Cat: PA2000-9392

Recombinant Human MMAB Protein,His

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Analytical Data

  • Gene name

    MMAB

  • Application

    SPRMSTBLIITCELISACELL ASSAYDRUG SCREENING

  • Alternative Names

    aquocob(I)alamin vitamin B12s adenosyltransferase; ATP:cob(I)alamin adenosyltransferase ; ATP:corrinoid adenosyltransferase; ATR ; c-diamide adenosyltransferase; cblB; Cob; Cob(I)alamin adenosyltransferase; Cob(I)yrinic acid a; cob(I)yrinic acid a c diamide adenosyltransferase mitochondrial; Methylmalonic aciduria (cobalamin deficiency) cblB type; Methylmalonic aciduria type B protein; MGC20496; mitochondrial; MMAB; MMAB gene; MMAB_HUMAN; OTTHUMP00000240563; OTTHUMP00000240564

  • Species

    Human

  • Source

    E. coli

  • Tag

    His tag N-Terminus

  • Purity

    Greater than 90% as determined by SDS-PAGE.

  • Uniprot

    Q96EY8

  • Expression Region

    33-250 aa

  • AA Sequence

    QSRGPQGV EDGDRPQPSS KTPRIPKIYT KTGDKGFSST FTGERRPKDD QVFEAVGTTD ELSSAIGFAL ELVTEKGHTF AEELQKIQCT LQDVGSALAT PCSSAREAHL KYTTFKAGPI LELEQWIDKY TSQLPPLTAF ILPSGGKISS ALHFCRAVCR RAERRVVPLV QMGETDANVA KFLNRLSDYL FTLARYAAMK EGNQEKIYMK NDPSAESEGL

  • Molecular Weight

    27.3 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

    Site-directed mutagenesis Custom tag design Custom buffer formulation Custom full-length protein production

  • 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.

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Protein Description

MMAB (Methylmalonate-semialdehyde dehydrogenase) is an essential enzyme involved in the metabolism of branched-chain amino acids, specifically in the catabolism of methylmalonic acid, serving as a critical component in the metabolic pathway that converts methylmalonic acid to succinyl-CoA. Dysfunction or deficiency of the MMAB enzyme is linked to methylmalonic acidemia, a rare genetic disorder characterized by the accumulation of methylmalonic acid in the body, leading to severe metabolic disturbances. This disorder can result in neurological complications, developmental delays, and various health challenges. To address these issues, researchers have focused on the recombinant expression of MMAB proteins using techniques such as bacterial or yeast expression systems, which allows for the large-scale production of the enzyme for further study. The recombinant MMAB proteins can be utilized to investigate their biochemical properties, structure-function relationships, and potential therapeutic applications. Understanding the enzymatic mechanisms and developing effective treatments for methylmalonic acidemia require in-depth studies of MMAB's structure and function, emphasizing the importance of recombinant protein research in elucidating the underlying pathways of this metabolic disorder. By exploring the catalytic activity and regulation of MMAB, researchers hope to devise innovative strategies for managing and potentially curing related metabolic disorders. This body of research not only contributes to our understanding of MMAB itself but also has broader implications for designing enzyme replacement therapies and improving patient outcomes in those affected by metabolic diseases.

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