Render Target: STATIC
Render Timestamp: 2024-10-11T10:20:29.317Z
Commit: 56767fe525c928647c8401233a175d0d607d385d
XML generation date: 2024-08-01 15:27:09.780
Product last modified at: 2024-09-27T13:15:08.067Z
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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.

IRE1α (14C10) Rabbit mAb #3294

Filter:
  • WB
  • IP

    Supporting Data

    REACTIVITY H M R
    SENSITIVITY Endogenous
    MW (kDa) 130
    Source/Isotype Rabbit IgG
    Application Key:
    • WB-Western Blotting 
    • IP-Immunoprecipitation 
    Species Cross-Reactivity Key:
    • H-Human 
    • M-Mouse 
    • R-Rat 

    Product Information

    Product Usage Information

    Application Dilution
    Western Blotting 1:1000
    Immunoprecipitation 1:50

    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

    IRE1α (14C10) Rabbit mAb detects endogenous levels of total IRE1α protein.

    Species Reactivity:

    Human, Mouse, Rat

    Source / Purification

    IRE1α (14C10) Rabbit mAb is produced by immunizing rabbits with a synthetic peptide corresponding to residues surrounding His963 of human IRE1α.

    Background

    The secretory, intra-organellar and transmembrane proteins translocate into the endoplasmic reticulum (ER) after their synthesis. Inside the ER, they are post-translationally modified and properly folded. Disruptions of ER homeostasis leads to the accumulation of unfolded proteins (1). The ER has developed an adaptive mechanism called unfolded protein response (UPR) to counteract compromised protein folding (1). One of the players in UPR, IRE1, was first identified in Saccharomyces cerevisiae as a transmembrane serine/threonine kinase (2-4). This kinase was proposed to be a proximal sensor for UPR that transmits the unfolded protein signal across the ER membrane (3,4). A human homolog of this kinase, IRE1α, was later identified and shown to be ubiquitously expressed in human tissues (5). Upon activation of UPR, IRE1α splices X-box binding protein (XBP1) mRNA by an unconventional mechanism using its endoribonuclease activity (6). This converts XBP1 into a potent transcriptional activator that induces many UPR responsive genes (6). Recently, IRE1α was shown to mediate the rapid degradation of certain mRNAs based on the ER-localization and primary sequences of their encoded proteins, suggesting a novel mechanism in UPR (7).
    For Research Use Only. Not For Use In Diagnostic Procedures.
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