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Kanamycin Sulfate

Kanamycin Sulfate is a broad-spectrum aminoglycoside antibiotic derived from the bacterium Streptomyces kanamyceticus.
It is commonly used in research and clinical settings to select for bacterial cells that have been transformed with recombinant DNA.
Kanamycin Sulfate inhibits protein synthesis by binding to the 30S subunit of the bacterial ribosome, making it effective against both Gram-positive and Gram-negative bacteria.
Its use as a selectable marker has been instrumental in advancements in molecular biology and genetic engineering.
Reserchers can optimize Kanamycin Sulfate protocols using PubCompare.ai to identify the most accurate and reproducible methods from literature, pre-prints, and patents, enhancing the accuracy and reproducibility of their work.

Most cited protocols related to «Kanamycin Sulfate»

1
Yeast Genetic Marker Mutagenesis Protocol
Standard techniques were used for DNA manipulation. Restriction enzymes were
purchased from New England Biolabs, except for PfoI, which was
purchased from Fermentas. Ligations were performed using T4 DNA ligase purchased from
Invitrogen. Both PCR-mediated site-directed mutagenesis and gene amplification for
cloning purposes were performed using either cloned Pfu Turbo DNA
polymerase (Stratagene) or KOD HotStart DNA polymerase (Toyobo, Novagen/EMD
Chemicals). Antarctic phosphatase (New England Biolabs) was used to treat symmetrical
ends of plasmids cut with a single restriction enzyme to prevent recircularization.
Plasmid propagation was carried out in Invitrogen MAX Efficiency DH5α bacteria
grown in lysogeny broth (LB) (Bertani 2004 (link))
supplemented with either 50–100 μg/ml ampicillin sodium salt or 10
μg/ml kanamycin sulfate purchased from Sigma-Aldrich. Bacterial transformants
were selected for on LB 2% agar plates supplemented with either 100 μg/ml
ampicillin sodium salt or 60 μg/ml kanamycin sulfate.
Plasmid construction details are provided in supporting information, File S1. In general, we followed the strategy employed for mutagenesis
of TRP1, LEU2, and URA3 during construction of the YXplac plasmids (Gietz and Sugino 1988 (link)). We used silent
mutations that preserve the amino acid sequence to mutagenize restriction sites found
in the open reading frame of the yeast-selectable auxotrophic marker genes
ADE2, HIS3, TRP1, LEU2, URA3, ADE1, and HIS2 (Table S1). As for the few sites occurring in the untranslated regions
of these genes, we used neutral changes that should not affect either transcription
initiation or termination. Oligonucleotides used for site-directed mutagenesis are
listed in Table S2.
Chee M.K, & Haase S.B. (2012). New and Redesigned pRS Plasmid Shuttle Vectors for Genetic Manipulation of Saccharomyces cerevisiae. G3: Genes|Genomes|Genetics, 2(5), 515-526.
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Publication 2012
Agar Amino Acid Sequence Bacteria DNA-Directed DNA Polymerase DNA Restriction Enzymes Gene Amplification Genes Kanamycin Sulfate Ligation Lysogeny Mutagenesis, Site-Directed Oligonucleotides Phosphoric Monoester Hydrolases Plasmids Sodium Sodium, Ampicillin Sodium Chloride T4 DNA Ligase tyrosinase-related protein-1 Yeast, Dried
2
Plasmid Construction and Bacterial Transformation
Phusion® High Fidelity Polymerase (Thermo Scientific) and primers synthesized by Integrated DNA Technologies (IDT) or Eurofins Genomics were used in all PCR amplifications for plasmid construction. Plasmids were constructed using NEBuilder® HiFi DNA Assembly Master Mix (New England Biolabs – NEB) or T4 DNA ligase (NEB) according to manufacturer's instructions. Plasmids were transformed into either competent Top10 (Life Technologies), NEB 5-alpha F’Iq (NEB), or Epi400 (Epicentre Biotechnologies) Escherichia coli according to manufacturer's instructions. Transformants were selected on LB (Miller) agar plates containing 50 mg/L kanamycin sulfate for selection and incubated at 37 °C. Plasmids were constructed using a combination of ligation of phosphorylated oligonucleotides, DNA synthesis by GenScript and IDT and Gibson Assembly. Sequences of all plasmids were confirmed using Sanger sequencing performed by GenScript or Eurofins Genomics. Annotated plasmid sequences are provided in Supplemental File 1.
