Analytical Data
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Gene name
cysH
- Application
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Alternative Names
cysH;Phosphoadenosine 5'-phosphosulfate reductase
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Species
E.coli
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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
P17854
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Expression Region
1-244aa
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AA Sequence
MGSSHHHHHHSSGLVPRGSHMSKLDLNALNELPKVDRILALAETNAELEK LDAEGRVAWALDNLPGEYVLSSSFGIQAAVSLHLVNQIRPDIPVILTDTG YLFPETYRFIDELTDKLKLNLKVYRATESAAWQEARYGKLWEQGVEGIEK YNDINKVEPMNRALKELNAQTWFAGLRREQSGSRANLPVLAIQRGVFKVL PIIDWDNRTIYQYLQKHGLKYHPLWDEGYLSVGDTHTTRKWEPGMAEEET RFFGLKRECGLHEG
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Molecular Weight
30 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 the cysH recombinant protein stems from its critical role in the biosynthesis of cofactor molybdenum, an essential element for various enzymatic reactions in organisms. CysH, a known enzyme, is involved in the synthesis of cysteine and the metabolism of sulfur-containing compounds, which are vital for cellular functions and processes such as antioxidant defense and protein synthesis. Given the increasing interest in biotechnological applications and the potential for finding novel therapeutic targets, understanding cysH at the molecular level has gained significant attention. Researchers aim to elucidate its structure-function relationship, optimize its expression in heterologous systems, and explore its kinetic properties and regulatory mechanisms. By producing recombinant cysH, scientists can investigate its enzymatic activity, interactions with other biomolecules, and its impact in various metabolic pathways. This research not only enhances our comprehension of sulfur metabolism but may also lead to advancements in fields like synthetic biology, where engineering microbial strains for bioproduction of pharmaceuticals or biofuels is of prime interest. Furthermore, studying cysH could contribute to the understanding of certain disease mechanisms linked to sulfur metabolism, opening avenues for innovative therapeutic strategies.
