Analytical Data
-
Gene name
MMAA
- Application
-
Alternative Names
MMAAMethylmalonic aciduria type A protein; mitochondrial; EC 3.6.-.-
-
Species
Human
-
Source
E. coli
-
Tag
His tag N-Terminus
-
Purity
Greater than 90% as determined by SDS-PAGE.
-
Uniprot
Q8IVH4
-
Expression Region
66-418 aa
-
AA Sequence
CVQTT LKDHTEGLSD KEQRFVDKLY TGLIQGQRAC LAEAITLVES THSRKKELAQ VLLQKVLLYH REQEQSNKGK PLAFRVGLSG PPGAGKSTFI EYFGKMLTER GHKLSVLAVD PSSCTSGGSL LGDKTRMTEL SRDMNAYIRP SPTRGTLGGV TRTTNEAILL CEGAGYDIIL IETVGVGQSE FAVADMVDMF VLLLPPAGGD ELQGIKRGII EMADLVAVTK SDGDLIVPAR RIQAEYVSAL KLLRKRSQVW KPKVIRISAR SGEGISEMWD KMKDFQDLML ASGELTAKRR KQQKVWMWNL IQESVLEHFR THPTVREQIP LLEQKVLIGA LSPGLAADFL LKAFKSRD
-
Molecular Weight
46.5 kDa
-
Endotoxin
< 1.0 EU per μg protein as determined by the LAL method.
-
Form
Freeze-dried powder
-
Buffer formulation
PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300.
-
Reconstitution
Reconstitute in ddH2O to a concentration of 0.1-0.5 mg/mL. Do not vortex.
- Customization
-
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.
-
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.
-
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
MMAA (Methylmalonic Aciduria Associated Protein) is a key protein of interest in the study of metabolic disorders, particularly those related to methylmalonic aciduria, a rare inherited condition affecting the metabolism of certain amino acids and lipids. Individuals with this condition often experience a deficiency in the enzyme methylmalonyl-CoA mutase, which is crucial for the conversion of methylmalonyl-CoA into succinyl-CoA, leading to the accumulation of toxic levels of methylmalonic acid in the body. Research on MMAA focuses on understanding its structure, function, and the molecular mechanisms underlying its role in metabolic pathways. This protein is also implicated in cellular processes beyond metabolism, including cell signaling and stress responses. Advances in biophysical techniques, including X-ray crystallography and NMR spectroscopy, have facilitated a deeper understanding of MMAA's structure-function relationship. By unraveling the biochemical pathways and genetic mutations associated with MMAA, researchers aim to develop targeted therapies and management strategies to alleviate the symptoms associated with methylmalonic aciduria, ultimately improving the quality of life for affected individuals. Furthermore, insights gained from MMAA studies may have broader implications for understanding related metabolic disorders, making it a vital area of research in biomedical sciences.