Elmore J.R., Furches A., Wolff G.N., Gorday K, & Guss A.M. (2017). Development of a high efficiency integration system and promoter library for rapid modification of Pseudomonas putida KT2440. Metabolic Engineering Communications, 5, 1-8.
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Publication 2017
Agar DNA Replication Escherichia coli Kanamycin Sulfate Ligation Oligonucleotide Primers Oligonucleotides Plasmids T4 DNA Ligase
3
Comparative Swab Sampling for Swine Influenza
During June–August 2013, 553 paired nasal swabs and snout wipes were taken congruently from pigs at the end of 29 agricultural fairs across Ohio and Indiana. Each pig was restrained with a snare and a polyester-tipped swab was inserted into both nares of the pig after which the nasal swab was placed in an individual vial containing 1·8 ml of VTM. A snout wipe was collected from the same pig by wiping a 2 in. × 2 in (5·08 cm × 5·08 cm) sterile cotton gauze pad across the pig's snout with a gloved hand (Figure1). Gauze was placed in a sterile HDPE storage pot containing 5 ml VTM. Gloves were changed between pigs, and the snare was disinfected with Wexcide (Wexford Labs, Kirkwood, MO, USA). The order of nasal swab and snout wipe was alternated between pigs to correct for bias toward the sampling method used first on each pig. Nasal swab and snout wipe vials were frozen in the field on dry ice and stored at ≤−70°C until testing was conducted. Animals used in this study were included in protocol number 2009A0134-R1, which was approved by Institutional Animal Care and Use Committee of The Ohio State University.
The nasal swab samples were thawed in a 37°C dry bead bath, treated with amphotericin B (20 μg/ml), gentamicin sulfate (1000 μg/ml), and kanamycin sulfate (325 μg/ml) and vigorously agitated before centrifugation at 1200 g for 30 minutes at 4°C. Snout wipe samples were also thawed at 37°C after which they were treated with amphotericin B (22·5 μg/ml), gentamicin sulfate (1000 μg/ml), and kanamycin sulfate (325 μg/ml). A slightly higher concentration of amphotericin B was used for the snout wipes due to increased risk of fungal contamination from environmental debris. Due to the flat bottom of the HDPE vials and the volume of VTM, the snout wipes were not centrifuged like the nasal swabs.
Viral transport media supernatants from the nasal swab and snout wipes underwent testing by real-time reverse transcription PCR (rRT-PCR) using the VetMAX™-Gold SIV Detection Kit (Life Technologies) and were inoculated in quadruplicate onto monolayers of serum-free adapted and maintained Madin-Darby canine kidney cells, on 24-well plates.15 The rRT-PCR and virus isolation results from nasal swabs and snout wipes were cross-tabulated and compared using the kappa static.17
Edwards J.L., Nelson S.W., Workman J.D., Slemons R.D., Szablewski C.M., Nolting J.M, & Bowman A.S. (2014). Utility of snout wipe samples for influenza A virus surveillance in exhibition swine populations. Influenza and Other Respiratory Viruses, 8(5), 574-579.
