Analytical Data
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Gene name
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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Alternative Names
cah; Cephalosporin-C deacetylase; Acetylxylan esterase
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Species
Others
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Source
E. coli
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Tag
Tag Free
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
P94388
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Expression Region
M1-G318
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Protein Length
Full Length
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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
Related Products
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.
