Analytical Data
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Gene name
sucC
- Application
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Alternative Names
sucC；scsB；Succinate--CoA ligase [GDP-forming] subunit beta
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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
A0Q5H4
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Expression Region
1-387aa
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AA Sequence
MNLHEYQAKDLLESYGLKVQKGIVAHNPNEAAQAFDQLGGKFAVVKAQVHAGGRGKAGGVKVVKSSQEAREVAESLIGKNLVTFQTDAEGQPVNSVGVFEDVYPVTRELYLGAVVDRSSRKVTFMASTEGGVDIEEVAHNSPEKILKVEVDPLVGLQPFQAREVAFKLGLEGKQINDFVKTMLGAYKAFIECDFALFEINPLAVRENGEIVCVDGKINLDSNALYRHPKLLALRDKSQENAKELKASEHELNYVALEGNIGCMVNGAGLAMATMDIIQLYGGKPANFLDVGGGATKERVIEAFKLILDDENVKAVLINIFGGIVRCDMIAEAIIEAVKEVNVTVPVVVRLEGNNAEKGAKILADSGLKLIPADGLADAADKVVKSLG
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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 sucC recombinant protein has garnered significant attention due to its crucial role in the metabolic pathways of various microorganisms. SucC, a subunit of the succinyl-CoA synthetase enzyme complex, is involved in the conversion of succinyl-CoA to succinate, facilitating energy production and carbon metabolism. Understanding the function and regulation of sucC is essential for biotechnological applications, such as biofuel production and fermentation processes, as it directly influences the efficiency of organic acid production. Additionally, investigating sucC can provide insights into the metabolic engineering of microorganisms for improved yields in industrial processes. The recombinant expression of sucC allows for detailed functional studies and structural analyses, paving the way for potential applications in synthetic biology. Furthermore, the ability to manipulate sucC expression can lead to the development of strains with enhanced metabolic capabilities, offering solutions to current challenges in sustainable production. Thus, research on sucC recombinant protein not only expands our fundamental knowledge of microbial metabolism but also holds promising implications for various industrial applications.
