Escherichia coli TOP10 (Invitrogen) and E. coli CA434 [39] (link) were cultured in Luria-Bertani (LB) medium, supplemented with chloramphenicol (25 µg/ml), where appropriate. Routine cultures of C. difficile 630 Δerm[40] (link) and C. difficile R20291 were carried out in BHIS medium (brain heart infusion medium supplemented with 5 mg/ml yeast extract and 0.1% [wt/vol] L-cysteine) [41] (link). C. difficile medium was supplemented with D-cycloserine (250 µg/ml), cefoxitin (8 µg/ml), lincomycin (20 µg/ml), and/or thiamphenicol (15 µg/ml) where appropriate. A defined minimal media [18] (link) was used as uracil-free medium when performing genetic selections. A basic nutritive mannitol broth for growth assays of C. difficile strains were prepared as follows : Proteose peptone no. 2 4% [wt/vol] (BD Diagnostics, USA), sodium phosphate dibasic 0.5%[wt/vol], potassium phosphate monobasic 0.1%[wt/vol], sodium chloride, 0.2% [wt/vol], magnesium sulfate, 0.01% [wt/vol], mannitol, 0.6% [wt/vol] with final pH at +/−7.35. For solid medium, agar was added to a final concentration of 1.0% (wt/vol). Clostridium sporogenes ATCC 15579 was cultivated in TYG media [7] (link). All Clostridium cultures were incubated in an anaerobic workstation at 37°C (Don Whitley, Yorkshire, United Kingdom). Uracil was added at 5 µg/ml, and 5-Fluoroorotic acid (5-FOA) at 2 mg/ml. All reagents, unless noted, were purchased from Sigma-Aldrich.
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Thiamphenicol
Thiamphenicol
Thiamphenicol is a broad-spectrum antibiotic used to treat various bacterial infections.
It is chemically similar to chloramphenicol, but has a lower risk of causing serious side effects.
Thiamphenicol works by inhibiting protein synthesis in bacteria, preventing them from growing and replicating.
It is commonly used to treat respiratory tract infections, urinary tract infections, and other systemic infections.
Researchers can leverage PubCompare.ai to optimize their Thiamphenicol research by accessing the best protocols from literature, preprints, and patents, while enhancing reproducibility and accuracy through AI-driven comparisons.
This tool can help streamline the research process and uncover new insights to advance the understanding and therapeutic applications of Thiamphenicol.
It is chemically similar to chloramphenicol, but has a lower risk of causing serious side effects.
Thiamphenicol works by inhibiting protein synthesis in bacteria, preventing them from growing and replicating.
It is commonly used to treat respiratory tract infections, urinary tract infections, and other systemic infections.
Researchers can leverage PubCompare.ai to optimize their Thiamphenicol research by accessing the best protocols from literature, preprints, and patents, while enhancing reproducibility and accuracy through AI-driven comparisons.
This tool can help streamline the research process and uncover new insights to advance the understanding and therapeutic applications of Thiamphenicol.
Most cited protocols related to «Thiamphenicol»
Escherichia coli TOP10 (Invitrogen) and E. coli CA434 [39] (link) were cultured in Luria-Bertani (LB) medium, supplemented with chloramphenicol (25 µg/ml), where appropriate. Routine cultures of C. difficile 630 Δerm[40] (link) and C. difficile R20291 were carried out in BHIS medium (brain heart infusion medium supplemented with 5 mg/ml yeast extract and 0.1% [wt/vol] L-cysteine) [41] (link). C. difficile medium was supplemented with D-cycloserine (250 µg/ml), cefoxitin (8 µg/ml), lincomycin (20 µg/ml), and/or thiamphenicol (15 µg/ml) where appropriate. A defined minimal media [18] (link) was used as uracil-free medium when performing genetic selections. A basic nutritive mannitol broth for growth assays of C. difficile strains were prepared as follows : Proteose peptone no. 2 4% [wt/vol] (BD Diagnostics, USA), sodium phosphate dibasic 0.5%[wt/vol], potassium phosphate monobasic 0.1%[wt/vol], sodium chloride, 0.2% [wt/vol], magnesium sulfate, 0.01% [wt/vol], mannitol, 0.6% [wt/vol] with final pH at +/−7.35. For solid medium, agar was added to a final concentration of 1.0% (wt/vol). Clostridium sporogenes ATCC 15579 was cultivated in TYG media [7] (link). All Clostridium cultures were incubated in an anaerobic workstation at 37°C (Don Whitley, Yorkshire, United Kingdom). Uracil was added at 5 µg/ml, and 5-Fluoroorotic acid (5-FOA) at 2 mg/ml. All reagents, unless noted, were purchased from Sigma-Aldrich.
