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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

Synonyme(s) :

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

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About This Item

Numéro MDL:
MFCD01092314
Code UNSPSC :
12352203
Nomenclature NACRES :
NA.46

Source biologique

rabbit

Niveau de qualité

200

Conjugué

unconjugated

Forme d'anticorps

IgG fraction of antiserum

Type de produit anticorps

primary antibodies

Clone

polyclonal

Forme

buffered aqueous solution

Poids mol.

antigen 26 kDa

Validation améliorée

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

Conditions d'expédition

dry ice

Température de stockage

−20°C

Modification post-traductionnelle de la cible

unmodified

Description générale

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.

Spécificité

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).

Immunogène

bacterial chloramphenicol acetyl transferase (CAT).

Application

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

Actions biochimiques/physiologiques

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.

Forme physique

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

Clause de non-responsabilité

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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Code de la classe de stockage

10 - Combustible liquids

Classe de danger pour l'eau (WGK)

WGK 3

Point d'éclair (°F)

Not applicable

Point d'éclair (°C)

Not applicable

Certificats d'analyse (COA)

Recherchez un Certificats d'analyse (COA) en saisissant le numéro de lot du produit. Les numéros de lot figurent sur l'étiquette du produit après les mots "Lot" ou "Batch".

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Chloramphenicol acetyltransferase assay.
Smale, S., T.
Cold Spring Harbor Protocols, doi:10-doi:10 (2010)
Bhaskar Anand Jha et al.
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
Eva Bjur et al.
Infection and immunity, 74(9), 5140-5151 (2006-08-24)
The effect of the cytoplasmic reductase and protein chaperone thioredoxin 1 on the virulence of Salmonella enterica serovar Typhimurium was evaluated by deleting the trxA, trxB, or trxC gene of the cellular thioredoxin system, the grxA or gshA gene of
W V Shaw
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
Intercellular nanotubes mediate bacterial communication
Dubey GP and Ben-Yehuda S
Cell, 144, 590-600 (2011)
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