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Publication 2014
Amphotericin B Animals Bath Centrifugation Dry Ice Freezing Gold Gossypium Institutional Animal Care and Use Committees isolation Kanamycin Sulfate Madin Darby Canine Kidney Cells Nose Pigs Polyesters Polyethylene, High-Density Real-Time Polymerase Chain Reaction Reverse Transcription Serum SNAP Receptor Sterility, Reproductive Sulfate, Gentamicin Virus
4
Purification of Mouse SNARE Complexes
Full-length mouse VAMP2 with a COOH-terminal his6-tag was expressed in E. coli from plasmid pTW2 and purified as described (Weber et al. 1998). The t-SNARE complex between mouse his6–SNAP-25 and rat syntaxin1A was expressed and purified as follows:
A 100-ml preculture of BL21(DE3) cells transformed with plasmid pTW34 (Parlati et al. 1999) was grown overnight at 37°C in Luria-Bertani (LB) medium containing 0.5% (wt/vol) glucose and 50 μg/ml kanamycin. This preculture was used to inoculate a 12-l containing the same medium. After overnight growth at 37°C, this culture was used to seed 300 l of LB medium containing 50 μg/ml kanamycin. The cells were grown until they reached a density of 0.8 A260 and were then induced with isopropylthio-β-d-galactoside (IPTG) (0.2 mM final concentration). After 1 h at 37°C, an additional 15 g of kanamycin sulfate was added and the incubation continued for an additional 3.5 h. After centrifugation, the cell paste was frozen in liquid nitrogen in three aliquots.
One aliquot of this cell paste (∼900 g) was resuspended in 2 l of breaking buffer (25 mM Hepes/KOH, pH 7.40, 100 mM KCl, 10% [wt/vol] glycerol and 10 mM β-mercaptoethanol). After addition of 30 ml 200 mM PMSF in ethanol and 500 ml 20% (wt/vol) Triton X-100, the cells were disrupted by one passage through an Emulsiflex C5 cell disrupter (Avestin) at >10,000 psi. Cell debris was then removed by centrifugation in a GS3 rotor for 30 min at 8,000 rpm. The supernatant was additionally clarified by centrifugation in a Ti45 rotor for 45 min at 35,000 rpm. To this lysate, 30 ml packed Ni-NTA agarose (Qiagen) that has been washed first in breaking buffer containing 1% (wt/vol) Triton X-100 and 500 mM imidazole (pH adjusted to pH 7.5 with acetic acid) and then equilibrated with breaking buffer containing 1% (wt/vol) Triton X-100 was added. After mixing gently overnight at 4°C on an orbital shaker, the slurry was poured into a column and successively washed with 300 ml of (a) breaking buffer containing 1% (wt/vol) TX-100, (b) breaking buffer containing 1% (wt/vol) n-octyl-β-d-glucopyranoside, and (c) breaking buffer containing 50 mM imidazole and 1% (w/v) n-octyl-β-d-glucopyranoside. Finally, the t-SNARE complex was eluted with a linear gradient (∼250 ml) to breaking buffer containing 500 mM imidazole and 1% (wt/vol) n-octyl-β-d-glucopyranoside. All fractions containing significant amounts of t-SNARE complex were pooled. In an effort to remove heat-shock proteins, 1 mM in MgCl2 and 100 mg ATP-agarose (Sigma) was added to the pooled fractions. After overnight incubation at 4°C on a turning wheel, the beads were removed by filtration and the t-SNARE complex frozen in 550 μl aliquots that were stored at −80°C. The protein concentration was determined according to Schaffner and Weissmann (1973) using a bovine IgG as a standard, and was found to be 1.19 mg/ml.
The complex between his6–SNAP-25 and a thrombin-cleavable version of syntaxin1A was expressed in E. coli from the polycistronic plasmid pTW69 purified by Ni-nitrilotriacetic acid (Ni-NTA) affinity chromatography (Parlati et al. 1999). All membrane proteins and protein complexes were purified in 1% (wt/vol) n-octyl-β-d-glucopyranoside. His6-NSF-myc (Söllner et al. 1993a) and his6-αSNAP (Whiteheart et al. 1993) were expressed in E. coli and purified as described in Whiteheart et al. 1994 and Whiteheart et al. 1993, respectively, with the following modifications: the final gel filtration step in the purification of NSF was omitted and NSF was dialyzed against 25 mM Hepes/KOH, pH 7.5, 150 mM KCl, 1 mM DTT, 1 mM MgCl2, 0.5 mM ATP, 15% glycerol, and αSNAP was dialyzed against 25 mM Hepes/KOH, pH 7.8, 100 mM KCl, 1 mM DTT, 10% glycerol. The expression clone for his6–BoNT D light chain was a kind gift of Dr. Heiner Niemann (Medizinische Hochschale Hannover, Department of Biochemistry, Hannover, Germany) and the protein was expressed and purified as described (Glenn and Burgoyne 1996). The cytosolic domain of VAMP2 (amino acids 1–94) was expressed in E. coli from plasmid pET-rVAMP2CD and purified as described (Weber et al. 1998).