5-fluoroorotic acid
Agar
Biological Assay
Brain
Cefoxitin
Chloramphenicol
Clostridium
Clostridium sporogenes
Cycloserine
Cysteine
Diagnosis
Escherichia coli
Genetic Selection
Heart
Lincomycin
Mannitol
potassium phosphate
proteose-peptone
Sodium Chloride
sodium phosphate
Strains
Sulfate, Magnesium
Thiamphenicol
Uracil
Yeast, Dried
C. thermocellum was transformed via electroporation as described
[5 (link),6 ] with modifications. Briefly, 400 mlC. thermocellum was grown to an OD between 0.8 and 1.0, centrifuged without measures to exclude oxygen, since washing the cells in the presence of O2 seemed to have no impact on transformation efficiency (unpublished observations), at room temperature in a Beckman Coulter Avanti J-25 centrifuge with a JA-10 rotor at 5000 × g, and the supernatant was removed. Being careful to minimize disturbance, cell pellets were washed with 400 ml ice cold electroporation buffer prepared without measures to exclude oxygen and consisting of 250 mM sucrose, 10% glycerol, 100 µM MOPS pH 7.0, 0.5 mM MgCl2, 0.5 mM MgSO4 and centrifuged at 4000×g. The cells were rinsed and centrifuged a second time as above and brought on ice into a Coy anaerobic chamber, maintaining anaerobicity for the remainder of the transformation. Cells were resuspended in an additional 500 µl electroporation buffer and kept on ice until use. Plasmid DNA (2 µl at 500 ng/µl) was mixed with 20 µl washed cells in pre-chilled 1 mm electroporation cuvettes. The mixture was then subjected to a 1.2 kV, 1.5 msec square pulse using a BioRad GenePulser XCell. Cells were immediately resuspended in 1 ml room temperature growth medium and serial dilutions were plated with no recovery period (to ensure each colony represents a unique transformant) by mixing with 25 ml molten media+0.8% agar+thiamphenicol. Once plates had solidified, they were placed in 2.5 L AnaeroPack Rectangular Jars (bioMerieux, Durham, NC, USA) to minimize desiccation and incubated at 51°C for up to one week. Transformations were repeated at least three times, and the mean and range of efficiency is reported.
Successful transformation was confirmed by re-isolation of plasmid DNA. Briefly, chromosomal DNA was isolated from thiamphenicol resistant C. thermocellum transformants using the QIAGEN DNeasy kit (Qiagen, Valencia, CA) following the pretreatment protocol for DNA isolation from Gram-positive bacteria according to manufacturer’s specifications. This DNA was transformed into E. coli Top10 cells, re-isolated, and subjected to restriction enzyme digestion to confirm the identity of the plasmid.
[5 (link),6 ] with modifications. Briefly, 400 mlC. thermocellum was grown to an OD between 0.8 and 1.0, centrifuged without measures to exclude oxygen, since washing the cells in the presence of O2 seemed to have no impact on transformation efficiency (unpublished observations), at room temperature in a Beckman Coulter Avanti J-25 centrifuge with a JA-10 rotor at 5000 × g, and the supernatant was removed. Being careful to minimize disturbance, cell pellets were washed with 400 ml ice cold electroporation buffer prepared without measures to exclude oxygen and consisting of 250 mM sucrose, 10% glycerol, 100 µM MOPS pH 7.0, 0.5 mM MgCl2, 0.5 mM MgSO4 and centrifuged at 4000×g. The cells were rinsed and centrifuged a second time as above and brought on ice into a Coy anaerobic chamber, maintaining anaerobicity for the remainder of the transformation. Cells were resuspended in an additional 500 µl electroporation buffer and kept on ice until use. Plasmid DNA (2 µl at 500 ng/µl) was mixed with 20 µl washed cells in pre-chilled 1 mm electroporation cuvettes. The mixture was then subjected to a 1.2 kV, 1.5 msec square pulse using a BioRad GenePulser XCell. Cells were immediately resuspended in 1 ml room temperature growth medium and serial dilutions were plated with no recovery period (to ensure each colony represents a unique transformant) by mixing with 25 ml molten media+0.8% agar+thiamphenicol. Once plates had solidified, they were placed in 2.5 L AnaeroPack Rectangular Jars (bioMerieux, Durham, NC, USA) to minimize desiccation and incubated at 51°C for up to one week. Transformations were repeated at least three times, and the mean and range of efficiency is reported.
