Sign In to View Organizational & Contract Pricing.
Select a Size
Change View
About This Item
Specific activity:
50,000-150,000 units/mg protein
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)
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.
Physical form
Clear, colorless solution in 50% glycerol containing 5 mM Tris-HCl, pH 7.8, and 0.5 mM 2-mercaptoethanol
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.
Still not finding the right product?
Explore all of our products under Chloramphenicol Acetyltransferase from Escherichia coli
Storage Class
10 - Combustible liquids
wgk
WGK 1
flash_point_f
Not applicable
flash_point_c
Not applicable
Regulatory Information
新产品
This item has
Choose from one of the most recent versions:
Already Own This Product?
Find documentation for the products that you have recently purchased in the Document Library.