Product: Phospho-IRE1 (Ser724) Antibody
Catalog: AF7150
Source: Rabbit
Application: WB, IHC, IF/ICC, ELISA(peptide)
Reactivity: Human, Mouse, Rat
Prediction: Pig, Bovine, Horse, Sheep, Rabbit, Dog, Chicken, Xenopus
Mol.Wt.: 110kD; 110kD,102kD(Calculated).
Uniprot: O75460 | Q76MJ5
RRID: AB_2843590

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Product Info

Source:
Rabbit
Application:
WB 1:500-1:2000, IHC 1:50-1:200, IF/ICC 1:50-1:200, ELISA(peptide) 1:20000-1:40000
*The optimal dilutions should be determined by the end user.
Reactivity:
Human,Mouse,Rat
Prediction:
Pig(100%), Bovine(100%), Horse(100%), Sheep(100%), Rabbit(100%), Dog(100%), Chicken(100%), Xenopus(90%)
Clonality:
Polyclonal
Specificity:
Phospho-IRE1 (Ser724) Antibody detects endogenous levels of IRE1 only when phosphorylated at phospho S724.
RRID:
AB_2843590
Cite Format: Affinity Biosciences Cat# AF7150, RRID:AB_2843590.
Purification:
The antibody is from purified rabbit serum by affinity purification via sequential chromatography on phospho-peptide and non-phospho-peptide affinity columns.
Storage:
Rabbit IgG in phosphate buffered saline , pH 7.4, 150mM NaCl, 0.02% sodium azide and 50% glycerol. Store at -20 °C. Stable for 12 months from date of receipt.
Alias:

Fold/Unfold

Endoplasmic reticulum (ER) to nucleus signalling 1; Endoplasmic reticulum to nucleus signaling 1; Endoplasmic reticulum-to-nucleus signaling 1; Endoribonuclease; ER to nucleus signaling 1; ERN 1; Ern1; ERN1_HUMAN; hIRE 1p; hIRE1p; Inositol requiring 1; Inositol requiring 1, S. cerevisiae, homolog of; Inositol requiring enzyme 1, S. cerevisiae, homolog of; Inositol requiring protein 1; inositol-requiring enzyme 1; Inositol-requiring protein 1; IRE 1; IRE 1a; IRE 1P; Ire1 alpha; Ire1-alpha; IRE1a; Ire1alpha; IRE1P; MGC163277; MGC163279; Protein kinase/endoribonuclease; RGD1559716; Serine/threonine protein kinase/endoribonuclease IRE1; Endoplasmic reticulum (ER) to nucleus signalling 1; Endoplasmic reticulum to nucleus signaling 1; Endoplasmic reticulum-to-nucleus signaling 1; Endoribonuclease; ER to nucleus signaling 1; ERN 1; Ern1; ERN1_HUMAN; hIRE 1p; hIRE1p; Inositol requiring 1; Inositol requiring 1, S. cerevisiae, homolog of; Inositol requiring enzyme 1, S. cerevisiae, homolog of; Inositol requiring protein 1; inositol-requiring enzyme 1; Inositol-requiring protein 1; IRE 1; IRE 1a; IRE 1P; Ire1 alpha; Ire1-alpha; IRE1a; Ire1alpha; IRE1P; MGC163277; MGC163279; Protein kinase/endoribonuclease; RGD1559716; Serine/threonine protein kinase/endoribonuclease IRE1;

Immunogens

Immunogen:
Uniprot:
Gene(ID):
Expression:
O75460 ERN1_HUMAN:

Ubiquitously expressed. High levels observed in pancreatic tissue.

