Analytical Data
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Gene name
T484A,V541A
- Application
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Alternative Names
SH2B adapter protein 1(Pro-rich, PH and SH2 domain-containing signaling mediator)(PSM)(SH2 domain-containing protein 1B)
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Species
Human
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Source
E. coli
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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
Q9NRF2
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Expression Region
246-671aa(T484A,V541A)
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Molecular Weight
52.9 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
The T484A and V541A mutations in recombinant proteins have garnered significant interest in recent years due to their potential effects on protein stability, functionality, and interactions. These mutations are often introduced to explore the relationship between protein structure and function, providing insights into mechanisms that govern enzymatic activity and binding affinities. For instance, amino acid alterations at these positions can influence the conformational dynamics of proteins, potentially enhancing or diminishing their effectiveness in specific applications such as therapeutic development or biocatalysis. By studying T484A and V541A variants, researchers aim to elucidate key structural features that contribute to the functional properties of recombinant proteins. This research is particularly pertinent in fields such as biotechnology and pharmaceuticals, where engineered proteins are crucial for the development of novel treatments or industrial processes. Understanding the implications of these mutations can lead to the design of more robust and efficient proteins, ultimately improving the efficacy and stability of therapeutic agents.