Weber T., Parlati F., McNew J.A., Johnston R.J., Westermann B., Söllner T.H, & Rothman J.E. (2000). Snarepins Are Functionally Resistant to Disruption by Nsf and αSNAP. The Journal of Cell Biology, 149(5), 1063-1072.
Publication 2000
2-Mercaptoethanol Acetic Acid Amino Acids ATP-sepharose Bos taurus Buffers Cells Centrifugation Chromatography, Affinity Clone Cells Cytosol Escherichia coli Ethanol Filtration Freezing Galactosides Gel Chromatography Glucose Glycerin Heat Shock Proteins HEPES his6 tag imidazole Kanamycin Kanamycin Sulfate Magnesium Chloride Membrane Proteins Mus Nitrilotriacetic Acid Nitrogen Paste Plasmids polyethylene glycol monooctylphenyl ether Proteins Sepharose SNAP25 protein, human SNAP Receptor Target Membrane SNARE Proteins Thrombin TNFSF14 protein, human Triton X-100 Vesicle-Associated Membrane Protein 2
5
Characterization of C. pseudotuberculosis Mutants
The following strains were used: the previously generated C. pseudotuberculosis TnFuZ recombinant strains [3 (link)], the T1 pathogenic wild-type parental strain and the caprine-pathogenic MIC-6 strain. The strains were grown aerobically in Brain Heart Infusion broth (BHI, Oxoid Ltd., Hampshire, England) at 37 °C. The mutant strains were grown in the presence of kanamycin (kanamycin sulphate, 25 μg/mL; solid and liquid media) and 5-bromo-4-chloro-3-indolylphosphate (BCIP, 40 μg/mL; Sigma-Aldrich Co., St. Louis, MO, USA; solid medium), a substrate that allows the recovery of C. pseudotuberculosis insertional mutant colonies with positive alkaline phosphatase activity.
Ribeiro D., Rocha F.D., Leite K.M., Soares S.D., Silva A., Portela R.W., Meyer R., Miyoshi A., Oliveira S.C., Azevedo V, & Dorella F.A. (2014). An iron-acquisition-deficient mutant of Corynebacterium pseudotuberculosis efficiently protects mice against challenge. Veterinary Research, 45(1), 28.
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Publication 2014
Alkaline Phosphatase Brain Goat Heart Kanamycin Kanamycin Sulfate Parent Pathogenicity Strains Yersinia pseudotuberculosis Infections

Most recents protocols related to «Kanamycin Sulfate»

1
Isolating Menstrual Blood-Derived Stem Cells
MenSCs were provided by the Innovative Precision Medicine (IPM) Group, and the specific process of obtaining cells was as above [37 (link), 47 (link), 48 (link)]. In brief, menstrual blood samples were collected from healthy young women (n = 3) aged 20 to 30 years during menstruation using Divacup (Kitchener, ON). Fresh menstrual blood samples should not be stored for more than 72 hours in a storage solution containing kanamycin sulfate, cefadroxil, vancomycin hydrochloride, amphotericin B, gentamicin sulfate, and heparin in a 4°C refrigerator. Stem cells in menstrual blood were obtained by density gradient centrifugation with Ficoll-Hypaque (DAKEWE, China). The isolated interlayer cells were cultured in Minimum Essential Medium α (MEMα) (Gibco, USA) adding 15% Australian fetal bovine serum (FBS). MenSCs were completely digested with 0.25% trypsin-EDTA (Fisher Scientific, USA) for 5 min, then neutralized with complete medium, and centrifuged to complete subculture. Passages 5-8 (p5-p8) of MenSCs can be used for collection of small EVs.
