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C9336

Sigma-Aldrich

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

enhanced validation

IgG fraction of antiserum, buffered aqueous solution

Synonyma:

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

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About This Item

MDL number:
MFCD01092314
UNSPSC Code:
12352203
NACRES:
NA.46

biological source

rabbit

conjugate

unconjugated

antibody form

IgG fraction of antiserum

antibody product type

primary antibodies

clone

polyclonal

form

buffered aqueous solution

mol wt

antigen 26 kDa

enhanced validation

recombinant expression
Learn more about Antibody Enhanced Validation

technique(s)

indirect immunofluorescence: 10 μg/mL using eukaryotic cells transfected with a plasmid bearing the CAT gene
western blot: 10 μg/mL using eukaryotic cells transfected with a plasmid bearing the CAT gene

shipped in

dry ice

storage temp.

−20°C

target post-translational modification

unmodified

General description

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.

Specificity

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).

Immunogen

bacterial chloramphenicol acetyl transferase (CAT).

Application

Anti-Chloramphenicol Acetyl Transferase (CAT) has been used in
  • immunoblotting
  • indirect immunofluorescence
  • immunofluorescence microscopy

Biochem/physiol Actions

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.

Physical form

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

Disclaimer

Unless otherwise stated in our catalog or other company documentation accompanying the product(s), our products are intended for research use only and are not to be used for any other purpose, which includes but is not limited to, unauthorized commercial uses, in vitro diagnostic uses, ex vivo or in vivo therapeutic uses or any type of consumption or application to humans or animals.

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Storage Class

10 - Combustible liquids

wgk_germany

WGK 3

flash_point_f

Not applicable

flash_point_c

Not applicable

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FEBS letters, 589(15), 1966-1974 (2015-06-02)
DRBD13 RNA-binding protein (RBP) regulates the abundance of AU-rich element (ARE)-containing transcripts in trypanosomes. Here we show that DRBD13 regulates RBP6, the developmentally critical protein in trypanosomatids. We also show DRBD13-specific regulation of transcripts encoding cell surface coat proteins including
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In this work, we describe the identification of synthetic, controllable promoters that function in the bacterial pathogen Francisella novicida, a model facultative intracellular pathogen. Synthetic DNA fragments consisting of the tetracycline operator (tetO) flanked by a random nucleotide sequence were
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CRC critical reviews in biochemistry, 14(1), 1-46 (1983-01-01)
Naturally occurring chloramphenicol resistance in bacteria is normally due to the presence of the antibiotic inactivating enzyme chloramphenicol acetyltransferase (CAT) which catalyzes the acetyl-S-CoA-dependent acetylation of chloramphenicol at the 3-hydroxyl group. The product 3-acetoxy chloramphenicol does not bind to bacterial
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