Analytical Data
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Gene name
sspP
- Application
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Alternative Names
Staphopain A(EC 3.4.22.48)(Staphylococcal cysteine proteinase A)(Staphylopain A)
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Species
Staphylococcus aureus
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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
P81297
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Expression Region
215-388aa
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Molecular Weight
27.4 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 research on the recombinant protein SSPP (S-formylglutathione hydrolase) stems from its potential applications in biotechnology and medicine. SSPP is an enzyme involved in the metabolic pathway of glutathione, a critical antioxidant that protects cells from oxidative stress and maintains redox homeostasis. The manipulation and study of SSPP through recombinant DNA technology offer insights into its structure-function relationships and catalytic mechanisms. Additionally, understanding the role of SSPP in disease processes, particularly those related to oxidative damage and cellular stress, provides avenues for therapeutic interventions. Given the increasing prevalence of conditions associated with oxidative stress, such as neurodegenerative diseases and cancer, the ability to produce recombinant SSPP can facilitate the development of novel inhibitors or modulators that could have significant therapeutic implications. Moreover, the recombinant production system allows for large-scale availability and the possibility of post-translational modifications, which are essential for the enzyme's functionality. Hence, investigating SSPP as a recombinant protein not only enhances our fundamental understanding of this critical enzyme but also contributes to potential biomedical advancements.