Xu H., Fu J., Chen L., Zhou S., Fang Y., Zhang Q., Chen X., Yuan L., Li Y., Xu Z, & Xiang C. (2023). TNF-α Enhances the Therapeutic Effects of MenSC-Derived Small Extracellular Vesicles on Inflammatory Bowel Disease through Macrophage Polarization by miR-24-3p. Stem Cells International, 2023, 2988907.
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Publication 2023
Amphotericin B BLOOD Cefadroxil Cells Centrifugation, Density Gradient Edetic Acid Fetal Bovine Serum Ficoll Heparin Hydrochloride, Vancomycin Hypaque Kanamycin Sulfate Menstruation Peripheral Blood Stem Cells Physiology, Cell Precision Medicine Sulfate, Gentamicin Trypsin Woman
2
Probiotic Strains Impact on Gut Microbiome
All animal experiments were conducted according to the Danish guidelines for experimental animal welfare, and the study protocols were approved by the Danish Animal Experiment Inspectorate (license number 2020-15-0201-00405). The study was carried out in accordance with the ARRIVE guidelines (du Sert et al., 2020). All in vivo experiments were conducted on male C57BL/6 mice (6−8 weeks old; Taconic Bioscience). Unless otherwise stated, all mice were housed at room temperature on a 12-h light/dark cycle and given ad libitum access to water and standard chow (Safe Diets, A30). All mice were randomised according to body weight and acclimated for at least 1 week prior to the first oral administration. Each animal study received a freshly prepared batch of S. boulardii. Body weight and food intake were recorded once per week. The researchers were blinded in all mouse experiments. The mice were euthanised by cervical dislocation at the end of the study.
The mice were divided into four groups (n = 4), either receiving the Sb wild-type, Sb bts1∆, Sb thi6∆ or Sb bts1∆ + thi6∆ strain. The mice were orally administered via intragastric gavage with ∼108 CFU of the S. boulardii strain in 100 µL of 1x PBS and 20% glycerol. The mice were orally administered with S. boulardii for five consecutive days, followed by a 6-day washout. The drinking water was supplemented with an antibiotic cocktail containing 0.3 g/L ampicillin sodium salt, 0.3 g/L kanamycin sulfate, 0.3 g/L metronidazole, and 0.15 g/L vancomycin hydrochloride after the washout period. After 5 days of antibiotic treatment, the mice were orally administered with S. boulardii in 100 µL of 1x PBS (containing 1.0 g/L ampicillin sodium salt, 1.0 g/L kanamycin sulfate, 1.0 g/L metronidazole, and 1.0 g/L vancomycin hydrochloride) and 10% glycerol for five consecutive days. The washout for the antibiotic-treated mice was monitored for 33 days.
The faeces were collected in pre-weighed 1.5 ml or 2.0 ml Eppendorf tubes containing 1 ml of 1x PBS and 25% glycerol and weighed again to determine the faecal weight. All sample preparation for assessing CFU numbers was kept on ice and followed the same practice. The faecal samples were homogenised by vortexed at ∼2,400 rpm for 20 min. The samples were then spun down at 100 g for 30 s, followed by a dilution series, where 5 µL of each dilution was plated in duplicates or triplicates. Under the antibiotic-treated washout period, 100 µL was plated. The faecal samples were plated on SC supplemented with 20 mg/L uracil plates containing 100 mg/L ampicillin, 50 mg/L kanamycin, and 30 mg/L chloramphenicol (Sigma Aldrich).
Hedin K.A., Kruse V., Vazquez-Uribe R, & Sommer M.O. (2023). Biocontainment strategies for in vivo applications of Saccharomyces boulardii. Frontiers in Bioengineering and Biotechnology, 11, 1136095.
