Analytical Data
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Gene name
MPST
- Application
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Alternative Names
MPST;TST2;3-mercaptopyruvate sulfurtransferase
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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
P25325
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Expression Region
1-297aa
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AA Sequence
MGSSHHHHHHSSGLVPRGSHMGSHMASPQLCRALVSAQWVAEALRAPRAG QPLQLLDASWYLPKLGRDARREFEERHIPGAAFFDIDQCSDRTSPYDHML PGAEHFAEYAGRLGVGAATHVVIYDASDQGLYSAPRVWWMFRAFGHHAVS LLDGGLRHWLRQNLPLSSGKSQPAPAEFRAQLDPAFIKTYEDIKENLESR RFQVVDSRATGRFRGTEPEPRDGIEPGHIPGTVNIPFTDFLSQEGLEKSP EEIRHLFQEKKVDLSKPLVATCGSGVTACHVALGAYLCGKPDVPIYDGSW VEWYMRARPEDVISEGRGKTH
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Molecular Weight
35 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 study of MPST (Mercaptopyruvate Sulfurtransferase) recombinant proteins has gained attention due to their significant role in sulfur metabolism and cellular antioxidant defense mechanisms. MPST is an enzyme that catalyzes the transfer of sulfur from mercaptopyruvate to various acceptors, playing an essential role in the biosynthesis of hydrogen sulfide, a crucial signaling molecule. Understanding the structure and function of MPST is vital for comprehending its involvement in various physiological processes and diseases, including neurodegeneration, cancer, and metabolic disorders. Recombinant MPST proteins are valuable tools for elucidating the enzyme's biochemical pathways and developing potential therapeutic strategies. Previous research has shown that MPST exhibits unique properties that may vary across species, emphasizing the need for detailed studies of its recombinant forms. These efforts aim to enhance our understanding of sulfur metabolism and its implications for health and disease, paving the way for innovative approaches in drug development and metabolic engineering. As the field continues to explore the multifaceted roles of sulfur-containing compounds, MPST recombinant proteins stand out as a critical focus for advancing biochemical research and therapeutic applications.
