IRE1 Antibody (YA3557)(PBS only)
(Synonyms: IRE1; IRE1P; IRE1a; hIRE1p; FLJ30999; MGC163277; MGC163279; ERN1)IRE1 Antibody (YA3557) is a Mouse-derived and non-conjugated IgG1 monoclonal antibody, targeting to IRE1.
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Host:
Mouse
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Isotype:
IgG
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Application:
WB, IHC-P, ELISA
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Reactivity :
Human
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Formulation:
Supplied in PBS, pH 7.4.
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Conjugation:
Non-conjugated
To place orders, for customer services and technical support, please contact: MedChemExpress USA
Tel: 609-228-6898 E-mail: [email protected] [email protected]
Applications
| Application |
WB
WB: Western Blot
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IHC-P
IHC-P: Immunohistochemistry-Paraffin
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ELISA
ELISA: Enzyme Linked Immunosorbent Assay
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|---|---|---|---|
| Dilution Ratio | 1:500-1:2000 | 1:200-1:1000 | 1:10000 |
Product Details
IRE1 Antibody (YA3557) is a Mouse-derived and non-conjugated IgG1 monoclonal antibody, targeting to IRE1.
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Host Mouse
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Species ReactivityHuman
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Observed Molecular WeightObserved band size: 110 kDa
Note: Due to possible protein modifications or aggregation, the molecular weight should be confirmed by actual measurement, and the predicted value is for reference only.
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Calculated Molecular Weight Predicted band size: 110 kDa
Purified recombinant fragment of human ERN1(aa282-433) expressed in E. Coli.
affinity purified.
Non-conjugated
IgG
Product Properties
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Appearance
Solution
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Formulation
Supplied in PBS, pH 7.4.
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Storage & Stability
Stored at -20°C for 1 year. Avoid repeated freeze / thaw cycles.
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Shipping
Shipping with blue ice.
Background
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Function
Inositol-requiring enzyme 1 (IRE1) is a bifunctional serine/threonine kinase and endoribonuclease that is a major mediator of the unfolded protein response (UPR) during endoplasmic reticulum (ER) stress. It represents a potential therapeutic target for a number of diseases associated with endoplasmic reticulum stress.
IRE1 is the only identified ER stress sensor in yeast and essential for UPR in animals and plants. As an ER transmembrane protein, IRE1 monitors ER homeostasis through an ER luminal stress-sensing domain and triggers UPR through a cytoplasmic kinase domain and an RNase domain. Upon ER stress, IRE1 RNase is activated through conformational change, autophosphorylation, and higher order oligomerization. Mammalian IRE1 initiates diverse downstream signaling of the UPR either through unconventional splicing of the transcription factor Xbp-1 or and through posttranscriptional modifications via Regulated IRE1-Dependent Decay (RIDD) of multiple substrates.
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Subcellular Localization
Endoplasmic reticulum membrane; Single-pass type I membrane protein
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Expression
Tissue_specificity:Widely expressed. High expression levels are observed in pancreatic tissue.
Induction:Induced by the ER stressor tunicamycin -
Isoforms & Post-Translational Modification
O75460 has 2 isomers: O75460-1: 109735 Da (predicted); O75460-2: 6649 Da (predicted).
Autophosphorylated following homodimerization. Autophosphorylation promotes activation of the endoribonuclease domain (PubMed:12637535, PubMed:21317875, PubMed:28128204, PubMed:9637683). In response to ER stress, phosphorylated at Ser-724, Ser-729 and possibly Ser-726; phosphorylation promotes oligomerization and endoribonuclease activity (PubMed:30118681). Dephosphorylated at Ser-724, Ser-729 and possibly Ser-726 by RPAP2 to abort failed ER-stress adaptation and trigger apoptosis (PubMed:30118681). Phosphorylated at Ser-724; in response to the ER stressor tunicamycin (PubMed:36739529);ADP-ribosylated by PARP16 upon ER stress, which increases both kinase and endonuclease activities -
Subunit
Monomer (PubMed:16973740, PubMed:29198525). Homodimer; disulfide-linked; homodimerization takes place in response to endoplasmic reticulum stress and promotes activation of the kinase and endoribonuclease activities (PubMed:12637535, PubMed:16973740, PubMed:21317875, PubMed:24508390, PubMed:30118681). Dimer formation is driven by hydrophobic interactions within the N-terminal luminal domains and stabilized by disulfide bridges (PubMed:12637535). Interacts (via the luminal region) with DNAJB9/ERdj4; interaction takes place in unstressed cells and promotes recruitment of HSPA5/BiP (PubMed:29198525). Interacts (via the luminal region) with HSPA5/BiP; HSPA5/BiP is a negative regulator of the unfolded protein response (UPR) that prevents homodimerization of ERN1/IRE1 and subsequent activation of the protein (PubMed:12637535, PubMed:29198525, PubMed:36739529). Interaction with HSPA5 also competitively inhibits ERN1 interaction with MANF (PubMed:36739529). Interacts with PDIA6, a negative regulator of the UPR; the interaction is direct and disrupts homodimerization (PubMed:24508390). Interacts with DAB2IP (via PH domain); the interaction occurs in a endoplasmic reticulum stress-induced dependent manner and is required for subsequent recruitment of TRAF2 to ERN1/IRE1 (By similarity). Interacts with TAOK3 and TRAF2 (PubMed:11278723). Interacts with RNF13 (PubMed:23378536). Interacts with LACC1 (PubMed:31875558). Interacts (when unphosphorylated) with DDRGK1; interaction is dependent on UFM1 and takes place in response to endoplasmic reticulum stress, regulating ERN1/IRE1-alpha stability (PubMed:28128204). Interacts (via N-terminus) with P4HB/PDIA1; the interaction is enhanced by phosphorylation of P4HB by FAM20C in response to endoplasmic reticulum stress and results in attenuation of ERN1 activity (PubMed:32149426). Interacts with TMBIM6; this interaction inhibits ERN1 activity (PubMed:19328063). Interacts (via luminal domain) with MANF (via C-terminus); the interaction is decreased in the presence of increasing concentrations of Ca(2+) (PubMed:36739529)
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SwissProt ID
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Synonyms
IRE1; IRE1P; IRE1a; hIRE1p; FLJ30999; MGC163277; MGC163279; ERN1
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