Analytical Data
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Gene name
T131A
- Application
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Alternative Names
UV excision repair protein RAD23 homolog A(HR23A)(hHR23A)
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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
P54725
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Expression Region
1-362aa(T131A)
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Molecular Weight
47.0 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 T131A recombinant protein is a variant of a specific protein that has garnered attention in the field of molecular biology and biochemistry due to its potential implications in understanding protein function and interaction. This protein variant is created by site-directed mutagenesis, where the threonine residue at position 131 is replaced with alanine. This modification is significant as it can alter the protein's structural and functional properties, thereby providing insights into the role of this residue in the protein's biological activity. Research surrounding T131A has focused on its effects on protein stability, enzyme activity, and interaction with other biomolecules. Studies have shown that such mutations can lead to changes in enzymatic efficiency and substrate specificity, making it crucial for investigating metabolic pathways and signaling mechanisms. Moreover, understanding the implications of the T131A mutation can aid in the design of therapeutic agents by providing a clearer picture of how specific modifications can influence protein behavior. Overall, the study of T131A recombinant protein serves as a vital tool for unraveling the complexities of protein function and its applications in biotechnology and medicine.
