Analytical Data
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Gene name
QSOX1
- Application
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Alternative Names
QSOX1；QSCN6；Sulfhydryl oxidase 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
O00391
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Expression Region
101-175aa
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AA Sequence
CAEETNSAVCRDFNIPGFPTVRFFKAFTKNGSGAVFPVAGADVQTLRERLIDALESHHDTWPPACPPLEPAKLEE
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Molecular Weight
43.4 kDa
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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
QSOX1, or quiescin sulfhydryl oxidase 1, is a highly conserved enzyme that plays a crucial role in oxidative protein folding within the endoplasmic reticulum (ER) by catalyzing the formation of disulfide bonds in nascent polypeptides. Its significance is underscored by its involvement in various biological processes, including cell proliferation, differentiation, and apoptosis, as well as its potential implications in cancer and neurodegenerative diseases. Recent studies have revealed that QSOX1 not only contributes to protein homeostasis but also influences the redox environment of the ER, suggesting a broader role in cellular stress responses. Given its unique enzymatic activity, QSOX1 has drawn attention as a potential therapeutic target and biomarker in diseases associated with protein misfolding. Research into recombinant QSOX1 protein has opened avenues to explore its mechanistic functions, facilitate structural studies, and assess its interaction with various substrates, thereby enhancing our understanding of its role in cellular physiology and pathology. As a result, QSOX1 represents a compelling focus in the field of redox biology, with implications for innovative strategies in treating disease states characterized by protein folding defects.