Successful transformation was confirmed by re-isolation of plasmid DNA. Briefly, chromosomal DNA was isolated from thiamphenicol resistant C. thermocellum transformants using the QIAGEN DNeasy kit (Qiagen, Valencia, CA) following the pretreatment protocol for DNA isolation from Gram-positive bacteria according to manufacturer’s specifications. This DNA was transformed into E. coli Top10 cells, re-isolated, and subjected to restriction enzyme digestion to confirm the identity of the plasmid.
Agar
Bacteria, Anaerobic
Buffers
Cells
Chromosomes
Cold Temperature
Culture Media
Desiccation
Digestion
DNA Restriction Enzymes
Electroporation
Escherichia coli
Glycerin
Gram-Positive Bacteria
Magnesium Chloride
morpholinopropane sulfonic acid
Oxygen
Pellets, Drug
Plasmids
Pulse Rate
Sucrose
Sulfate, Magnesium
Technique, Dilution
Thiamphenicol
C. difficile strains, outlined in Table 1 , were propagated either in TY broth without thioglycolate [5] (link) or on BHI agar. Cultures were incubated at 37 °C in an anaerobic environment composed of 80% nitrogen, 10% hydrogen and 10% carbon dioxide. Escherichia coli was routinely grown in LB broth or on LB agar. E. coli strain CA434 (HB101 carrying R702) was used as the conjugation donor throughout. NEB5α (New England Biolabs) was used for cloning and plasmid propagation. Growth media was supplemented with chloramphenicol (15 μg/ml), thiamphenicol (15 μg/ml) or cycloserine (250 μg/ml) as appropriate.
Agar
Carbon dioxide
Chloramphenicol
Culture Media
Cycloserine
Escherichia coli
Hydrogen
Nitrogen
Plasmids
Strains
Thiamphenicol
Thioglycolates
Tissue Donors
A previously described and widely used conjugation protocol was used as the starting point for development of our improved method [2] (link). 200 μl samples of C. difficile overnight cultures were heated, as above, and incubated at 37 °C for 2 min. 1 ml of overnight E. coli conjugant donor (CA434) culture was harvested by centrifugation at 4000g for 2 min and transferred into the anaerobic workstation. E. coli cell pellets were then gently resuspended in 200 μl of heat treated or untreated C. difficile culture. This mixed cell suspension was then pipetted onto well-dried, non-selective agar plates (10 × 10 μl spots) and allowed to dry. BHI agar was used routinely but BHIS (BHI agar supplemented with 0.1% (w/v) cysteine and 0.5% (w/v) yeast extract), TY [5] (link) and Brazier’s (Brazier’s CCEY media, 1% (v/v) defibrinated horse blood, 4% (v/v) egg yolk emulsion) agar were also tested. All solid media contained 1.5% agar. Conjugations were then incubated for 8–24 h following which growth was harvested using 900 μl of TY broth, serially diluted and spread on plates containing either cycloserine (for total C. difficile CFU counts), or cycloserine and thiamphenicol (to select for transconjugants). Approximate conjugation efficiency was then calculated as transconjugant CFU/total C. difficile CFU. These experiments were performed using biological duplicates with technical triplicates. Statistical significance of these results was determined using either individual student t-tests or in combination with one way analysis of variance (ANOVA), performed using GraphPad Prism 6. P values of<0.05 were considered statistically significant.
Agar
Biopharmaceuticals
BLOOD
Cells
Centrifugation
Cycloserine
Cysteine
Emulsions
Equus caballus
Escherichia coli
Exanthema
Pellets, Drug
prisma
Student
Thiamphenicol
Tissue Donors
Yeast, Dried
Yolks, Egg
The procedure adopted was as previously described [9] (link). For inactivation of pyrE, E. coli CA434 donor cells carrying pMTL-YN18 were conjugated with R20291 and transconjugants selected on BHIS media supplemented D-cycloserine (250 µg/ml), cefoxitin (8 µg/ml), thiamphenicol (15 µg/ml) and uracil (5 µg/ml). A single transconjugant was re-streaked onto the same medium and then a ‘large’ representative colony streaked onto minimal agar medium agar supplemented with FOA (2 mg/ml) and uracil (5 µg/ml). The colonies that arose were re-streaked twice onto the same media, and analyzed by PCR to confirm deletion of pyrE (as detailed in Results ), and Sanger sequencing was used to confirm the expected genotype. Confirmation that the plasmid had been lost, was obtained by patch plating onto BHIS agar supplemented with thiamphenicol and establishing that no growth occurred. For correction of the pyrE mutation (ie., plasmids pMTL-YN1, 1C, 1X, 2, 2C and 2X) transconjugants were streaked onto minimal media without uracil or FOA supplementation and those colonies that developed analysed as above.