Sequence:
MPARRLLLLLTLLLPGLGIFGSTSTVTLPETLLFVSTLDGSLHAVSKRTGSIKWTLKEDPVLQVPTHVEEPAFLPDPNDGSLYTLGSKNNEGLTKLPFTIPELVQASPCRSSDGILYMGKKQDIWYVIDLLTGEKQQTLSSAFADSLCPSTSLLYLGRTEYTITMYDTKTRELRWNATYFDYAASLPEDDVDYKMSHFVSNGDGLVVTVDSESGDVLWIQNYASPVVAFYVWQREGLRKVMHINVAVETLRYLTFMSGEVGRITKWKYPFPKETEAKSKLTPTLYVGKYSTSLYASPSMVHEGVAVVPRGSTLPLLEGPQTDGVTIGDKGECVITPSTDVKFDPGLKSKNKLNYLRNYWLLIGHHETPLSASTKMLERFPNNLPKHRENVIPADSEKKSFEEVINLVDQTSENAPTTVSRDVEEKPAHAPARPEAPVDSMLKDMATIILSTFLLIGWVAFIITYPLSMHQQQQLQHQQFQKELEKIQLLQQQQQQLPFHPPGDTAQDGELLDTSGPYSESSGTSSPSTSPRASNHSLCSGSSASKAGSSPSLEQDDGDEETSVVIVGKISFCPKDVLGHGAEGTIVYRGMFDNRDVAVKRILPECFSFADREVQLLRESDEHPNVIRYFCTEKDRQFQYIAIELCAATLQEYVEQKDFAHLGLEPITLLQQTTSGLAHLHSLNIVHRDLKPHNILISMPNAHGKIKAMISDFGLCKKLAVGRHSFSRRSGVPGTEGWIAPEMLSEDCKENPTYTVDIFSAGCVFYYVISEGSHPFGKSLQRQANILLGACSLDCLHPEKHEDVIARELIEKMIAMDPQKRPSAKHVLKHPFFWSLEKQLQFFQDVSDRIEKESLDGPIVKQLERGGRAVVKMDWRENITVPLQTDLRKFRTYKGGSVRDLLRAMRNKKHHYRELPAEVRETLGSLPDDFVCYFTSRFPHLLAHTYRAMELCSHERLFQPYYFHEPPEPQPPVTPDAL

MASAVRGSRPWPRLGLQLQFAALLLGTLSPQVHTLRPENLLLVSTLDGSLHALSKQTGDLKWTLRDDPVIEGPMYVTEMAFLSDPADGSLYILGTQKQQGLMKLPFTIPELVHASPCRSSDGVFYTGRKQDAWFVVDPESGETQMTLTTEGPSTPRLYIGRTQYTVTMHDPRAPALRWNTTYRRYSAPPMDGSPGKYMSHLASCGMGLLLTVDPGSGTVLWTQDLGVPVMGVYTWHQDGLRQLPHLTLARDTLHFLALRWGHIRLPASGPRDTATLFSTLDTQLLMTLYVGKDETGFYVSKALVHTGVALVPRGLTLAPADGPTTDEVTLQVSGEREGSPSTAVRYPSGSVALPSQWLLIGHHELPPVLHTTMLRVHPTLGSGTAETRPPENTQAPAFFLELLSLSREKLWDSELHPEEKTPDSYLGLGPQDLLAASLTAVLLGGWILFVMRQQQPQVVEKQQETPLAPADFAHISQDAQSLHSGASRRSQKRLQSPSKQAQPLDDPEAEQLTVVGKISFNPKDVLGRGAGGTFVFRGQFEGRAVAVKRLLRECFGLVRREVQLLQESDRHPNVLRYFCTERGPQFHYIALELCRASLQEYVENPDLDRGGLEPEVVLQQLMSGLAHLHSLHIVHRDLKPGNILITGPDSQGLGRVVLSDFGLCKKLPAGRCSFSLHSGIPGTEGWMAPELLQLLPPDSPTSAVDIFSAGCVFYYVLSGGSHPFGDSLYRQANILTGAPCLAHLEEEVHDKVVARDLVGAMLSPLPQPRPSAPQVLAHPFFWSRAKQLQFFQDVSDWLEKESEQEPLVRALEAGGCAVVRDNWHEHISMPLQTDLRKFRSYKGTSVRDLLRAVRNKKHHYRELPVEVRQALGQVPDGFVQYFTNRFPRLLLHTHRAMRSCASESLFLPYYPPDSEARRPCPGATGR

Predictions

Predictions:

Score>80(red) has high confidence and is suggested to be used for WB detection. *The prediction model is mainly based on the alignment of immunogen sequences, the results are for reference only, not as the basis of quality assurance.

Species
Results
Score
Pig
100
Horse
100
Bovine
100
Sheep
100
Dog
100
Chicken
100
Rabbit
100
Xenopus
90
Zebrafish
0
Model Confidence:
High(score>80) Medium(80>score>50) Low(score<50) No confidence

PTMs - O75460/Q76MJ5 As Substrate

Site PTM Type Enzyme
T49 Phosphorylation
K88 Ubiquitination
K95 Ubiquitination
T132 Phosphorylation
Y161 Phosphorylation
Y166 Phosphorylation
Y179 Phosphorylation
T283 Phosphorylation
Y289 Phosphorylation
K374 Acetylation
K374 Ubiquitination
K485 Ubiquitination
S533 Phosphorylation
S536 Phosphorylation
S544 Phosphorylation
S548 Phosphorylation
S551 Phosphorylation
Y628 Phosphorylation O75460 (ERN1)
K633 Ubiquitination
K706 Ubiquitination
S724 Phosphorylation O75460 (ERN1)
S726 Phosphorylation
S729 Phosphorylation
K851 Ubiquitination
K860 Ubiquitination
T973 Phosphorylation
Site PTM Type Enzyme
S268 Phosphorylation
S802 Phosphorylation
Y860 Phosphorylation

