Anti-Chloramphenicol Acetyl Transferase (CAT) antibody produced in rabbit

Chloramphenicol Acetyl Transferases (CATs) shows conservation and differences in their amino acid sequences. CAT is encode by cat gene and exists as monomer and later assemble into a trimer.

bacterial chloramphenicol acetyl transferase (CAT).

Anti-Chloramphenicol Acetyl Transferase (CAT) has been used in

• immunoblotting
• indirect immunofluorescence
• immunofluorescence microscopy

Anti-Chloramphenicol Acetyl Transferase (CAT) antibody is specific for bacterial CAT and recombinant CAT expressed in transfected eukaryotic cells (a predominant band of approx. 26 kD).

Bacterial chloramphenicol acetyl transferase (CAT) is an enzyme that catalyzes the inactivation of the antibiotic, chloramphenicol, by acetylation and subsequently confers bacterial resistance to the antibiotic. CAT, being a stable prokaryotic enzyme, is often used as a reporter gene in transfection assays developed for eukaryotic promoters. Quantification of reporter gene expressions, such as that of CAT, can be correlated to the transcriptional functions of the target sequence. Thus, antibodies directed against CAT can be used for the study of gene sequences that are fused to the CAT reporter gene
Anti-Chloramphenicol Acetyl Transferase (CAT) antibody is specific for bacterial CAT and recombinant CAT expressed in transfected eukaryotic cells (a predominant band of approx. 26 kD). Staining of CAT by the antibody is inhibited by the bacterial CAT antigen in cells transfected with CAT.

Solution in 0.01 M phosphate buffered saline, pH 7.4, containing 15 mM sodium azide.

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