Agar
Cefoxitin
Cells
Cycloserine
Deletion Mutation
Escherichia coli
Genotype
Mutation
Plasmids
Thiamphenicol
Tissue Donors
Uracil
Most recents protocols related to «Thiamphenicol»
Strains and plasmids used in this study are listed in Table 1 , whereas primers are listed in Table 2 . The genes encoding cdtA and cdtB were deleted from C difficile R20291ΔpyrE using allelic-exchange technology [16 (link)]. To achieve this, left and right homology arms corresponding to the regions annealing immediately upstream and downstream of cdtA/B were amplified by polymerase chain reaction (PCR) using cdtAB LAF/RAR and cdtAB RAF/RAR primer sets, respectively. The homology arms were then spliced together by overlap-extension (SOEing) PCR by means of their overlapping 20-base pair (bp) homologous regions before cloning the ensuing product into pMTL-YN4 using flanking SbfI-AscI restriction sites, thus generating the knockout cassette (KOC) pMTL-YN4-cdtAB KOC. The plasmid was then conjugated into C difficile R20291ΔpyrE exactly as previously described, and transconjugants were selected on the basis of thiamphenicol resistance [17 (link)]. Thereafter, single crossover integrants (SCOs) were identified by 2 parallel PCR screens using cdtAB diag F/YN4 primers for left arm recombinants and YN4 F/cdtAB diag R primers for right arm recombinants, respectively (data not shown). To select for double crossover recombinants, SCO integrants were harvested, diluted 1 × 10−3, and cultured onto C difficile minimal medium (CDMM) [18 (link)] containing 500 µg/mL 5-fluoroorotic acid and 1 µg/mL uracil, to force plasmid loss through the counter-selection marker pyrE and to select for double crossover mutants before confirming plasmid loss on the basis of thiamphenicol sensitivity. The intended deletions were confirmed by PCR analysis using cdtAB diag F/R primers. The deletion mutant generated an approximately 4-kbp product, while its wild-type (WT) counterpart generated a 4.6-kbp product (Figure 1 A ). Finally, the pyrE allele was restored to WT using pMTL-YN2 exactly as described previously [17 (link)].
Strains differentially producing CDTa or CDTb were generated by the integration of either cdtA or cdtB at the pyrE locus, under the control of cdtA promoter PcdtA. First, cdtA coupled with its native promoter was amplified by PCR using PcdtA F and cdtA R primers, the product of which was cloned into pMTL-YN2C by means of flanking NotI-BamHI restriction sites, thus generating the complementation cassette pMTL-YN2C-PcdtA-cdtA. In a similar fashion, pMTL-YN2C-PcdtA-cdtB was generated by amplifying PcdtA using PcdtA F/PcdtA LAR primers, and cdtB was generated using cdtB RAF/cdtB RAR primers, before SOEing the products together and cloning them into pMTL-YN2C by means of flanking NotI-SalI restriction sites. The CDTb-encoding construct could only be generated with a single-nucleotide polymorphism in the promoter region of PcdtA using an A-G substitution at position-124 relative to the start codon. The resultant plasmids were applied in parallel, to individually integrate the respective CDT constructs at the pyrE locus of R20291ΔpyrEΔcdtAB concomitant with the repair of pyrE, after successful conjugation and selection for uracil prototrophs on CDMM lacking uracil. The PCR analysis using primer pyrE WT F, coupled with either cdtA R or cdtB RAR, demonstrated effective knock-in at the pyrE locus (Figure 1 B ), thus generating strains R20291ΔcdtAB*PcdtA-cdtA and R20291ΔcdtAB*PcdtA-cdtB.
