Analytical Data
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Gene name
MMA
- Application
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Alternative Names
MMA；Glutathione S-transferase omega-2
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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
P78417
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Expression Region
2-241aa
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AA Sequence
SGESARSLG KGSAPPGPVP EGSIRIYSMR FCPFAERTRL VLKAKGIRHE VININLKNKP EWFFKKNPFG LVPVLENSQG QLIYESAITC EYLDEAYPGK KLLPDDPYEK ACQKMILELF SKVPSLVGSF IRSQNKEDYA GLKEEFRKEF TKLEEVLTNK KTTFFGGNSI SMIDYLIWPW FERLEAMKLN ECVDHTPKLK LWMAAMKEDP TVSALLTSEK DWQGFLELYL QNSPEACDYG L
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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
MMA (Methylmalonic Acidemia) is a genetic disorder resulting from a deficiency in the enzyme mutase, which is crucial for the metabolism of certain fatty acids and amino acids. This condition leads to the accumulation of methylmalonic acid in the body, causing various metabolic disturbances and severe health issues, including developmental delays and neurological complications. Research into MMA has increasingly focused on the potential for recombinant proteins, such as the development of engineered forms of the human mutase enzyme, to provide therapeutic solutions. These recombinant proteins can be designed to enhance enzymatic activity, improve stability, and facilitate cellular uptake, thereby potentially alleviating the biochemical imbalances caused by the deficiency. Advances in molecular biology techniques, including genetic engineering and protein expression systems, have allowed for the production of these proteins in sufficient quantities for therapeutic use. Ongoing studies aim to evaluate the effectiveness and safety of these interventions in clinical settings, addressing not only the metabolic aspects of MMA but also the broader implications for gene therapy and enzyme replacement strategies. The ultimate goal of MMA recombinant protein research is to offer a viable treatment option that can significantly improve the quality of life for individuals affected by this challenging disorder.
