Analytical Data
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Gene name
SDH1
- Application
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Alternative Names
SDH1; MGG_05059Scytalone dehydratase; SD; SDH; EC 4.2.1.94
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Species
Magnaporthe oryzae
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Source
E. coli
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Tag
N- His-SUMO
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
P56221
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Expression Region
1-172aa
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Molecular Weight
36.2 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
Related Products
Protein Description
SDH1, also known as succinate dehydrogenase subunit A, plays a crucial role in the tricarboxylic acid (TCA) cycle and the electron transport chain, linking mitochondrial respiration to cellular metabolism. Dysregulation of SDH1 has been implicated in various pathological conditions, including certain types of cancer, mitochondrial diseases, and metabolic disorders. The study of SDH1 recombinant protein is significant because it allows for detailed investigation of its biochemical properties, interactions, and regulatory mechanisms within the cell. Advanced techniques such as site-directed mutagenesis and protein crystallization enable researchers to elucidate the structural and functional aspects of SDH1, facilitating the understanding of its role in tumorigenesis and metabolic regulation. Moreover, recombinant SDH1 can be used to explore therapeutic strategies aimed at modulating its activity or targeting related pathways, presenting potential avenues for treating diseases associated with aberrant SDH1 function. By providing insights into the molecular basis of SDH1's activity, research on its recombinant form contributes to the broader understanding of mitochondrial function and its implications in health and disease.