Strains differentially producing CDTa or CDTb were generated by the integration of either cdtA or cdtB at the pyrE locus, under the control of cdtA promoter PcdtA. First, cdtA coupled with its native promoter was amplified by PCR using PcdtA F and cdtA R primers, the product of which was cloned into pMTL-YN2C by means of flanking NotI-BamHI restriction sites, thus generating the complementation cassette pMTL-YN2C-PcdtA-cdtA. In a similar fashion, pMTL-YN2C-PcdtA-cdtB was generated by amplifying PcdtA using PcdtA F/PcdtA LAR primers, and cdtB was generated using cdtB RAF/cdtB RAR primers, before SOEing the products together and cloning them into pMTL-YN2C by means of flanking NotI-SalI restriction sites. The CDTb-encoding construct could only be generated with a single-nucleotide polymorphism in the promoter region of PcdtA using an A-G substitution at position-124 relative to the start codon. The resultant plasmids were applied in parallel, to individually integrate the respective CDT constructs at the pyrE locus of R20291ΔpyrEΔcdtAB concomitant with the repair of pyrE, after successful conjugation and selection for uracil prototrophs on CDMM lacking uracil. The PCR analysis using primer pyrE WT F, coupled with either cdtA R or cdtB RAR, demonstrated effective knock-in at the pyrE locus (
5-fluoroorotic acid
Alleles
Base Pairing
CDTA
Codon, Initiator
Culture Media
Deletion Mutation
Gene Deletion
Genes
Hypersensitivity
Oligonucleotide Primers
Plasmids
Polymerase Chain Reaction
Single Nucleotide Polymorphism
sodium-binding benzofuran isophthalate
Strains
Thiamphenicol
Thiel-Behnke corneal dystrophy
Uracil
The strains used in this study are listed in Table S3. Strains were cultured on brain heart infusion (BHI) agar or broth (Oxoid) at 37°C in an anaerobic chamber (Biomerieux, Marcy l’Etoile, France) (v/v: 80% N2, 10% H2, 10% CO2). When necessary, the medium was supplemented with cycloserine (250 mg.mL−1), thiamphenicol (15 mg.mL−1 to select KO strains or 7.5 mg.mL−1 to maintain the plasmid pMTL007-hbd), or erythromycin (5 mg.mL−1). Escherichia coli TOP10 strain was used for cloning and plasmid propagation. E. coli HB101 (RP4) strain was used as the conjugative donor for developing the clostridia KO strains. E. coli strains were cultured aerobically at 37°C in Luria–Bertani agar or broth, and when needed, the medium was supplemented with ampicillin (100 mg.mL−1) or chloramphenicol (25 mg.mL−1).
Agar
Ampicillin
Brain
Chloramphenicol
Clostridium
Cycloserine
Erythromycin
Escherichia coli
Heart
Plasmids
Strains
Thiamphenicol
Tissue Donors
The oligonucleotides and plasmids used in this study are listed in Table S1 and S4, respectively. The mobile group II intron system was used as described previously to inactivate the hbd.34 (link),48 (link) The algorithm available on the TargeTron Design Site (http://www.clostron.com/clostron2.php ) was used to identify the intron insertion site within hbd (position 414) and design primers to retarget the group II intron in hbd (c-hbd-414|415s-IBS, c-hbd-414|415s-EBS1d, and c-hbd-414|415s-EBS2). These primers were used with EBS universal primers and intron template DNA to generate a DNA fragment by overlap PCR as recommended by manufacturers. The PCR product was purified using QIAquick PCR Purification Kit (Qiagen, Courtaboeuf, France) and digested by BsrGI and HindIII restriction enzymes. Plasmid pMTL007C-E2-hbd was developed by ligating (T4 DNA ligase) (Sigma Aldrich Chimie, Saint-Quentin-Fallavier, France) the digested PCR product and pMTL007C-E2 digested with BsrGI/HindIII and purified with QIAEX II Gel Extraction kit (Qiagen). The ligation mixture was introduced into E. coli TOP10 by electroporation. After extracting the plasmid (QIAprep Spin Miniprep kit, Qiagen) and amplifying the insert by FastStart High Fidelity PCR System (Sigma Aldrich Chimie,) with primers pMTLCE2seqF and pMTLseqR, the cloned insert was verified by DNA sequencing using the same primers (Genewiz, Takeley, UK). The plasmid pMTL007C-E2-hbd was transformed into the conjugative donor E. coli HB101 (RP4) and transferred into the C. butyricum 1002 and C. neonatale 250.09 strains via conjugation. The transconjugants were selected on BHI agar supplemented with cycloserine and thiamphenicol. Inactivation of hbd was verified by screening transconjugants for erythromycin resistance and thiamphenicol sensitivity, and the resultant strains were named CbuCB1002-hbd415s::CT and Cne205.09-hbd415s::CT. Further, genomic DNA was extracted (InstaGene Matrix Kit) (Bio-Rad, Marnes-la-Coquette, France) and subjected to PCR using primers flanking hbd (hbdF and hbdR) to verify the intron insertion into the correct target gene. Moreover, the presence of the ermB was confirmed by PCR using primers RAMFCE2 and RAMRCE2, and the orientation of insertion was verified by PCR with a combination of hbdF, hbdR, and EBS Universal primers.