PTMs - O75460/Q76MJ5 As Enzyme

Substrate Site Source
O75460 (ERN1) Y628 Uniprot
O75460 (ERN1) S724 Uniprot
Substrate Site Source

Research Backgrounds

Function:

Serine/threonine-protein kinase and endoribonuclease that acts as a key sensor for the endoplasmic reticulum unfolded protein response (UPR). In unstressed cells, the endoplasmic reticulum luminal domain is maintained in its inactive monomeric state by binding to the endoplasmic reticulum chaperone HSPA5/BiP. Accumulation of misfolded protein in the endoplasmic reticulum causes release of HSPA5/BiP, allowing the luminal domain to homodimerize, promoting autophosphorylation of the kinase domain and subsequent activation of the endoribonuclease activity. The endoribonuclease activity is specific for XBP1 mRNA and excises 26 nucleotides from XBP1 mRNA. The resulting spliced transcript of XBP1 encodes a transcriptional activator protein that up-regulates expression of UPR target genes. Acts as an upstream signal for ER stress-induced GORASP2-mediated unconventional (ER/Golgi-independent) trafficking of CFTR to cell membrane by modulating the expression and localization of SEC16A.

PTMs:

Autophosphorylated following homodimerization. Autophosphorylation promotes activation of the endoribonuclease domain.

ADP-ribosylated by PARP16 upon ER stress, which increases both kinase and endonuclease activities.

Subcellular Location:

Endoplasmic reticulum membrane>Single-pass type I membrane protein.

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionSubcellular location
Tissue Specificity:

Ubiquitously expressed. High levels observed in pancreatic tissue.

Subunit Structure:

Monomer. Homodimer; disulfide-linked; homodimerization takes place in response to endoplasmic reticulum stress and promotes activation of the kinase and endoribonuclease activities. Dimer formation is driven by hydrophobic interactions within the N-terminal luminal domains and stabilized by disulfide bridges. Interacts (via the luminal region) with DNAJB9/ERdj4; interaction takes place in unstressed cells and promotes recruitment of HSPA5/BiP. 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. Interacts with PDIA6, a negative regulator of the UPR; the interaction is direct and disrupts homodimerization. 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. Interacts with RNF13.

Family&Domains:

Belongs to the protein kinase superfamily. Ser/Thr protein kinase family.

Function:

Induces translational repression through 28S ribosomal RNA cleavage in response to ER stress. Pro-apoptotic. Appears to play no role in the unfolded-protein response, unlike closely related proteins.

PTMs:

Autophosphorylated.

Subcellular Location:

Endoplasmic reticulum membrane>Single-pass type I membrane protein.

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionSubcellular location
Family&Domains:

Belongs to the protein kinase superfamily. Ser/Thr protein kinase family.

Research Fields

· Cellular Processes > Transport and catabolism > Autophagy - animal.   (View pathway)

· Cellular Processes > Cell growth and death > Apoptosis.   (View pathway)

· Genetic Information Processing > Folding, sorting and degradation > Protein processing in endoplasmic reticulum.   (View pathway)

· Human Diseases > Endocrine and metabolic diseases > Non-alcoholic fatty liver disease (NAFLD).

· Human Diseases > Neurodegenerative diseases > Alzheimer's disease.

References

1). Zhao YS et al. Hydrogen and Oxygen Mixture to Improve Cardiac Dysfunction and Myocardial Pathological Changes Induced by Intermittent Hypoxia in Rats. Oxid Med Cell Longev 2019 Mar 7;2019:7415212 (PubMed: 30984338) [IF=7.310]

Application: WB    Species: rat    Sample: endoplasmic reticulum

Figure 3: |The H2-O2 mixture-induced inhibition of ER stress caused by CIH for 35 d: (a) the ER stress markers GRP 78, caspase 12, and CHOP protein expressions; (b–d) the ratios of p-PERK, p-eIF2α/eIF2α, and p-IRE 1/IRE 1 in the left ventricle

2). Chen X et al. Deletion of ACLY Disrupts Histone Acetylation and IL-10 Secretion in Trophoblasts, Which Inhibits M2 Polarization of Macrophages: A Possible Role in Recurrent Spontaneous Abortion. Oxid Med Cell Longev 2022 May 11;2022:5216786. (PubMed: 35602106) [IF=7.310]

