Analytical Data
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基因名
Cephalosporin C deacetylase
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简介
Cephalosporin C deacetylase Protein, an esterase, selectively removes acetyl groups from substrates like acetylated xylose and cephalosporin C. Its catalytic activity excludes polymeric acetylated xylan and amide linkages, highlighting its nuanced, targeted deacetylation function. Cephalosporin C deacetylase Protein, Bacillus subtilis is the recombinant Cephalosporin C deacetylase protein, expressed by E. coli , with tag free.
- Application
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别名
cah; Cephalosporin-C deacetylase; Acetylxylan esterase
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种属
Others
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表达系统
E. coli
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标签
Tag Free
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纯度
Greater than 90% as determined by SDS-PAGE.
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蛋白编号
P94388
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表达区间
M1-G318
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蛋白长度
Full Length
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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
Cephalosporin C deacetylase (CCD) is an enzyme that plays a critical role in the bioconversion of cephalosporin C, a crucial antibiotic produced by the fungus Acremonium chrysogenum. This enzyme mediates the hydrolysis of the acetyl group in cephalosporin C, facilitating the synthesis of 7-aminocephalosporanic acid (7-ACA), a core structure in the development of various cephalosporin antibiotics. Given the increasing emergence of antibiotic-resistant bacteria, there is a pressing need to discover and develop novel antibiotics, making the enzymatic conversion of cephalosporin C highly relevant for pharmaceutical applications. The study of recombinant CCD offers significant advantages, such as enhanced enzyme production and simpler purification processes, contributing to more efficient industrial applications. In recent years, advancements in genetic engineering techniques have enabled researchers to clone, express, and purify CCD in heterologous systems, thereby improving our understanding of its catalytic mechanisms and substrate specificity. This research not only opens avenues for optimizing antibiotic production but also provides insights into enzyme engineering for improved performance, potentially leading to innovative strategies in combating bacterial resistance and enhancing the efficacy of existing antibiotics. Thus, the exploration of recombinant Cephalosporin C deacetylase represents a pivotal area of study in modern microbiology and pharmaceutical development.