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Publication 2023
Administration, Oral Aftercare Ampicillin Animals Animals, Laboratory Antibiotics Chloramphenicol Diet Eating Feces Glycerin Hydrochloride, Vancomycin Joint Dislocations Kanamycin Kanamycin Sulfate Males Metronidazole Mice, House Mice, Inbred C57BL Neck Sodium, Ampicillin Sodium Chloride Strains Technique, Dilution Tube Feeding Uracil
3
Arabidopsis Promoter-GFP Fusion Constructs
The fusion gene constructs with various lengths of GLN1;2 (At1g66200), GLT1 (At5g53460) and GLU2 (At2g41220) promoters were generated as follows. The 5’-intergenic regions upstream of coding sequences of GLN1;2, GLT1 and GLU2 were amplified by polymerase chain reaction (PCR) from genomic DNA of Arabidopsis Col-0 accession and cloned as promoter fragments to generate the GFP reporter fusion constructs. PCR was carried out using KOD plus DNA polymerase (Toyobo, Osaka, Japan) and pairs of forward and reverse oligonucleotide (Table 1). The forward primers were designed for amplification of promoter fragments starting 3,583-bp upstream of the translation initiation site of GLN1;2, 2,814-bp, 2,200-bp, 2,100-bp, 2,000-bp, 1,930-bp, 1,730-bp, and 1,050-bp upstream of GLT1, and 1,358-bp upstream of GLU2. Among these forward primers, GLN1;2P3583L_F designed for the amplification of GLN1;2 promoter region has an overhang of a HindIII site (AAGCTT) at the 5’-end. The rest of the forward primers designed for the amplification of GLT1 and GLU2 promoter regions have an overhang of a BamHI site (GGATCC) at the 5’-end. The reverse primers were designed to have the complementary sequences with the 5’-untranslated regions immediately upstream of the translation initiation sites of GLN1;2, GLT1 and GLU2. These reverse primers have an overhang of an NcoI site (CCATGG) at the 5’-end. The ATG in the NcoI site is the translation initiation site for GFP. The amplified PCR products were subcloned into pCR-Blunt II-TOPO (Thermo Fisher Scientific K.K., Tokyo, Japan), and fully sequenced to confirm the identity. These promoter fragments were then cut out as a HindIII-NcoI fragment (for GLN1;2) or BamHI-NcoI fragments (for GLT1 and GLU2) and cloned into respective restriction sites of pTH-10KI, replacing the cauliflower mosaic virus (CaMV) 35S promoter, to obtain the promoter:GFP:teminator cassettes. pTH-10KI is the modified version of CaMV35S-synthetic GFP (sGFP, S65T) vector(Chiu et al., 1996 (link); Niwa et al., 1999 (link)) and has a full EGFP coding sequence (Takara Bio Inc. Shiga, Tokyo) between the 35S promoter and the nopaline synthase terminator (NosT). Finally, the promoter:GFP : NosT cassettes created in pTH-10KI were cut out as a HindIII-EcoRI fragment (for GLN1;2) or BamHI-EcoRI fragments (for GLT1 and GLU2) and cloned into pBI101 (Takara Bio Inc.). These binary vector plasmids were introduced into Agrobacterium tumefaciens GV3101 (pMP90) by freeze-thaw method as previously described (Ishiyama et al., 2004a (link)). Arabidopsis plants were transformed according to the floral dip method (Clough and Bent, 1998 (link)). Transgenic plants were selected on GM medium (Valvekens et al., 1988 (link)) containing 50 mg/L kanamycin sulfate. Kanamycin-resistant T2 progenies were used for analyses.
Kojima S., Minagawa H., Yoshida C., Inoue E., Takahashi H, & Ishiyama K. (2023). Coregulation of glutamine synthetase1;2 (GLN1;2) and NADH-dependent glutamate synthase (GLT1) gene expression in Arabidopsis roots in response to ammonium supply. Frontiers in Plant Science, 14, 1127006.
