IRE1 Protein, Human (sf9)

IRE1 is a key serine/threonine protein kinase and endoribonuclease essential for sensing the unfolded protein response (UPR) in the endoplasmic reticulum. In cellular homeostasis, it remains monomeric by binding to HSPA5/BiP. IRE1 Protein, Human (sf9) is the recombinant human-derived IRE1 protein, expressed by Sf9 insect cells , with tag free.

IRE1, a serine/threonine-protein kinase and endoribonuclease, serves as a pivotal sensor in the endoplasmic reticulum unfolded protein response (UPR). In the absence of cellular stress, the endoplasmic reticulum luminal domain maintains its inactive monomeric state through binding to the endoplasmic reticulum chaperone HSPA5/BiP. Upon the accumulation of misfolded proteins, the release of HSPA5/BiP allows the luminal domain to homodimerize, facilitating autophosphorylation of the kinase domain and subsequent activation of the endoribonuclease activity. This endoribonuclease activity is specific to XBP1 mRNA, excising 26 nucleotides from the XBP1 transcript. The resulting spliced XBP1 transcript encodes a transcriptional activator that up-regulates the expression of UPR target genes. Beyond its role in the UPR, IRE1 acts as an upstream signal for ER stress-induced GORASP2-mediated unconventional trafficking of CFTR to the cell membrane by modulating the expression and localization of SEC16A, highlighting its involvement in diverse cellular processes beyond the UPR.

1.The kinase activity of this recombinant protein is testing in progress, we cannot offer a guarantee yet.
2.Measured by its nuclease activity to cleave Xbp1 single stem-loop mini-substrate.

Human

Sf9 insect cells

Tag Free

O75460-1 (P465-L977)

2081  [NCBI]

Cytoplasmic Domain

PLSMHQQQQLQHQQFQKELEKIQLLQQQQQQLPFHPPGDTAQDGELLDTSGPYSESSGTSSPSTSPRASNHSLCSGSSASKAGSSPSLEQDDGDEETSVVIVGKISFCPKDVLGHGAEGTIVYRGMFDNRDVAVKRILPECFSFADREVQLLRESDEHPNVIRYFCTEKDRQFQYIAIELCAATLQEYVEQKDFAHLGLEPITLLQQTTSGLAHLHSLNIVHRDLKPHNILISMPNAHGKIKAMISDFGLCKKLAVGRHSFSRRSGVPGTEGWIAPEMLSEDCKENPTYTVDIFSAGCVFYYVISEGSHPFGKSLQRQANILLGACSLDCLHPEKHEDVIARELIEKMIAMDPQKRPSAKHVLKHPFFWSLEKQLQFFQDVSDRIEKESLDGPIVKQLERGGRAVVKMDWRENITVPLQTDLRKFRTYKGGSVRDLLRAMRNKKHHYRELPAEVRETLGSLPDDFVCYFTSRFPHLLAHTYRAMELCSHERLFQPYYFHEPPEPQPPVTPDAL

Approximately 65 kDa, based on SDS-PAGE under reducing conditions, due to the glycosylation.

≥ 80%, as determined by reducing SDS-PAGE.

Solution.

1.Supplied as a 0.22 μm filtered solution of 20 mM Tris, 500 mM NaCl, 10% glycerol, pH 7.4.
2.Supplied as a 0.22 μm filtered solution of 20 mM Tris, 500 mM NaCl, 10% Glycerol, pH 7.5, 0.5 mM TCEP.
Note: For SPR assay, please replace the buffer. Primary amine components (e.g., Tris, imidazole) can affect protein-coupled chips.
Please refer to the lot-specific COA for specific buffer information.

<1 EU/μg, determined by LAL method.

Please use rapid thawing with running water to thaw the protein.

Stored at -80°C for 1 year from date of receipt. It is stable at -20°C for 3 months after opening. It is recommended to freeze aliquots at -80°C for extended storage. Avoid repeated freeze-thaw cycles.

Shipping with dry ice.