Human ERN1 protein (Recombinant) (N-His) (STJP003356)
SPECIFICATIONS
HostE.coli
ImmunogenHomo sapiens (Human)
General Information
| Short Description | Recombinant-Human ERN1-N-His protein was developed from e.coli for the region N-His. For use in research applications. |
| Applications | ELISA/Immunogen/SDS-PAGE/WB |
| Host | E.coli |
| Note | STRICTLY FOR FURTHER SCIENTIFIC RESEARCH USE ONLY (RUO). MUST NOT BE USED IN DIAGNOSTIC OR THERAPEUTIC APPLICATIONS. |
Product Properties
| Dilution Range | Reconstitute in sterile water for a stock solution. A copy of datasheet will be provided with the products, please refer to it for details. |
| Formulation | Lyophilized from a solution in PBS pH 7.4, 0.02% NLS, 1mM EDTA, 4% Trehalose, 1% Mannitol. |
| Storage Instruction | Use a manual defrost freezer and avoid repeated freeze thaw cycles. Store at 2 to 8°C for frequent use. Store at-20 to-80°C for twelve months from the date of receipt. |
Target Information
| Gene Symbol | ERN1 |
| Gene ID | 2081 |
| Uniprot ID | ERN1_HUMAN |
| Immunogen | Homo sapiens (Human) |
| Immunogen Region | Phe571-Leu977 |
Additional Info
| Post Translational Modifications | Autophosphorylated following homodimerization. Autophosphorylation promotes activation of the endoribonuclease domain. In response to ER stress, phosphorylated at Ser-724, Ser-729 and possibly Ser-726.phosphorylation promotes oligomerization and endoribonuclease activity. Dephosphorylated at Ser-724, Ser-729 and possibly Ser-726 by RPAP2 to abort failed ER-stress adaptation and trigger apoptosis. Phosphorylated at Ser-724.in response to the ER stressor tunicamycin. ADP-ribosylated by PARP16 upon ER stress, which increases both kinase and endonuclease activities. |
| 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 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. 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. |
| Protein Name | Serine/Threonine-Protein Kinase/Endoribonuclease Ire1Endoplasmic Reticulum-To-Nucleus Signaling 1Inositol-Requiring Protein 1Hire1pIre1-AlphaIre1a Includes - Serine/Threonine-Protein Kinase - Endoribonuclease |
| Database Links | Reactome: R-HSA-381070 |
| Cellular Localisation | Endoplasmic Reticulum MembraneSingle-Pass Type I Membrane Protein |
| Alternative Protein Names | Serine/Threonine-Protein Kinase/Endoribonuclease Ire1 proteinEndoplasmic Reticulum-To-Nucleus Signaling 1 proteinInositol-Requiring Protein 1 proteinHire1p proteinIre1-Alpha proteinIre1a Includes - Serine/Threonine-Protein Kinase - Endoribonuclease proteinERN1 proteinIRE1 protein |
Information sourced from Uniprot.org