3). Sun ZM et al. Resveratrol protects against CIH-induced myocardial injury by targeting Nrf2 and blocking NLRP3 inflammasome activation. Life Sci 2020 Jan 27:117362 (PubMed: 31996295) [IF=6.780]

Application: WB    Species: Rat    Sample: heart tissue

Fig. 4. Resveratrol treatment weakened cardiac ER stress in rats exposed to CIH. A. Representative western blot images related to ER stress. B. p-PERK/ERK ratio. C. p-IRE/IRE ratio. D. GRP78 expression. n = 6. *p < 0.05 vs. control group; #p < 0.05 vs. CIH group. △ There was a CIH × resveratrol interaction.

4). Wu L et al. Involvement of miR‐27a‐3p in diabetic nephropathy via affecting renal fibrosis, mitochondrial dysfunction, and endoplasmic reticulum stress. J Cell Physiol 2020 Jul 21. (PubMed: 32691413) [IF=6.513]

Application: WB    Species: mice    Sample: kidney

FIGURE 4 Effect of miR‐27a‐3p on endoplasmic reticulum stress and apoptosis in the renal cortex of db/db mice. (a) Western blot analysis of p‐IRE1α, IRE1α, XBP1s, p‐PERK, PERK, p‐eIF2α, eIF2α, and CHOP proteins in the kidney tissues of mice. (b) Apoptosis in renal cortex was visualized by TUNEL immunohistochemical staining. Data are presented as mean ± SD (n = 6). CHOP, C/EBP homologous protein; eIF2α, eukaryotic initiation factor 2 α; IRE1α, inositol‐requiring transmembrane kinase/endoribonuclease 1α; TUNEL, terminal deoxynucleotidyl transferase dUTP nick end labeling; XBP1, X‐box binding protein 1

5). Tao Y et al. IRE1α/NOX4 signaling pathway mediates ROS‐dependent activation of hepatic stellate cells in NaAsO2‐induced liver fibrosis. J Cell Physiol 2020 Aug 10. (PubMed: 32776539) [IF=6.513]

Application: WB    Species: mouse    Sample: HSC‐t6 cells

FIGURE 3 NaAsO2 caused activation of IRE1α–endoplasmic reticulum‐stress pathway, NOX4, and hepatic stellate cell in vitro. (a–c) Hepatic stellate cells‐T6 were treated with 0–4 μM NaAsO2 for 24 hr. (a) The level of IRE1α phosphorylation in cells was monitored through western blot. (b) The expression level of NOX4 and p22phox in cells was monitored through western blot. (c) The expression level of Collagen‐1 and α‐SMA in cells was monitored through western blot. Values are mean ± standard deviation, and n = 3. *p < .05, **p < .01 compared to the control group. Collagen‐1, collagen type 1; GAPDH, glyceraldehyde‐3‐phosphate dehydrogenase; NOX4, nicotinamide adenine dinucleotide phosphate oxidase 4; p‐IRE1α, phospho‐inositol‐requiring enzyme 1α; α‐SMA, α‐smooth muscle actin

6). Yang Y et al. Sesamol supplementation alleviates nonalcoholic steatohepatitis and atherosclerosis in high-fat, high carbohydrate and high-cholesterol diet-fed rats. Food Funct 2021 Oct 4;12(19):9347-9359. (PubMed: 34606548) [IF=6.317]

7). Hsu JY et al. Aqueous Extract of Pepino Leaves Ameliorates Palmitic Acid-Induced Hepatocellular Lipotoxicity via Inhibition of Endoplasmic Reticulum Stress and Apoptosis. Antioxidants (Basel) 2021 Jun 3;10(6):903. (PubMed: 34204987) [IF=6.312]

8). Fei H et al. CTRP1 Attenuates Cerebral Ischemia/Reperfusion Injury via the PERK Signaling Pathway. Front Cell Dev Biol 2021 Aug 4;9:700854. (PubMed: 34422821) [IF=6.081]

9). Liao J et al. Endoplasmic Reticulum Stress Contributes to Copper-Induced Pyroptosis via Regulating the IRE1α-XBP1 Pathway in Pig Jejunal Epithelial Cells. J Agric Food Chem 2022 Feb 2;70(4):1293-1303. (PubMed: 35075900) [IF=5.895]

10). Ma J et al. Peroxisome Proliferator-Activated Receptor-Gamma Reduces ER Stress and Inflammation via Targeting NGBR Expression. Front Pharmacol 2022 Jan 17;12:817784. (PubMed: 35111067) [IF=5.810]

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