Analytical Data
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Gene name
MMUT
- Application
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Alternative Names
Methylmalonyl-CoA isomerase
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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 90% as determined by SDS-PAGE.
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Uniprot
P22033
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Expression Region
33-750aa
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Molecular Weight
84.8 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
Research on recombinant MMUT (methylmalonyl-CoA mutase) has gained significant attention due to its crucial role in the metabolism of branched-chain amino acids and the catabolism of certain fatty acids. MMUT is an important enzyme encoded by the MUT gene, which is responsible for converting methylmalonyl-CoA to succinyl-CoA, a key step in the metabolic pathway that provides energy and precursors for biosynthetic processes. Deficiency in this enzyme can lead to methylmalonic acidemia (MMA), a metabolic disorder characterized by the accumulation of methylmalonic acid in the blood, causing severe neurological and developmental issues. Understanding the structure and function of recombinant MMUT is essential for developing therapeutic strategies to manage MMA and improve patient outcomes. Advances in recombinant DNA technology have facilitated the production of functional MMUT from various expression systems, allowing researchers to study its biochemical properties, enzymatic mechanisms, and interactions with other metabolic components. Furthermore, the availability of recombinant MMUT provides a valuable tool for the development of enzyme replacement therapies and novel clinical interventions. Overall, the investigation of MMUT at the molecular level not only enhances our understanding of metabolic regulation but also opens pathways for innovative treatments for metabolic disorders associated with its deficiency.
