Kanamycin

Manufactured by Sangon

Sourced in China

Kanamycin is a broad-spectrum antibiotic commonly used in laboratory settings. It functions as a selective agent, allowing for the identification and growth of bacterial cells that have been genetically modified to express resistance to the antibiotic.

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Lab products found in correlation

Ampicillin, by Sangon (21 mentions) Chloramphenicol, by Sangon (10 mentions) Isopropyl β d 1 thiogalactopyranoside (iptg), by Sangon (7 mentions) Gentamicin, by Sangon (7 mentions) Streptomycin, by Sangon (7 mentions) T4 dna ligase, by Takara Bio (6 mentions) Tetracycline, by Sangon (5 mentions) Vancomycin, by Sangon (5 mentions) Spectinomycin, by Sangon (4 mentions) Restriction enzyme, by Takara Bio (4 mentions) Erythromycin, by Sangon (4 mentions) Dulbecco s modified eagle medium dmem, by Thermo Fisher Scientific (3 mentions) Dna polymerase, by Takara Bio (3 mentions) Hygromycin, by Sangon (3 mentions) Rifampicin, by Sangon (3 mentions) Ciprofloxacin, by Sangon (3 mentions) Amikacin, by Sangon (3 mentions) Restriction endonuclease, by Takara Bio (3 mentions) Dna gel extraction kit, by Takara Bio (3 mentions) Tryptone, by Sangon (3 mentions)

Close spelling variants of this product

Kanamycin sulfate (9 citations) Kanamycin (Kan; (3 citations)

57 protocols using kanamycin

Screening and Characterization of Marine Xylanases

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Microbial strains, Plasmids and Chemicals. Several marine microorganisms (named: HY30, HY31, HY32, HY33, HY34, HY35 and HY36 ) have been screened from Yantai(China), and E. coli DH5α and E. coli BL21(DE3) were purchased from Novagen (USA) and used for gene cloning and expression, respectively. pET28a (+) vector was purchased from Invitrogen. (Waltham, MA, USA). Luria-Bertani (LB) medium was prepared for cultivating E. coli. SanPrep column DNA gel extraction kit, kanamycin, and medium components were purchased from Sangon (Shanghai, China).
Bovine serum albumin, D-xylose, and birchwood xylans were purchased from Sigma (Luis, USA). Ni-NTA His-Bind metal chelating column was purchased from GE Healthcare (USA). All other reagents were domestic analytical pure products. Xylan medium (1 L): xylan 1 g, yeast extract 0.1 g, tryptone 0.1 g, NaCl 2 g, and agar powder 15 g.

Tian Y., Xu J., Shi J., Kong M., Guo C., Cui C., Wang Y., Wang Y, & Zhou C. (2022). Cloning, Expression, and Characterization of a GHF 11 Xylanase from Alteromonas macleodii HY35 in Escherichia coli. The Journal of general and applied microbiology, 68(3).

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Cultivation and Maintenance of Streptococcus suis

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S. suis strains were maintained and grown in Todd-Hewitt broth (THB; OXOID, England) plus 5% fetal bovine serum (THB + 5% FBS) at 37°C. Solid media contained 2% agar. S. suis 05ZYH33 (isolated from a clinical patient with meningitis) and S. suis SC19 (isolated from a clinical diseased pig) were kindly provided by Professor Y. Feng (Zhejiang University) and Professor C. Tan (Huazhong Agricultural University), respectively. Escherichia coli strains Top10 and BL21(DE3) were cultured in Lysogeny Broth (LB) medium or plated on LB agar at 37°C. When required, differential final concentrations of antibiotics (Sangon, Shanghai, China) were added into the medium as follows: for S. suis, spectinomycin at 100 μg/mL; for E. coli, spectinomycin at 50 μg/mL, ampicillin at 100 μg/mL, and kanamycin at 50 μg/mL.

Xu Q., Chen H., Sun W., Zhang Y., Zhu D., Rai K.R., Chen J.L, & Chen Y. (2021). sRNA23, a novel small RNA, regulates to the pathogenesis of Streptococcus suis serotype 2. Virulence, 12(1), 3045-3061.

