| Overview |
| bs-70135R |
| IRE1 (Ser724) Antibody |
| WB |
| Specific for endogenous levels of the ~130 kDa GluR1 protein phosphorylated at Ser724. Immunolabeling is completely eliminated by treatment with λ-phosphatase. |
| Mouse |
| Human |
| Specifications |
| Unconjugated |
| Rabbit |
| Synthetic phosphopeptide corresponding to amino acid residues surrounding the phospho-Ser724 of mouse IRE1, conjugated to keyhole limpet hemocyanin (KLH). |
| Ser724 |
| Polyclonal |
| IgG |
| Lot Dependent |
| Antigen Affinity purification from Pooled whole antiserum |
| 10 mM HEPES (pH 7.5), 150 mM NaCl, 100 µg per ml BSA and 50% glycerol. |
| 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. |
| Target |
| 78943 |
| Q9EQY0 |
| Endoplasmic reticulum (ER) to nucleus signalling 1 antibody, Endoplasmic reticulum to nucleus signaling 1 antibody, Endoplasmic reticulum-to-nucleus signaling 1 antibody, Endoribonuclease antibody, ER to nucleus signaling 1 antibody, ERN 1 antibody, Ern1 antibody, ERN1_HUMAN antibody, hIRE 1p antibody, hIRE1p antibody, Inositol requiring 1 antibody, Inositol requiring 1, S. cerevisiae, homolog of antibody, Inositol requiring enzyme 1, S. cerevisiae, homolog of antibody, Inositol requiring protein 1 antibody, inositol-requiring enzyme 1 antibody, Inositol-requiring protein 1 antibody, IRE 1 antibody, IRE 1a antibody, IRE 1P antibody, Ire1 alpha antibody, Ire1-alpha antibody, IRE1a antibody, Ire1alpha antibody, IRE1P antibody, MGC163277 antibody, MGC163279 antibody, Protein kinase/endoribonuclease antibody, RGD1559716 antibody, Serine/threonine protein kinase/endoribonuclease IRE1 antibody |
| 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. |
| Application Dilution |
| WB |
1:300-5000 |
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