Analytical Data
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Gene name
sucC
- Application
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Alternative Names
(Succinyl-CoA synthetase subunit beta)(SCS-beta)
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Species
strain U112
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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
A0Q5H4
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Expression Region
1-387aa
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Molecular Weight
49.0 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
The study of the sucC gene, which encodes the enzyme succinyl-CoA synthetase, is significant due to its role in the tricarboxylic acid (TCA) cycle, a fundamental metabolic pathway in various organisms, including bacteria, plants, and animals. Succinyl-CoA synthetase catalyzes the reversible conversion of succinyl-CoA to succinate while generating GTP or ATP, thus playing a crucial role in energy production and biosynthetic processes. In recent years, the recombinant expression of sucC has garnered attention for its potential applications in bioengineering and biotechnology. By utilizing recombinant DNA technology, researchers can produce large quantities of the sucC protein, which facilitates in-depth studies of its enzymatic activity, structural characteristics, and regulation. Furthermore, understanding the functional properties of sucC can lead to advancements in metabolic engineering strategies aimed at enhancing the production of biofuels and biochemicals from renewable resources. Additionally, the manipulation of this pathway can have implications for improving plant growth and stress responses in agricultural systems. Overall, the research on sucC and its recombinant protein expression is essential for unraveling the complexities of cellular metabolism and for developing innovative solutions to address global energy and sustainability challenges.
