Name :
Recombinant Human IRE1 Protein (aa 465-977), HPLC-verified
Biological Activity :
Background :
Endoplasmic reticulum stress and hypoxia are necessary components of malignant tumors growth and suppression of ERN1 (from endoplasmic reticulum to nuclei-1) signalling pathway, which is linked to the apoptosis and cell death processes, significantly decreases proliferative processes. An enhanced expression of TP53 gene in ERN1 knockdown glioma cells correlates with the decreased level of ubiquitin ligase MDM2 and increased expression level of USP7 which deubiquitinates TP53 and MDM2 and induces TP53-dependent cell growth repression and apoptosis. Thus, the expression of genes encoding TP53 and related to TP53 factors depends upon the endoplasmic reticulum stress signaling as well as on hypoxia, and correlates with suppression of glioma growth under ERN1 knockdown. The dependence of insulin-like growth binding proteins as well as IGF2BP3 and HTRA1 gene expressions in U87 glioma cells on ERN1 signaling enzyme function and hypoxia, indicating its participation in the regulation of metabolic and proliferative processes via IGF/INS receptors, because endoplasmic reticulum stress is an important component of tumor growth and metabolic diseases.
Biological Activity :
1. Kinase activity untested2. Measured by its nuclease activity to cleave Xbp1 single stem-loop mini-substrate.
Expression Host :
Human
Source :
Baculovirus-Insect Cells
Tag :
Protein Accession No. :
O75460-1
NCBI Gene ID :
Synonyms :
Synonyms :
endoplasmic reticulum to nucleus signaling 1
Amino Acid Sequence :
Molecular Weight :
The secreted recombinant human ERN1 consists of 515 amino acids and predicts a molecular mass of 58.3 KDa. The apparent molecular mass of the protein is approximately 65 KDa in SDS-PAGE under reducing conditions due to glycosylation.
Purity :
≥ 80 % as determined by SDS-PAGE. ≥ 90 % as determined by SEC-HPLC.
State of Matter :
Product Concentration :
Storage and Stability :
Samples are stable for up to twelve months from date of receipt at -20℃ to -80℃. Store it under sterile conditions at -20℃ to -80℃. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.
Endotoxin Level :
< 1.0 EU per μg of the protein as determined by the LAL method
Protein Construction :
A DNA sequence encoding the human ERN1 (O75460-1) (Pro 465-Leu 977) was expressed and purified with two additional amino acids (Gly & Pro ) at the N-terminus.
Buffer Solution :
Supplied as sterile 20mM Tris, 500mM NaCl, 10% glycerol, pH 7.4.Please contact us for any concerns or special requirements.Please refer to the specific buffer information in the hardcopy of datasheet.
Shipping :
Kinases are highly recommended to be shipped at frozen temperature with blue ice or dry ice.Shipment made at ambient temperature may seriously affect the activity of the ordered products.
Redissolution :
A hardcopy of COA with reconstitution instruction is sent along with the products. Please refer to it for detailed information.
Synonyms :
hIRE1p Protein, Human; IRE1 Protein, Human; IRE1a Protein, Human; IRE1P Protein, Human IRE1 背景信息 Endoplasmic reticulum stress and hypoxia are necessary components of malignant tumors growth and suppression of ERN1 (from endoplasmic reticulum to nuclei-1) signalling pathway, which is linked to the apoptosis and cell death processes, significantly decreases proliferative processes. An enhanced expression of TP53 gene in ERN1 knockdown glioma cells correlates with the decreased level of ubiquitin ligase MDM2 and increased expression level of USP7 which deubiquitinates TP53 and MDM2 and induces TP53-dependent cell growth repression and apoptosis. Thus, the expression of genes encoding TP53 and related to TP53 factors depends upon the endoplasmic reticulum stress signaling as well as on hypoxia, and correlates with suppression of glioma growth under ERN1 knockdown. The dependence of insulin-like growth binding proteins as well as IGF2BP3 and HTRA1 gene expressions in U87 glioma cells on ERN1 signaling enzyme function and hypoxia, indicating its participation in the regulation of metabolic and proliferative processes via IGF/INS receptors, because endoplasmic reticulum stress is an important component of tumor growth and metabolic diseases.
References & Citations :
Trentmann,S.M. et al., 2000, Plant Mol Biol. 44 (1):11-25. Iwawaki T., et al., 2001, Nat. Cell Biol. 3:158-64. Liu C.Y., et al., 2003, J. Biol. Chem. 278:17680-7. Oppermann F.S., et al., 2009, Mol. Cell. Proteomics 8:1751-64.
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