Analytical Data
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Gene name
MCAD
- Application
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Alternative Names
MCAD; MCADH; ACAD1; Medium-chain specific acyl-CoA dehydrogenase, mitochondrial
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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
P11310
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Expression Region
Trp191~Asn421
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Molecular Weight
29kDa
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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
The study of MCAD (Medium-Chain Acyl-CoA Dehydrogenase) protein restructuring has gained significant attention in the field of metabolic disorders and enzymology. MCAD is an essential enzyme involved in the mitochondrial beta-oxidation of medium-chain fatty acids, and its deficiency can lead to severe metabolic crises, especially in infants. Understanding the structure and function of MCAD is crucial for developing targeted therapies for disorders arising from its deficiency. Research has been focused on the protein's conformational stability, enzymatic activity, and interaction with substrates and inhibitors. Moreover, advances in techniques like X-ray crystallography and cryo-electron microscopy have enabled researchers to visualize the intricate details of its three-dimensional structure, revealing how mutations can affect its functionality. The exploration of MCAD's catalytic mechanism and regulatory pathways not only enhances our comprehension of fatty acid metabolism but also opens avenues for therapeutic interventions in metabolic diseases. Continued investigation into the structural dynamics of MCAD will provide insights into potential drug design and management strategies for affected individuals.
