Description
Chloramphenicol, USP Grade (CAS 56‑75‑7) is a high-purity antibiotic optimized for molecular biology applications, particularly in bacterial selection and plasmid amplification.
By reversibly binding to the 50S ribosomal subunit, chloramphenicol halts protein synthesis while permitting replication of low-copy plasmids, enabling significantly enhanced DNA yield during plasmid purification.
This USP-grade formulation supports precise selection of cat-encoded plasmids and serves as a reference inhibitor in translational studies, resistance assays, and ribosome profiling.
With ≥98% purity, consistent solubility in ethanol, and robust long-term stability at −20°C, GoldBio’s chloramphenicol offers the quality and reproducibility you require for high-efficiency cloning, gene expression, and antibiotic mechanism assays.
TESTED AGAINST BOTH SENSITIVE AND RESISTANT CELLS AT GOLD BIOTECHNOLOGY LAB.
Common Research Applications
(Click each for more information)
Amplification of Low-Copy-Number Plasmids for High DNA Yield
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Purpose: To increase plasmid DNA yield from bacterial cultures containing low-copy-number plasmids during purification workflows.
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How It Works: Chloramphenicol inhibits bacterial protein synthesis by binding to the 50S ribosomal subunit, halting chromosomal replication and cell division. Plasmids with relaxed origins (e.g., ColE1, pMB1) continue replicating, resulting in elevated plasmid copy number.
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Applications: Miniprep, midiprep, and maxiprep protocols to enhance DNA recovery for cloning, sequencing, or expression.
Frenkel, L., & Bremer, H. (1986). Increased amplification of plasmids pBR322 and pBR327 by low concentrations of chloramphenicol. DNA, 5(6), 539–544.
Selectable Marker in Molecular Cloning Workflows
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Purpose: To selectively isolate bacteria that have taken up plasmids encoding chloramphenicol resistance.
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How It Works: Plasmids containing the cat gene produce chloramphenicol acetyltransferase (CAT), which inactivates chloramphenicol via acetylation. Only transformants survive under antibiotic selection.
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Applications: Selection and maintenance of recombinant clones in genetic engineering and cloning workflows.
Shaw, W. V. (1975). Chloramphenicol acetyltransferase from chloramphenicol-resistant bacteria. Methods in Enzymology, 43, 737–755.
Mechanistic Studies of Ribosomal Peptidyl-Transferase Inhibition
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Purpose: To investigate how antibiotics inhibit ribosomal function and protein synthesis at the molecular level.
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How It Works: Chloramphenicol binds to the peptidyl transferase center of the 50S ribosomal subunit, blocking peptide bond formation during translation.
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Applications: Structural biology, ribosome function studies, and antibiotic mechanism research.
Schlünzen, F., Zarivach, R., Harms, J., Bashan, A., Tocilj, A., Albrecht, R., et al. (2001). Structural basis for the interaction of antibiotics with the peptidyl transferase centre in eubacteria. Nature, 413(6858), 814–821.
Benchmark Control in Antibiotic Resistance and Efflux Studies
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Purpose: To evaluate bacterial resistance mechanisms such as efflux pumps and enzymatic detoxification.
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How It Works: Chloramphenicol serves as a known substrate for multidrug efflux systems (e.g., AcrAB-TolC). Growth responses are measured in strains with altered resistance mechanisms.
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Applications: Microbial pathogenesis, resistance surveillance, and functional genomics of efflux systems.
Langevin, A. M., & Dunlop, M. J. (2017). Stress introduction rate alters the benefit of AcrAB-TolC efflux pumps. Journal of Bacteriology, 200(1), e00525-17.
Context-Specific Ribosome Stalling Assays in Translation Profiling
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Purpose: To study sequence-dependent translation stalling induced by ribosome-targeting antibiotics.
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How It Works: Chloramphenicol induces stalling when specific amino acids (e.g., alanine, serine, threonine) are present at the penultimate position of the nascent peptide, enabling mapping of translation pauses.
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Applications: Ribosome profiling, toeprinting assays, and studies of translation dynamics and drug–ribosome interactions.
Marks, J., Kannan, K., Roncase, E. J., Klepacki, D., Kefi, A., Orelle, C., et al. (2016). Context-specific inhibition of translation by ribosomal antibiotics targeting the peptidyl transferase center. Nature Structural & Molecular Biology, 23(7), 626–633.
Benefits
- Reliable plasmid yield enhancement: Supports high-copy recovery from low-copy plasmids via selective replication arrest.
- Essential for clone selection: Compatible with cat-resistant vectors, especially in dual-antibiotic plasmid systems.
- Benchmark translation inhibitor: Gold-standard ribosomal inhibitor for mechanistic assays and structural biology.
- Valid control in resistance studies: Used in efflux pump research and microbial resistance profiling.
- Context-sensitive profiling agent: Enables fine-resolution analysis of sequence-specific ribosomal stalling.
Product Specifications
Grade: USP Grade
Formula: C11H12Cl2N2O5
Molecular Weight: 323.13 g/mol
PubChem Chemical ID: 5959
Storage/Handling:
Store desiccated at -20°C. Soluble in ethanol.
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