Analytical Data
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基因名
mdh
- Application
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别名
mdh;Malate dehydrogenase
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种属
E.coli
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表达系统
E. coli
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标签
His tag N-Terminus
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纯度
Greater than 90% as determined by SDS-PAGE.
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蛋白编号
P61889
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表达区间
1-312aa
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氨基酸序列
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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分子量
35 kDa
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内毒素
< 1.0 EU per μg protein as determined by the LAL method.
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性状
Freeze-dried powder
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缓冲液
PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300.
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复溶方法
Reconstitute in ddH2O to a concentration of 0.1-0.5 mg/mL. Do not vortex.
- 个性化定制
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稳定性测试
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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保存条件 & 期限
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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运输条件
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.
