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Mouse Anti-ERN1 (AA 401-500) Recombinant Antibody (CBFYE-1200) (CBMAB-E1770-FY)

This product is mouse antibody that recognizes ERN1. The antibody CBFYE-1200 can be used for immunoassay techniques such as: ELISA, IF, PLA, WB.
See all ERN1 antibodies

Summary

Host Animal
Mouse
Specificity
Human
Clone
CBFYE-1200
Antibody Isotype
IgG2a, κ
Application
ELISA, IF, PLA, WB

Basic Information

Immunogen
ERN1 partial recombinant protein with GST tag. MW of the GST tag alone is 26 KDa. Immunogen sequence: EEVINLVDQT SENAPTTVSR DVEEKPAHAP ARPEAPVDSM LKDMATIILS TFLLIGWVAF IITYPLSMHQ QQQLQHQQFQ KELEKIQLLQ QQQQQLPFHP
Specificity
Human
Antibody Isotype
IgG2a, κ
Clonality
Monoclonal
Application Notes
The COA includes recommended starting dilutions, optimal dilutions should be determined by the end user.

Formulations & Storage [For reference only, actual COA shall prevail!]

Format
Liquid
Storage
Store at +4°C short term (1-2 weeks). Aliquot and store at -20°C long term. Avoid repeated freeze/thaw cycles.
Epitope
AA 401-500

Target

Full Name
Endoplasmic Reticulum To Nucleus Signaling 1
Introduction
This gene encodes the transmembrane protein kinase inositol-requiring enzyme 1. The encoded protein contains two functional catalytic domains, a serine/threonine-protein kinase domain and an endoribonuclease domain. This protein functions as a sensor of unfolded proteins in the endoplasmic reticulum (ER) and triggers an intracellular signaling pathway termed the unfolded protein response (UPR). The UPR is an ER stress response that is conserved from yeast to mammals and activates genes involved in degrading misfolded proteins, regulating protein synthesis and activating molecular chaperones. This protein specifically mediates the splicing and activation of the stress response transcription factor X-box binding protein 1.
Entrez Gene ID
UniProt ID
Alternative Names
Endoplasmic Reticulum To Nucleus Signaling 1; Serine/Threonine-Protein Kinase/Endoribonuclease IRE1; Inositol-Requiring Protein 1; Inositol-Requiring Enzyme 1; ER To Nucleus Signalling 1; Ire1-Alpha; HIRE1p; IRE1a
Research Area
Serine/threonine-protein kinase and endoribonuclease that acts as a key sensor for the endoplasmic reticulum unfolded protein response (UPR) (PubMed:11779464, PubMed:11175748, PubMed:12637535, PubMed:9637683, PubMed:21317875, PubMed:28128204).

In unstressed cells, the endoplasmic reticulum luminal domain is maintained in its inactive monomeric state by binding to the endoplasmic reticulum chaperone HSPA5/BiP (PubMed:21317875).

Accumulation of misfolded proteins 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 (PubMed:21317875).

The endoribonuclease activity is specific for XBP1 mRNA and excises 26 nucleotides from XBP1 mRNA (PubMed:11779464, PubMed:24508390, PubMed:21317875).

The resulting spliced transcript of XBP1 encodes a transcriptional activator protein that up-regulates expression of UPR target genes (PubMed:11779464, PubMed:24508390, PubMed:21317875).

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 (PubMed:21884936, PubMed:28067262).
Biological Process
Cellular response to glucose stimulus Source: ParkinsonsUK-UCL
Cellular response to hydrogen peroxide Source: Ensembl
Cellular response to unfolded protein Source: ParkinsonsUK-UCL
Cellular response to vascular endothelial growth factor stimulus Source: UniProtKB
Endothelial cell proliferation Source: UniProtKB
Insulin metabolic process Source: ParkinsonsUK-UCL
Intrinsic apoptotic signaling pathway in response to endoplasmic reticulum stress Source: GO_Central
IRE1-mediated unfolded protein response Source: UniProtKB
mRNA catabolic process Source: ParkinsonsUK-UCL
mRNA cleavage Source: UniProtKB
mRNA cleavage involved in mRNA processing Source: ParkinsonsUK-UCL
mRNA splicing, via endonucleolytic cleavage and ligation Source: UniProtKB
Peptidyl-serine autophosphorylation Source: ParkinsonsUK-UCL
Peptidyl-serine trans-autophosphorylation Source: ParkinsonsUK-UCL
Positive regulation of endoplasmic reticulum unfolded protein response Source: UniProtKB
Positive regulation of JUN kinase activity Source: ParkinsonsUK-UCL
Positive regulation of RNA splicing Source: UniProtKB
Positive regulation of vascular associated smooth muscle cell proliferation Source: BHF-UCL
Protein autophosphorylation Source: ParkinsonsUK-UCL
Protein phosphorylation Source: UniProtKB
Regulation of cell cycle Source: UniProtKB
Regulation of macroautophagy Source: ParkinsonsUK-UCL
Response to endoplasmic reticulum stress Source: ParkinsonsUK-UCL
Cellular Location
Endoplasmic reticulum membrane
Topology
Lumenal: 19-443
Helical: 444-464
Cytoplasmic: 465-977
PTM
Autophosphorylated following homodimerization. Autophosphorylation promotes activation of the endoribonuclease domain.
ADP-ribosylated by PARP16 upon ER stress, which increases both kinase and endonuclease activities.

Pandeya, A., Khalko, R. K., Singh, S., Kumar, M., & Gosipatala, S. B. (2022). Hcmv-miR-UL148D regulates the staurosporine-induced apoptosis by targeting the Endoplasmic Reticulum to Nucleus signaling 1 (ERN1). Plos one, 17(9), e0275072.

Baeken, M. W., & Yokobayashi, Y. (2022). Identification of an ERN1 target site within EGFP mRNA. Journal of Cellular Biochemistry, 123(8), 1298-1305.

Minchenko, D. O., Khita, O. O., Tsymbal, D. O., Danilovskyi, S. V., Rudnytska, O. V., Halkin, V., ... & Minchenko, O. H. (2020). Expression of and genes in ERN1 knockdown U87 glioma cells: effect of hypoxia and glucose deprivation. Endocrine Regulations, 54(3), 183-195.

Minchenko, D. O., Tsymbal, D. O., Riabovol, O. O., Viletska, Y. M., Lahanovska, Y. O., Sliusar, M. Y., ... & Minchenko, O. H. (2019). Hypoxic regulation of EDN1, EDNRA, EDNRB, and ECE1 gene expressions in ERN1 knockdown U87 glioma cells. Endocrine regulations, 53(4), 250-262.

Chaurasia, M., Gupta, S., Das, A., Dwarakanath, B. S., Simonsen, A., & Sharma, K. (2019). Radiation induces EIF2AK3/PERK and ERN1/IRE1 mediated pro-survival autophagy. Autophagy, 15(8), 1391-1406.

Riabovol, O. O., Tsymbal, D. O., Minchenko, D. O., Lebid-Biletska, K. M., Sliusar, M. Y., Rudnytska, O. V., & Minchenko, O. H. (2019). Effect of glucose deprivation on the expression of genes encoding glucocorticoid receptor and some related factors in ERN1-knockdown U87 glioma cells. Endocrine Regulations, 53(4), 237-249.

Zhang, K. (2018). The primary unfolded protein response transducer endoplasmic reticulum-to-nucleus signaling 1 is downregulated in livers of human nonalcoholic steatohepatitis patients. Environmental Disease, 3(4), 80.

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For research use only. Not intended for any clinical use.

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