Analytical Data
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Gene name
OSTM1
- Application
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Alternative Names
GL; GIPN; Chloride channel 7 beta subunit
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Species
Human
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Source
E. coli
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Tag
N-His
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
Q86WC4
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Expression Region
Gln120~Gly251
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Molecular Weight
18kDa
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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
OSTM1 (Oligosaccharyltransferase Multimerization 1) is a crucial protein involved in the process of glycosylation, specifically in the transfer of oligosaccharides to nascent proteins within the endoplasmic reticulum. This process is essential for proper protein folding, stability, and function, making OSTM1 significant for cellular homeostasis and overall organismal health. Mutations or dysregulation of OSTM1 have been implicated in various diseases, including certain forms of cancer and congenital disorders. Moreover, its role in the endoplasmic reticulum-associated degradation (ERAD) pathway highlights its importance in maintaining cellular quality control mechanisms. Research on OSTM1 recombinant proteins focuses on understanding its structural dynamics, interaction with glycosylation machinery, and functional implications in disease contexts. By producing OSTM1 as a recombinant protein, researchers aim to elucidate its biochemical properties, regulatory mechanisms, and potential therapeutic targets. This study not only contributes to the fundamental knowledge of glycosylation processes but also paves the way for the development of innovative strategies for treating diseases linked to OSTM1 dysregulation. Through advanced techniques like crystallography and NMR, insights gained from OSTM1 studies can revolutionize our understanding of protein maturation and stability, leading to novel approaches in biomedicine and biotechnology.
