Analytical Data
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Gene name
XBP1
- Application
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Alternative Names
XBP1；TREB5；XBP2；X-box-binding Protein 1
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Species
Human
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Source
E. coli
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Tag
His tag N-Terminus
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
P17861
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Expression Region
1-185aa
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AA Sequence
MVVVAAAPNPADGTPKVLLLSGQPASAAGAPAGQALPLMVPAQRGASPEAASGGLPQARKRQRLTHLSPEEKALRRKLKNRVAAQTARDRKKARMSELEQQVVDLEEENQKLLLENQLLREKTHGLVVENQELRQRLGMDALVAEEEAEAKGNEVRPVAGSAESAALRLRAPLQQVQAQLSPLQN
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Endotoxin
< 1.0 EU per μg protein as determined by the LAL method.
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Form
Freeze-dried powder
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Buffer formulation
PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300.
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Reconstitution
Reconstitute in ddH2O to a concentration of 0.1-0.5 mg/mL. Do not vortex.
- Customization
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Stability Test
The thermal stability is described by the loss rate. The loss rate was determined by accelerated thermal degradation test, that is, incubate the protein at 37℃ for 48h, and no obvious degradation and precipitation were observed. The loss rate isless than 8% within the expiration date under appropriate storage condition.
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Storage & Shelf Life
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.
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Shipping
In general, recombinant proteins are supplied as lyophilized powder and shipped at ambient temperature. For bulk packages, the proteins are provided as frozen liquid and shipped with blue ice, unless otherwise requested by the customer.
Quality inspection process
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Protein Description
XBP1 (X-box binding protein 1) is a crucial transcription factor that plays a significant role in the unfolded protein response (UPR), a cellular stress response activated by the accumulation of misfolded proteins in the endoplasmic reticulum (ER). The UPR is vital for maintaining cellular homeostasis, and XBP1 is particularly important in orchestrating adaptive responses to ER stress. In mammals, XBP1 is initially expressed as an unactivated mRNA transcript, which undergoes unconventional splicing by the enzyme IRE1α during ER stress, resulting in a functional form that can regulate genes involved in protein folding, secretion, and degradation. Abnormal XBP1 activity has been linked to various diseases, including cancer, neurodegenerative disorders, and metabolic syndromes, making it a potential therapeutic target. Recent studies have focused on the production and characterization of recombinant XBP1 proteins to better understand its structure, function, and regulatory mechanisms. Researchers are leveraging recombinant DNA technology to generate XBP1 variants, enabling detailed studies on its interaction with target genes and other molecular partners in the UPR pathway. This research not only enhances our understanding of the molecular basis of ER stress responses but also opens avenues for developing novel therapeutics aimed at modulating XBP1 activity in disease contexts, providing a significant contribution to the fields of cell biology and molecular medicine.
