Analytical Data
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Gene name
COASY
- Application
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Alternative Names
NBP; PPAT; DPCK; UKR1; pOV-2; DPCOAK; Phosphopantetheine adenylyltransferase; Dephospho-CoA pyrophosphorylase; Dephospho-CoA kinase; Dephosphocoenzyme A kinase
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Species
Human
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Source
E. coli
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Tag
N-His
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Purity
Greater than 95% as determined by SDS-PAGE.
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Uniprot
Q13057
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Expression Region
Pro101~Ile366
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Molecular Weight
38kDa
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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
COASY (Coenzyme A Synthase), an essential enzyme in the biosynthesis of coenzyme A (CoA), has garnered significant attention in recent years due to its critical role in cellular metabolism and energy production. CoA is vital for various biochemical pathways, including fatty acid metabolism, the citric acid cycle, and the synthesis and degradation of ketone bodies. Its deficiency is associated with numerous metabolic disorders, leading researchers to investigate COASY as a potential therapeutic target. Despite its importance, the structural and functional properties of COASY remain poorly understood. Recent advancements in recombinant protein technology have enabled the expression and purification of COASY, allowing for in-depth studies of its enzymatic mechanisms, interactions with other cellular components, and potential regulation pathways. Understanding the function and regulation of COASY could pave the way for novel therapeutic strategies to combat metabolic diseases linked to CoA deficiency. Furthermore, insights gained from COASY research may also contribute to the broader field of metabolism and mitochondrial function, highlighting the enzyme's significance beyond its immediate biochemical roles. Overall, the study of COASY as a recombinant protein represents a promising avenue for elucidating the complexities of cellular metabolism and identifying new approaches to treat related disorders.
