Analytical Data
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基因名
CMAS
- Application
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别名
CMAS; CMP N acetylneuraminic acid synthase; CMP Neu5Ac synthetase; CMP NeuNAc synthetase; CMP sialic acid synthetase; CMP-N-acetylneuraminic acid synthase; CMP-N-acetylneuraminic acid synthetase; CMP-NeuNAc synthase; CSS
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种属
Human
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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
Q8NFW8
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表达区间
1-434aa
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氨基酸序列
MDSVEKGAAT SVSNPRGRPS RGRPPKLQRN SRGGQGRGVE KPPHLAALIL ARGGSKGIPL KNIKHLAGVP LIGWVLRAAL DSGAFQSVWV STDHDEIENV AKQFGAQVHR RSSEVSKDSS TSLDAIIEFL NYHNEVDIVG NIQATSPCLH PTDLQKVAEM IREEGYDSVF SVVRRHQFRW SEIQKGVREV TEPLNLNPAK RPRRQDWDGE LYENGSFYFA KRHLIEMGYL QGGKMAYYEM RAEHSVDIDV DIDWPIAEQR VLRYGYFGKE KLKEIKLLVC NIDGCLTNGH IYVSGDQKEI ISYDVKDAIG ISLLKKSGIE VRLISERACS KQTLSSLKLD CKMEVSVSDK LAVVDEWRKE MGLCWKEVAY LGNEVSDEEC LKRVGLSGAP ADACSTAQKA VGYICKCNGG RGAIREFAEH ICLLMEKVNN SCQK
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分子量
48.3 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
CMAS (Carboxymuconolactone Decarboxylase) is an essential enzyme involved in the microbial degradation of aromatic compounds, particularly in the breakdown of catecholic compounds. Its role is crucial for bioremediation processes and understanding microbial metabolism of environmental pollutants. The study of CMAS recombinant proteins has garnered attention due to the increasing need for sustainable methods to tackle the accumulation of toxic aromatic compounds in various ecosystems. By utilizing recombinant DNA technology, researchers aim to express and purify CMAS for further biochemical characterization, enabling detailed studies of its structure-function relationships. This research not only enhances our understanding of the enzyme's catalytic mechanisms but also explores its potential applications in biotechnology and environmental science. Enhanced understanding of CMAS can lead to advancements in biodegradation strategies and the development of novel biocatalysts for industrial applications, thereby contributing to environmental sustainability and pollution remediation efforts. Furthermore, the manipulation of CMAS through genetic engineering may pave the way for innovative approaches to enhance its activity or stability, making it a valuable candidate for biotechnological applications in detoxifying pollutants. Overall, CMAS recombinant protein studies represent a crucial intersection of enzymology, microbiology, and environmental science, aiming to harness natural systems for the mitigation of human impact on the environment.