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Publication 2023
Agrobacterium tumefaciens Arabidopsis Cauliflower Mosaic Virus Cloning Vectors Decompression Sickness Deoxyribonuclease EcoRI DNA-Directed DNA Polymerase Exons Freezing Genes Genome Intergenic Region Kanamycin Kanamycin Sulfate nopaline dehydrogenase Oligonucleotide Primers Oligonucleotides Open Reading Frames Plants Plants, Transgenic Plasmids Topoisomerase II Transcription Initiation Site Untranslated Regions
4
Recombinant Protein Expression and Purification
The protein expression constructs were transformed into the BL21 (DE3) Rosetta strain (Merck Millipore). The selected bacterial cells carrying the constructs were inoculated into 30 mL liquid Luria-Bertani (LB) media containing the kanamycin sulphate antibiotic (30 μm/mL), 2% (v/v) glucose, and were grown overnight at 37 °C. The following day, cells were diluted to 200 mL with liquid LB media containing the same antibiotics, 0.4% (v/v) glucose, and grown until OD600 reached the 0.6 value. Protein expression was induced using 1 mM Isopropyl β- d-1-thiogalactopyranoside (IPTG; Thermo Fisher Scientific); then, the cells were incubated at 37 °C for 2 h with constant shaking. Expressed proteins were then purified with the HIS-Select nickel affinity gel (Sigma-Aldrich, St. Louis, MO, USA) following the manufacturer’s instructions. Purified proteins were concentrated using Amicon Ultra 0.5 mL filters (Merck Millipore); and then, stored in 40% (v/v) glycerol at −20 °C for later use.
Kenesi E., Kolbert Z., Kaszler N., Klement É., Ménesi D., Molnár Á., Valkai I., Feigl G., Rigó G., Cséplő Á., Lindermayr C, & Fehér A. (2023). The ROP2 GTPase Participates in Nitric Oxide (NO)-Induced Root Shortening in Arabidopsis. Plants, 12(4), 750.
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Publication 2023
Antibiotics Antibiotics, Antitubercular Bacteria Cells Glucose Glycerin Isopropyl Thiogalactoside Kanamycin Sulfate Nickel Proteins Strains
5
Antibiotic Susceptibility Profiling of Desulfovibrio desulfuricans
These assays, which were based on a previously published method [26 (link)], were performed. The initial OD600 values of D. desulfuricans ATCC 29577 and isolated strains were adjusted to about 0.4, and 10% of the inoculum was inoculated into the fresh medium containing different antibiotics. The following antibiotics were tested: Neomycin sulphate (40 μg/mL), Polymyxin B sulphate (25 μg/mL), Nisin (25 μg/mL), Ampicillin (25 μg/mL), Metronidazole (20 μg/mL), Kanamycin sulphate (20 μg/mL). The evaluation criteria of resistance were referred to as EUCAST (European Committee on Antimicrobial Susceptibility Testing). D. desulfuricans ATCC 29577 was included as a control. The culture medium without antibiotics was considered the blank group, and the medium without inoculation as the blank control group was cultured statically under anaerobic conditions at 37 °C. The growth curve was constructed according to the OD600 value measured at 0, 1, 2, 4, 8, 12, 16, 24, 30, 36, 48, 60, 72, 84, 96, 108, 120, 132, 144 h. Additionally, different concentrations of antibiotics (0.000, 0.125, 0.250, 0.500, 0.750, 1.000, 1.250, 2.500, 5.000, 7.500, 10.00, 12.50, 15.00, 20.00, 25.00, 30.00, 35.00, 40.00, 45.00, 50.00 μg/mL) were used to detect the minimum inhibitory concentration (MIC). OD600 value was measured at 0, 12, 24, 48, and 72 h.
Lu G., Zhang Y., Ren Y., Shi J.S., Xu Z.H, & Geng Y. (2023). Diversity and Comparison of Intestinal Desulfovibrio in Patients with Liver Cirrhosis and Healthy People. Microorganisms, 11(2), 276.
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Publication 2023
Ampicillin Antibiotics, Antitubercular Biological Assay Europeans Kanamycin Sulfate Metronidazole Microbicides Minimum Inhibitory Concentration Neomycin Sulfate nisin A Polymyxin B Sulfate Strains Susceptibility, Disease Vaccination

Top products related to «Kanamycin Sulfate»

1
Kanamycin sulfate by Merck Group
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Kanamycin sulfate is a broad-spectrum antibiotic used in laboratory research and applications. It is a white to off-white crystalline powder that is soluble in water. Kanamycin sulfate is commonly used as a selective agent in cell culture and molecular biology experiments.
