Analytical Data
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Gene name
cysK
- Application
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Alternative Names
((thiol)-lyase A)(OAS-TL A)(O-acetylserine-specific cysteine synthase)(Sulfide-dependent cysteine synthase)
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Species
Mycobacterium bovis
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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
P0A535
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Expression Region
1-310aa
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Molecular Weight
40.2 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
CysK (cystathionine γ-synthase) is an essential enzyme involved in the transsulfuration pathway, a critical metabolic route that converts homocysteine to cysteine, an important amino acid. The dysfunction of this pathway has been linked to various health issues, including cardiovascular diseases and neurodegenerative disorders. Furthermore, cysteine plays a pivotal role in the synthesis of glutathione, an antioxidant that protects cells against oxidative stress. As such, studying CysK and its recombinant protein provides valuable insights into amino acid metabolism and offers potential therapeutic targets. The production and characterization of recombinant CysK can facilitate the exploration of its enzymatic properties, regulation mechanisms, and interactions with other proteins. Current research is focused on optimizing expression systems to produce high yields of functional CysK, along with investigating its structural characteristics through techniques like X-ray crystallography or nuclear magnetic resonance (NMR). These studies aim to unravel the intricacies of its catalytic mechanism and its role within metabolic pathways, ultimately advancing our understanding of related diseases and supporting the development of clinical interventions. The ongoing research into CysK recombinant proteins promises to contribute significantly to biochemistry and medical sciences, shedding light on how modulating this enzyme could influence metabolic health.