Agar
Cycloserine
DNA, A-Form
DNA Restriction Enzymes
Electroporation
Erythromycin
Escherichia coli
Gene Insertion
Genome
Hypersensitivity
Introns
Ligation
Oligonucleotide Primers
Oligonucleotides
Plasmids
Strains
T4 DNA Ligase
Thiamphenicol
Tissue Donors
Antibiotics
beta-glycerol phosphate
Calcium chloride
Carbenicillin
Cloning Vectors
Cysteine Hydrochloride
Escherichia coli
ferrous sulfate
Kanamycin
Magnesium Chloride
morpholinopropane sulfonic acid
Plasmids
potassium hydroxide
potassium phosphate, dibasic
Recombinase
Replication Origin
resazurin
Saccharomyces cerevisiae
Sodium
Sodium Chloride
Sodium Citrate
Spectinomycin
Strains
Streptomycin
Sulfate, Ammonium
Thiamphenicol
Electroporation was performed similarly to existing protocols for C. thermocellum (36 (link)). Two 5 mL cultures were inoculated with C. clariflavum 4-2a and grown overnight. The next day, two 200 mL cultures were inoculated with a 1% inoculum and grown until an optical density at 600 nm (OD600) of 0.9. Once the cultures were grown, they were centrifuged in 50 mL conical tubes at room temperature at 6,000 × g for 15 min. The supernatant was decanted, and 25 mL of electroporation buffer (250 mM sucrose, 10% glycerol) was added to the tube without disrupting the cell pellet. Cells were centrifuged again and washed twice more in the same way. After the last spin, the cell pellets were resuspended in ~ 100 μL electroporation buffer and transferred to a microcentrifuge tube.
Using fresh electrocompetent cells, 20 μL of cells were transformed with 1 μg of pMTL83151 (37 (link)). Cells were electroporated in a 1 mm cuvette with a square wave using a Bio-Rad Gene Pulser Xcell Electroporation System set at 1200 V with a 1.5 msec pulse. Cells were then resuspended in 1 mL CTFUD medium and incubated for 3 h at 50°C to recover. After recovery, transformants were plated within CTFUD with 1.5% agar and 5 μg/mL thiamphenicol and incubated for 4 days at 50°C. Colonies from the plates were picked into liquid CTFUD medium. Liquid culture was screened by PCR for the presence of the cat gene and further confirmed via 16S rRNA gene sequencing to verify the culture. Two batches of C. clariflavum competent cells were transformed with plasmid from each methylation state, each time in duplicate (n = 4 total).
Using fresh electrocompetent cells, 20 μL of cells were transformed with 1 μg of pMTL83151 (37 (link)). Cells were electroporated in a 1 mm cuvette with a square wave using a Bio-Rad Gene Pulser Xcell Electroporation System set at 1200 V with a 1.5 msec pulse. Cells were then resuspended in 1 mL CTFUD medium and incubated for 3 h at 50°C to recover. After recovery, transformants were plated within CTFUD with 1.5% agar and 5 μg/mL thiamphenicol and incubated for 4 days at 50°C. Colonies from the plates were picked into liquid CTFUD medium. Liquid culture was screened by PCR for the presence of the cat gene and further confirmed via 16S rRNA gene sequencing to verify the culture. Two batches of C. clariflavum competent cells were transformed with plasmid from each methylation state, each time in duplicate (n = 4 total).
Agar
Buffers
Cells
Electroporation
Genes
Genitalia
Glycerin
Methylation
Pellets, Drug
Plasmids
Pulse Rate
RNA, Ribosomal, 16S
Sucrose
Thiamphenicol
Vision
Top products related to «Thiamphenicol»
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Thiamphenicol is a broad-spectrum antibiotic that can be used in the laboratory setting. It functions as an inhibitor of bacterial protein synthesis.