2
Kanamycin sulfate by Thermo Fisher Scientific
Sourced in United States, United Kingdom
Kanamycin sulfate is a broad-spectrum aminoglycoside antibiotic used in various laboratory applications. It functions as a selective agent in cell culture and molecular biology techniques, inhibiting the growth of gram-negative bacteria.
3
Chloramphenicol by Merck Group
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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.
4
Kanamycin sulphate by Merck Group
Sourced in United States
Kanamycin sulphate is a broad-spectrum aminoglycoside antibiotic used in laboratory settings. It functions as a protein synthesis inhibitor, preventing bacterial growth.
5
Tetracycline by Merck Group
Sourced in United States, Germany, United Kingdom, France, Australia, Italy, China, Switzerland, Denmark, India, Czechia, Poland, Sao Tome and Principe, Japan, Sweden
Tetracycline is a type of antibiotic used for laboratory testing and research. It is a broad-spectrum antimicrobial agent effective against a variety of bacteria. Tetracycline is commonly used in microbiological studies and antimicrobial susceptibility testing.
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Gentamicin sulfate by Merck Group
Sourced in United States, Germany, Brazil, United Kingdom
Gentamicin sulfate is a broad-spectrum antibiotic used in various laboratory and research applications. It is a aminoglycoside compound derived from the bacterium Micromonospora. Gentamicin sulfate is commonly used as a selective agent in cell culture and molecular biology experiments to inhibit the growth of Gram-negative bacteria.
7
Ampicillin by Merck Group
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Ampicillin is a broad-spectrum antibiotic used in laboratory settings. It is a penicillin-based compound effective against a variety of gram-positive and gram-negative bacteria. Ampicillin functions by inhibiting cell wall synthesis, leading to bacterial cell lysis and death.
8
Kanamycin sulfate by Fujifilm
Sourced in Japan
Kanamycin sulfate is a broad-spectrum antibiotic used as a selective agent in microbiological procedures. It inhibits protein synthesis in bacteria, making it effective against a variety of gram-positive and gram-negative organisms. Kanamycin sulfate is commonly used in cell and molecular biology applications, such as the selection of transformed bacterial cells.
9
Streptomycin sulfate by Merck Group
Sourced in United States, Germany, Italy, Spain, Macao, United Kingdom, Sao Tome and Principe, Canada, China, Israel
Streptomycin sulfate is a white to pale yellow, crystalline powder. It is a broad-spectrum antibiotic that is effective against various bacteria, including Gram-positive and Gram-negative species.
10
Ampicillin sodium salt by Merck Group
Sourced in United States, Spain, Germany, China, United Kingdom
Ampicillin sodium salt is a powdered form of the antibiotic ampicillin. It is used as a laboratory reagent for microbiology and biochemistry applications.

More about "Kanamycin Sulfate"

Kanamycin Sulfate, also known as Kanamycin Sulphate or Kanamycin, is a broad-spectrum aminoglycoside antibiotic derived from the bacterium Streptomyces kanamyceticus.
It is commonly used in research and clinical settings as a selectable marker, allowing scientists to identify bacterial cells that have been transformed with recombinant DNA.
Kanamycin Sulfate works by inhibiting protein synthesis in bacteria.
It binds to the 30S subunit of the bacterial ribosome, making it effective against both Gram-positive and Gram-negative bacteria.
This mode of action is similar to other aminoglycoside antibiotics like Gentamicin Sulfate and Streptomycin Sulfate.
The use of Kanamycin Sulfate as a selectable marker has been instrumental in advancements in molecular biology and genetic engineering.
Researchers can optimize Kanamycin Sulfate protocols using PubCompare.ai, an AI-driven platform that helps identify the most accurate and reproducible methods from literature, pre-prints, and patents.
This enhances the accuracy and reproducibility of research involving Kanamycin Sulfate, as well as other antibiotics like Chloramphenicol, Tetracycline, and Ampicillin Sodium Salt.
By leveraging the insights and comparisons provided by PubCompare.ai, researchers can ensure that their Kanamycin Sulfate-based experiments are conducted using the most effective and reliable protocols, leading to more robust and reliable results.