Render Target: SSR
Render Timestamp: 2024-11-14T22:41:31.150Z
Commit: 3c1f305a63297e594ac8d7bb5424007d592d68be
XML generation date: 2024-04-05 20:28:11.820
Product last modified at: 2024-11-13T15:15:08.206Z
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PDP - Template Name: Monoclonal Antibody
PDP - Template ID: *******c5e4b77

CHOP (L63F7) Mouse mAb #2895

Filter:
  • WB
  • IP
  • IF
  • F
  • ChIP

    Supporting Data

    REACTIVITY H M R
    SENSITIVITY Endogenous
    MW (kDa) 27
    Source/Isotype Mouse IgG2a
    Application Key:
    • WB-Western Blotting 
    • IP-Immunoprecipitation 
    • IF-Immunofluorescence 
    • F-Flow Cytometry 
    • ChIP-Chromatin Immunoprecipitation 
    Species Cross-Reactivity Key:
    • H-Human 
    • M-Mouse 
    • R-Rat 

    Product Information

    Product Usage Information

    For optimal ChIP results, use 2.5 μl of antibody and 10 μg of chromatin (approximately 4 x 106 cells) per IP. This antibody has been validated using SimpleChIP® Enzymatic Chromatin IP Kits.

    Application Dilution
    Western Blotting 1:1000
    Immunoprecipitation 1:50
    Immunofluorescence (Immunocytochemistry) 1:400 - 1:1600
    Flow Cytometry (Fixed/Permeabilized) 1:250 - 1:1000
    Chromatin IP 1:200

    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.

    For a carrier free (BSA and azide free) version of this product see product #78063.

    Protocol

    Specificity / Sensitivity

    CHOP (L63F7) Mouse mAb detects endogenous levels of total CHOP protein.

    Species Reactivity:

    Human, Mouse, Rat

    Source / Purification

    Monoclonal antibody is produced by immunizing animals with a synthetic peptide corresponding to the sequence of human CHOP.

    Background

    CHOP was identified as a C/EBP-homologous protein that inhibits C/EBP and LAP in a dominant-negative manner (1). CHOP expression is induced by certain cellular stresses including starvation and the induced CHOP suppresses cell cycle progression from G1 to S phase (2). Later it was shown that, during ER stress, the level of CHOP expression is elevated and CHOP functions to mediate programmed cell death (3). Studies also found that CHOP mediates the activation of GADD34 and Ero1-Lα expression during ER stress. GADD34 in turn dephosphorylates phospho-Ser51 of eIF2α thereby stimulating protein synthesis. Ero1-Lα promotes oxidative stress inside the endoplasmic reticulum (ER) (4). The role of CHOP in the programmed cell death of ER-stressed cells is correlated with its role promoting protein synthesis and oxidative stress inside the ER (4).
    For Research Use Only. Not For Use In Diagnostic Procedures.
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