Product Name
Chloramphenicol Acetyltransferase from Escherichia coli, buffered aqueous glycerol solution
form
buffered aqueous glycerol solution
specific activity
50,000-150,000 units/mg protein
mol wt
75 kDa (three identical subunits)
shipped in
wet ice
storage temp.
−20°C
Gene Information
Escherichia coli ... cat(2847485)
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Application
Chloramphenicol acetyltransferase from Escherichia coli has been used in a study to assess the construction of a novel expression system in Klebsiella pneumoniae and its application for 1,3-propanediol production. Chloramphenicol acetyltransferase from Escherichia coli has also been used in a study to investigate site-directed mutagenesis and promoter functional analysis of the RM07 DNA fragment from Halobacterium halobium.
The enzyme has been used in chloramphenicol acetyltransferase assay to optimize the transfection of plasmid DNA into primary cultures of adult mouse keratinocytes. It has also been used to assess the acetyl-CoA carboxylase-carboxyltransferase (ACC-CT) domain activity. This has been done using a coupled-two phase system measuring the selective partition of [14C]acetylchloramphenicol into an organic layer.
Biochem/physiol Actions
The enzyme responsible for chloramphenicol resistance in bacteria. Catalyzes the conversion of acetyl-CoA + chloramphenicol to CoA + chloramphenicol 3-acetate.
Other Notes
One unit will convert 1.0 nanomole of chloramphenicol and acetyl-CoA to chloramphenicol 3-acetate and CoA per min at pH 7.8 at 25 °C.
Physical form
Clear, colorless solution in 50% glycerol containing 5 mM Tris-HCl, pH 7.8, and 0.5 mM 2-mercaptoethanol
Storage Class
10 - Combustible liquids
wgk
WGK 1
flash_point_f
Not applicable
flash_point_c
Not applicable
Regulatory Information
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N A Betz et al.
In vitro cellular & developmental biology : journal of the Tissue Culture Association, 28A(3 Pt 1), 188-192 (1992-03-01)
An efficient and reproducible technique for the transfection of primary cultures of adult mouse keratinocytes has been developed. The procedure involves culturing the primary adult mouse epidermal cells at 32 degrees C in an enriched media until they reach 70
Francis Rajamohan et al.
The Journal of biological chemistry, 286(48), 41510-41519 (2011-09-29)
Inhibition of acetyl-CoA carboxylases (ACCs), a crucial enzyme for fatty acid metabolism, has been shown to promote fatty acid oxidation and reduce body fat in animal models. Therefore, ACCs are attractive targets for structure-based inhibitor design, particularly the carboxyltransferase (CT)
Detection of florfenicol resistance genes in Riemerella anatipestifer isolated from ducks and geese.
Yen-Ping Chen et al.
Veterinary microbiology, 154(3-4), 325-331 (2011-08-09)
The cat gene, coding for chloramphenicol acetyltransferase has been reported for conferring the chloramphenicol resistance for Riemerella anatipestifer. Chloramphenicol acetyltransferases, however, are unable to inactivate florfenicol. In this study, 66 R. anatipestifer isolates were investigated for their susceptibility to chloramphenicol
Hirofumi Nariya et al.
Applied and environmental microbiology, 77(23), 8439-8441 (2011-10-04)
A xylose-inducible gene expression vector for Clostridium perfringens was developed. Plasmid pXCH contains a chromosomal region from Clostridium difficile (xylR-P(xy)(lB)): xylR, encoding the xylose repressor, xylO, the xyl operator sequence, and P(xylB), the divergent promoter upstream of xylBA encoding xylulo
Gregory F Dolan et al.
RNA (New York, N.Y.), 20(2), 202-213 (2013-12-18)
Group I introns are ribozymes (catalytic RNAs) that excise themselves from RNA primary transcripts by catalyzing two successive transesterification reactions. These cis-splicing ribozymes can be converted into trans-splicing ribozymes, which can modify the sequence of a separate substrate RNA, both
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