Analytical Data
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Gene name
R386Q
- Application
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Alternative Names
/
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Species
Human
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Source
Baculovirus
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Tag
N- His & C- Myc
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
P00747
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Expression Region
20-810aa(R386Q)
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Molecular Weight
92.3 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
Related Products
Protein Description
The R386Q variant of a recombinant protein has garnered attention in recent years due to its potential implications in understanding various biological processes and disease mechanisms. This specific mutation, located in a region known to influence protein stability and function, has been linked to alterations in enzymatic activity and binding interactions. Research has shown that such mutations can affect protein folding, leading to misfolded structures associated with diseases, including neurodegenerative disorders. Additionally, the study of the R386Q variant provides insights into the mechanisms of protein aggregation, as well as offers a platform for developing novel therapeutic strategies targeting these altered pathways. In the context of recombinant protein production, the R386Q variant presents an opportunity to elucidate the effects of single amino acid changes on the overall functionality of the protein, thereby enhancing our understanding of protein engineering and design. Investigating this variant could also pave the way for advancements in biopharmaceuticals, as optimizing protein characteristics through targeted mutations may lead to more effective treatments.
