Analytical Data
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Gene name
mdh
- Application
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Alternative Names
mdh;Malate dehydrogenase
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Species
E.coli
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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
P61889
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Expression Region
1-312aa
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AA Sequence
MGSSHHHHHH SSGLVPRGSH MGSHMKVAVL GAAGGIGQAL ALLLKTQLPS GSELSLYDIA PVTPGVAVDL SHIPTAVKIK GFSGEDATPA LEGADVVLIS AGVARKPGMD RSDLFNVNAG IVKNLVQQVA KTCPKACIGI ITNPVNTTVA IAAEVLKKAG VYDKNKLFGV TTLDIIRSNT FVAELKGKQP GEVEVPVIGG HSGVTILPLL SQVPGVSFTE QEVADLTKRI QNAGTEVVEA KAGGGSATLS MGQAAARFGL SLVRALQGEQ GVVECAYVEG DGQYARFFSQ PLLLGKNGVE ERKSIGTLSA FEQNALEGML DTLKKDIALG EEFVNK
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Molecular Weight
35 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
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Protein Description
The study of MDH (malate dehydrogenase) recombinant proteins has garnered significant attention due to their pivotal role in various metabolic pathways, particularly in the tricarboxylic acid (TCA) cycle, which is fundamental for cellular energy production. MDH enzymes catalyze the reversible oxidation of malate to oxaloacetate, playing a critical role in cellular respiration and biosynthesis. Given their importance in health and disease, particularly in metabolic disorders and cancer, researchers are focused on characterizing MDH proteins to understand their functional mechanisms and interactions. The use of recombinant technology not only allows for the production of MDH proteins in a more controlled manner but also facilitates the study of their structure-function relationships. This is essential for exploring potential therapeutic avenues, as engineered MDH proteins may provide insights into drug design or serve as novel therapeutic agents. Furthermore, studying MDH at a molecular level can reveal evolutionary adaptations in different organisms, enhancing our understanding of metabolic plasticity. Overall, the research on MDH recombinant proteins is vital for elucidating metabolic processes and developing strategies to manipulate these pathways for therapeutic benefits.
