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Human ERN1 Protein expressed in Baculovirus infected Insect Cells - ABIN2004877
Trentmann: ERN1, a novel ethylene-regulated nuclear protein of Arabidopsis. in Plant molecular biology 2000
Show all 5 Pubmed References
Human ERN1 Protein expressed in HEK-293 Cells - ABIN2720502
Lee, Wang, Reyes, Armstrong, Kulikowicz, Santos, Lee, Koehler, Martin: Hypothermia and Rewarming Activate a Macroglial Unfolded Protein Response Independent of Hypoxic-Ischemic Brain Injury in Neonatal Piglets. in Developmental neuroscience 2016
Data show that LPS (show TLR4 Proteins) induces endoplasmic reticulum (ER) stress and P300 (show NOTCH1 Proteins) activity via the XBP1 (show XBP1 Proteins)/IRE1 pathway.
cytokine-activated STAT3 and STAT6 cooperate in macrophages to promote a secretory phenotype that enhances tumor progression in a cathepsin-dependent manner.
Data suggest that activation of GRP78 (show HSPA5 Proteins)/Ire1/Xbp1 (show XBP1 Proteins) pathway of ER stress-unfolded protein response is involved in mouse decidualization.
Fortilin directly interacts with the cytoplasmic domain of IRE1alpha, inhibits both kinase and endoribonuclease (RNase) activities of this stress sensor, and protects cells against apoptotic cell death at both cellular and whole animal levels.
Regulated IRE1-dependent mRNA decay sets the threshold for dendritic cell survival.
defective autophagy in intestinal epithelial cells (IECs) may predispose to Crohn's disease ileitis via impaired clearance of IRE1alpha aggregates during ER stress at this site.
The findings indicate that IRE1-XBP1 (show XBP1 Proteins) downregulation distinguishes germinal center B-cell-like diffuse large B-cell lymphoma (DLBCL) from other DLBCL subtypes and contributes to tumor growth.
the ABL (show ABL1 Proteins) family of tyrosine kinases rheostatically enhances IRE1alpha's enzymatic activities, thereby potentiating endoplasmic reticulum stress-induced apoptosis.
We reveal distinct binding affinities between the binary and ternary complexes thus formed, that suggest a preference for the PERK (show EIF2AK3 Proteins) signaling branch under stress, and a predilection for the GRP78 (show HSPA5 Proteins)-UPR sensor complex formation upon stressor removal. These results imply a gated UPR mechanism that tunes the overall cellular behavior to the accumulation of unfolded proteins.
Inositol-Requiring Enzyme 1 Facilitates Diabetic Wound Healing Through Modulating MicroRNAs.
Overall, these data demonstrate that hypoxia can suppress adiponectin (show ADIPOQ PLURAL_@37961@) expression and activate the PERK (show EIF2AK3 PLURAL_@37961@) and IRE1 signaling pathways in differentiated adipocytes, and this two pathways are involved in the suppression of adiponectin (show ADIPOQ PLURAL_@37961@) expression induced by hypoxia.
ER stress-regulated IRE1 dependent decay is involved in regulation of hepatic diseases. (review)
The unfolded protein response reduces glucose metabolism via IRE1 signaling.
Results of this investigation demonstrate that inhibition of IRE1 signaling enzyme function affects the expression of NRIP1 (show NRIP1 Proteins), EBBP (show TRIM16 Proteins), ESRRA (show ESRRA Proteins), E2IG5 (show FAM162A Proteins), PGRMC2 (show PGRMC2 Proteins), and SLC39A6 (show SLC39A6 Proteins) genes in U87 glioma cells in gene specific manner and these changes possibly contribute to the suppression of the cell proliferation. Most of these genes are regulated by hypoxia and preferentially through IRE1 signaling pathway of endoplasmic reticulum stress
IRE1alpha was shown to cleave miR (show MLXIP Proteins)-150 and thereby to release the suppressive effect that miR (show MLXIP Proteins)-150 exerted on alphaSMA (show ACTA2 Proteins) expression through c-Myb (show MYB Proteins). Inhibition of IRE1alpha was also demonstrated to block endoplasmic reticulum expansion through an XBP-1 (show XBP1 Proteins)-dependent pathway.
IRE-1 has an ancient function as a cytoplasmic sentinel that activates p38 (show CRK Proteins) and SKN-1(Nrf2 (show GABPA Proteins)). csteine modifications induced by ROS (show ROS1 Proteins) signals can direct proteins to adopt unexpected functions and may coordinate many cellular processes.
Western blot analysis of subcutaneously implanted AsPC-1 and BxPC-3 tumors as well as orthotopically implanted Panc-1 tumors demonstrated upregulation of BIP (show GDF10 Proteins), CHOP (show DDIT3 Proteins), and IRE1alpha expression in the tumor lysates from penfluridol-treated mice as compared to tumors from control mice
The protein encoded by this gene is the ER to nucleus signalling 1 protein, a human homologue of the yeast Ire1 gene product. This protein possesses intrinsic kinase activity and an endoribonuclease activity and it is important in altering gene expression as a response to endoplasmic reticulum-based stress signals.
ER to nucleus signalling 1
, endoplasmic reticulum-to-nucleus signaling 1
, inositol-requiring 1
, inositol-requiring enzyme 1
, inositol-requiring protein 1
, protein kinase/endoribonuclease
, serine/threonine-protein kinase/endoribonuclease IRE1
, endoplasmic reticulum to nucleus signalling 1
, inositol-requiring 1 alpha
, endoplasmic reticulum (ER) to nucleus signalling 1
, endoplasmic reticulum-to-nucleus signaling 2
, inositol-requiring 1 (Yeast homologue)
, inositol-requiring 1 beta
, inositol-requiring protein 2
, serine/threonine-protein kinase/endoribonuclease IRE2
, endoplasmic reticulum to nucleus signaling 1