Analytical Data
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Gene name
GSTa5
- Application
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Alternative Names
GSTa5；Glutathione S-transferase A5
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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
Q7RTV2
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Expression Region
2-222aa
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AA Sequence
AEKPKLHYS NARGSMESIR WLLAAAGVEL EEKFLESAED LDKLRNDGSL LFQQVPMVEI DGMKLVQTRA ILNYIASKYN LYGKDMKERA LIDMYTEGIV DLTEMILLLL ICQPEERDAK TALVKEKIKN RYFPAFEKVL KSHRQDYLVG NKLSWADIHL VELFYYVEEL DSSLISSFPL LKALKTRISN LPTVKKFLQP GSQRKPPMDE KSLEEARKIF RF
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Molecular Weight
25.7 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
GSTa5 is a glutathione S-transferase that has garnered significant attention in the field of protein research due to its role in various biochemical processes, including detoxification and cellular defense mechanisms. As a member of the GST family, GSTa5 is involved in the conjugation of glutathione to a wide range of hydrophobic and electrophilic substrates, facilitating their excretion and thereby protecting cells from potential damage caused by toxic compounds. The study of GSTa5 is particularly relevant for understanding drug metabolism, as alterations in its expression can influence the efficacy and toxicity of pharmaceutical agents. Furthermore, researchers have focused on the recombinant expression of GSTa5 to develop robust experimental models for functional assays, structural studies, and potential therapeutic applications. By utilizing techniques such as molecular cloning and protein engineering, scientists aim to produce high yields of purified GSTa5 for biochemical characterization. This research not only advances our understanding of GSTa5's molecular mechanisms but also holds promise for novel strategies in drug design and personalized medicine, where modulation of GST activity could lead to improved therapeutic outcomes. The exploration of GSTa5 as a biomarker for certain diseases is also an emerging area of interest, highlighting its potential role in diagnostics and targeted therapies. Overall, the ongoing investigation into GSTa5 and its recombinant forms underscores the enzyme's significance in molecular biology and pharmacology, paving the way for innovative applications in biotechnology and medicine.
