Synthetic phosphopeptide corresponding to amino acid residues surrounding the phospho-Ser724 of mouse IRE1, conjugated to keyhole limpet hemocyanin (KLH).
Specificity
Specific for endogenous levels of the ~130 kDa GluR1 protein phosphorylated at Ser724. Immunolabeling is completely eliminated by treatment with λ-phosphatase.
Buffer
10 mM HEPES (pH 7.5), 150 mM NaCl, 100 µg per ml BSA and 50% glycerol.
Concentration
lot specific
Purification
Antigen Affinity Purified from Pooled Serum
Conjugation
Unconjugated
Storage
Storage at -20°C is recommended, as aliquots may be taken without freeze/thawing due to presence of 50% glycerol. Stable for at least 1 year at -20°C.
Stability
After date of receipt, stable for at least 1 year at -20°C.
Shipping
Blue Ice
Predicted Protein Size
130
Gene Name
endoplasmic reticulum (ER) to nucleus signalling 1
IRE1, inositol requiring 1 protein, is an ER transmembrane sensor that activates unfolded protein response (UPR) to maintain the ER and cellular function (Chen et al, 2013). The activation of UPR involves three signaling pathways, IRE1, PERK, and ATF6, which are crucial to returning protein homoeostasis to levels of non-stressed cells (Stewart et al, 2012). Changes in ER homeostasis causing unfolded protein buildup can be due to Ca2+ depletion, hypoxia, altered glycosylation, and viral infection triggering the UPR and activation of IRE1 (Stewart et al, 2012). UPR dysfunction plays an important role in the pathogenesis of neurodegenerative diseases including Alzheimer's disease, Parkinson's disease, amyotrophic lateral sclerosis and Huntington's disease, which is characterized by the accumulation and aggregation of misfolded proteins (Xiang C et al, 2017). The phosphorylation of IRE1 at ser724 may play a significant role in understanding these diseases.
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