane protein and putative component of the ER-membrane-associated protein degradation (ERAD) pathway (1). HERPUD1 is a transmembrane protein with both amino- and carboxy-termini exposed to the cytoplasm. The amino-terminal HERPUD1 region contains an ubiquitin-like (UBL) domain (1). Increased expression of HERPUD1 protein following ER stress and its association with ERAD component proteins suggests that HERPUD1 may play an integral role in ERAD pathway function (1). Research studies demonstrate that HERPUD1 associates with components of the ERAD machinery, such as the E3 ubiquitin ligase HRD1, which enhances HRD1-mediated ubiquitination and proteasomal degradation of potentially toxic ERAD substrates (2-4). The HERPUD1 protein may act as a molecular adaptor for the recruitment of ERAD machinery and the amino-terminal UBL domain may important for this function (3,4). The loss of HERPUD1 expression renders cells more susceptible to ER stress and apoptosis (5,6).
    For Research Use Only. Not For Use In Diagnostic Procedures.
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