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The Anaerobic Chamber is a laboratory equipment designed to provide a controlled, oxygen-free environment for various applications that require an anaerobic atmosphere. It maintains a low-oxygen, high-nitrogen or carbon dioxide atmosphere to support the growth and handling of anaerobic organisms or to perform experiments and procedures that require an anaerobic environment.
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Chloramphenicol is a bacteriostatic antibiotic that inhibits protein synthesis in bacteria. It is commonly used in microbiology laboratories for selective cultivation and identification of bacterial species.
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L-cysteine is an amino acid that serves as a key component in the manufacturing of various laboratory reagents and equipment. It functions as a building block for proteins and plays a crucial role in the formulation of buffers, cell culture media, and other essential laboratory solutions.
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Thiamphenicol is a broad-spectrum antibiotic used in the treatment of various bacterial infections. It functions by inhibiting bacterial protein synthesis, thereby preventing the growth and proliferation of bacteria.
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Florfenicol is a synthetic antibiotic compound that belongs to the class of amphenicol antibiotics. It is a broad-spectrum antimicrobial agent used in various veterinary applications. Florfenicol functions by inhibiting protein synthesis in bacteria, thereby exerting its antibacterial activity.
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Brain Heart Infusion medium is a microbiological culture medium used for the cultivation of a variety of microorganisms, including bacteria and fungi. It provides essential nutrients and growth factors required for the optimal growth of these microorganisms.
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More about "Thiamphenicol"
Thiamphenicol is a broad-spectrum antibiotic that belongs to the phenicol class of antibiotics, which also includes chloramphenicol.
It is used to treat a variety of bacterial infections, including respiratory tract infections, urinary tract infections, and other systemic infections.
Thiamphenicol works by inhibiting protein synthesis in bacteria, preventing them from growing and replicating.
Compared to chloramphenicol, thiamphenicol is considered to have a lower risk of serious side effects, such as aplastic anemia.
This makes it a viable alternative for patients who cannot tolerate chloramphenicol.
Thiamphenicol is chemically similar to chloramphenicol, but with a slightly modified structure that alters its pharmacokinetic and safety profile.
Researchers can leverage the PubCompare.ai tool to optimize their thiamphenicol research.
This AI-driven platform allows researchers to access the best protocols from literature, preprints, and patents, while enhancing the reproducibility and accuracy of their experiments.
By using PubCompare.ai, researchers can streamline their research process and uncover new insights to advance the understanding and therapeutic applications of thiamphenicol.
In addition to thiamphenicol, other related terms and concepts that may be relevant to researchers include anaerobic chambers, chloramphenicol, erythromycin, L-cysteine, the MG1000 Anaerobic Work Station, florfenicol, Brain Heart Infusion medium, and taurocholate.
These tools and compounds can be used in conjunction with thiamphenicol research to optimize experimental design, improve experimental conditions, and enhance the overall understanding of this important antibiotic.
It is used to treat a variety of bacterial infections, including respiratory tract infections, urinary tract infections, and other systemic infections.
Thiamphenicol works by inhibiting protein synthesis in bacteria, preventing them from growing and replicating.
Compared to chloramphenicol, thiamphenicol is considered to have a lower risk of serious side effects, such as aplastic anemia.
This makes it a viable alternative for patients who cannot tolerate chloramphenicol.
Thiamphenicol is chemically similar to chloramphenicol, but with a slightly modified structure that alters its pharmacokinetic and safety profile.
Researchers can leverage the PubCompare.ai tool to optimize their thiamphenicol research.
This AI-driven platform allows researchers to access the best protocols from literature, preprints, and patents, while enhancing the reproducibility and accuracy of their experiments.
By using PubCompare.ai, researchers can streamline their research process and uncover new insights to advance the understanding and therapeutic applications of thiamphenicol.
In addition to thiamphenicol, other related terms and concepts that may be relevant to researchers include anaerobic chambers, chloramphenicol, erythromycin, L-cysteine, the MG1000 Anaerobic Work Station, florfenicol, Brain Heart Infusion medium, and taurocholate.
These tools and compounds can be used in conjunction with thiamphenicol research to optimize experimental design, improve experimental conditions, and enhance the overall understanding of this important antibiotic.