Render Target: STATIC
Render Timestamp: 2024-11-08T10:03:22.633Z
Commit: 3c1f305a63297e594ac8d7bb5424007d592d68be
XML generation date: 2024-08-01 15:26:30.320
Product last modified at: 2024-10-23T15:15:08.585Z
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PDP - Template Name: Polyclonal Antibody
PDP - Template ID: *******59c6464

BAG6 Antibody #8523

Filter:
  • WB

    Supporting Data

    REACTIVITY H M R Mk Pg
    SENSITIVITY Endogenous
    MW (kDa) 150
    SOURCE Rabbit
    Application Key:
    • WB-Western Blotting 
    Species Cross-Reactivity Key:
    • H-Human 
    • M-Mouse 
    • R-Rat 
    • Mk-Monkey 
    • Pg-Pig 

    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

    BAG6 Antibody recognizes endogenous levels of total BAG6 protein. It does not cross-react with other BCL2-associated athanogene (Bag) family members.

    Species Reactivity:

    Human, Mouse, Rat, Monkey, Pig

    Source / Purification

    Polyclonal antibodies are produced by immunizing animals with a synthetic peptide corresponding to residues near the carboxy terminus of human BAG6 protein. Antibodies are purified by protein A and peptide affinity chromatography.

    Background

    BAG6 (BCL2-associated athanogene-6), alternately known as BAT3 (HLA-B-associated transcript 3), was originally identified as a gene within the class III region of the human major histocompatibility complex, but has subsequently been found to exhibit protein chaperone activity. BAG6, in conjunction with other chaperone proteins and ubiquitin ligases, regulates protein stability and insertion of tail-anchored membrane proteins into the endoplasmic reticulum (ER) (1-3). The BAT3 complex, consisting of BAG6, TRC35, and Ubl4a localizes to ribosomes synthesizing membrane proteins and facilitates tailed-anchored protein capture by TRC40 and subsequent insertion of the nascent protein in to the ER membrane (4,5). BAG6 also plays a critical role in clearing cells of mis-folded and mis-localized peptides via ER-associated degradation and the ubiquitin-proteasome system (1,6,7). BAG6 may also act as a chaperone for glycoproteins through its interaction with DERLIN2 (8).

    In addition to its role as a chaperone, BAG6 has also been implicated in regulating chromatin structure and gene expression. For example, BAG6 and SET1A act as binding partners for BORIS to effect changes of chromatin structure and gene expression (9). Similarly, increased expression of BAG6 induces p300-mediated acetylation of p53, which is required for DNA damage response (10). BAG6 has also been found to interact with TGF-β, and in so doing acts as a positive regulator of TGF-β1 stimulation of type 1 collagen expression (11). BAG6 also suppresses bone morphogenic protein (BMP) signaling via its interaction with and regulation of small C-terminal domain phosphatase (SCP) that dephosphorylates SMAD proteins, resulting in subsequent termination of BMP-mediated events (12).
    For Research Use Only. Not For Use In Diagnostic Procedures.
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