Analytical Data
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Gene name
MCEE
- Application
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Alternative Names
MCEE;Methylmalonyl-CoA epimerase. mitochondrial
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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
Q96PE7
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Expression Region
37-176aa
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AA Sequence
MGSSHHHHHHSSGLVPRGSHMQVTGSVWNLGRLNHVAIAVPDLEKAAAFY KNILGAQVSEAVPLPEHGVSVVFVNLGNTKMELLHPLGRDSPIAGFLQKN KAGGMHHICIEVDNINAAVMDLKKKKIRSLSEEVKIGAHGKPVIFLHPKD CGGVLVELEQA
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Molecular Weight
17 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
The study of MCEE (Methylmalonyl-CoA Epimerase) recombinant proteins has garnered significant attention in recent years due to the enzyme's crucial role in the metabolism of branched-chain amino acids and the catabolism of certain fatty acids. MCEE catalyzes the conversion of methylmalonyl-CoA to succinyl-CoA, which is essential in the pathway of propionate metabolism in both prokaryotic and eukaryotic organisms. Deficiencies in MCEE can lead to metabolic disorders, resulting in the accumulation of toxic metabolites and subsequently severe health issues. Recombinant protein technology has emerged as a powerful tool to produce MCEE in vitro, allowing researchers to obtain large quantities of the enzyme for detailed biochemical characterization, structure elucidation, and functional studies. This research has implications not only for understanding fundamental biological processes but also for developing potential therapeutic interventions for metabolic disorders associated with MCEE dysfunction. By optimizing expression systems and purification strategies, scientists aim to explore the enzyme's kinetic properties, investigate its interactions with cofactors, and assess its stability under various conditions. Furthermore, the availability of recombinant MCEE opens avenues for high-throughput screening of small molecules that could modulate its activity, paving the way for drug discovery efforts aimed at addressing metabolic diseases linked to MCEE deficiencies.