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Protein Expression and Purification Protocol

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Sodium phenylpyruvate (PPA), β-nicotinamide adenine dinucleotide disodium salt (NADH), kanamycin and Ni-TED pre-packed gravity column (5 ml) were purchased from Sangon Biotech (Shanghai, China) Co., Ltd. Tryptone and yeast extract were obtained from Oxoid Co., Ltd (United Kingdom). PrimeSTAR^® HS DNA polymerase, QuickCut™ restriction enzymes, PCR reagents, loading buffers for nucleic acid electrophoresis and SDS-PAGE, DNA and protein markers, as well as the Bradford protein assay kit were purchased from Takara Biotechnology (Dalian, China) Co., Ltd. The plasmid miniprep kits were purchased from Axygen Biotechnology (Hangzhou, China) Co., Ltd. Oligonucleotide synthesis and DNA sequencing were conducted by Sangon Biotech Co., Ltd (Shanghai, China). Unless specified otherwise, all other reagents and chemicals used in this study were obtained from general commercial suppliers and used without further purification.
E. coli BL21 (DE3) and pET-28a (+) were used as the host strain and vector for protein expression. The plasmid pET28a-lrldh with the lactic dehydrogenase gene from Lactobacillus rossiae was used as the template for the site-saturation mutagenesis.
The engineered E. coli strains were grown in Luria-Bertani (LB) medium (0.5% yeast extract, 1.0% tryptone and 1.0% NaCl), supplemented with 50 μg ml⁻¹ kanamycin.

Luo X., Wang Y., Zheng W., Sun X., Hu G., Yin L., Zhang Y., Yin F, & Fu Y. (2022). Simultaneous improvement of the thermostability and activity of lactic dehydrogenase from Lactobacillus rossiae through rational design. RSC Advances, 12(51), 33251-33259.

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Purification of Recombinant Proteins

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Restriction enzymes, BamH I, Hind III, Nde I, and Xho I, and T4 DNA ligase were purchased from New England Biolabs. Pfu DNA polymerase, dNTPs, isopropyl β-D-thiogalactoside (IPTG), Triton X-100, imidazole, ampicillin, and kanamycin were purchased from Sangon (Shanghai, China). Ni-NTA resin was purchased from Qiagen. All other reagents were of analytical grade. The pET-41b plasmid and Escherichia coli BL21(DE3) strain, pQE30 plasmid, and M15 strain (Novagen) were used as expression vectors and host strains. The pGEX-B plasmid was constructed in our lab. YM-5 ultrafiltration membrane was from Amicon. Sephadex G-25 was purchased from Pharmacia Biotech. Low- and mid-range protein markers were obtained from Bio Basic Inc.

Zhao D, & Huang Z. (2016). Effect of His-Tag on Expression, Purification, and Structure of Zinc Finger Protein, ZNF191(243-368). Bioinorganic Chemistry and Applications, 2016, 8206854.

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Recombinant Protein Expression Protocols

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ChFatB2 excluding the transit peptide (residues 129–395) was constructed on the pCold II vector and transformed into E. coli BL21 (DE3) for protein expression, as described previously [24 (link)]. For the expression of holo-ACP, pET28a_EcACP was transferred into the host strain BAP1, which contained a chromosomal insertion of the Bacillus subtilis Sfp gene, as described [37 (link)]. Moreover, pET28a_ClACP2 (Uniport No. P52412) with residues 54–137 was expressed in consistency with EcACP. Chemical reagents including ampicillin, kanamycin, Bradford, and DTT are purchased from Sangon Biotech in Shanghai, China.

Yang T., Yang Y., Yang M., Ren J., Xue C., Feng Y, & Xue S. (2023). Conformational Changes of Acyl Carrier Protein Switch the Chain Length Preference of Acyl-ACP Thioesterase ChFatB2. International Journal of Molecular Sciences, 24(7), 6864.

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Recombinant Protein Expression and Purification

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The verified plasmids were transformed into E. coli BL21 (DE3) cells, which was then cultured in LB medium supplemented with 50 μg/mL kanamycin (Sangon Biotech, Shanghai, China) at 37°C until OD₆₀₀ = 0.6–0.8, followed by inducing expressing using 0.5 mM isopropyl-β-D-1-thiogalactopyranoside (IPTG; Sangon Biotech, Shanghai, China) for 20 h at 20°C. E. coli BL21 (DE3) cells were harvested by centrifugation and resuspended in lysis buffer (50 mM NaH₂PO₄ and 300 mM NaCl at pH 8.0). After ultrasonic fragmentation, the His-tagged proteins were purified using a Ni Sepharose 6 Fast Flow column (GE Healthcare, Uppsala, Sweden). The eluent was replaced with PC buffer (20 mM sodium phosphate and 10 mM citrate at pH 6.0) and then filtered using a 3 kDa cutoff membrane (Millipore, Billerica, MA, United States) at 4°C. The protein obtained was analyzed by sodium dodecyl sulfate-polyacrylamide gel electrophoresis. Protein concentrations were determined using the Bradford method (Bradford, 1976 (link)).

Wu X., Zhang Q., Zhang L., Liu S., Chen G., Zhang H, & Wang L. (2020). Insights Into the Role of Exposed Surface Charged Residues in the Alkali-Tolerance of GH11 Xylanase. Frontiers in Microbiology, 11, 872.

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Efficient Production of Antimicrobial Peptides

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Pseudomonas aeruginosa JCM5962 was preserved in our laboratory; E. coli DH5α and BL21(DE3) competent cells were purchased from Tiangen Biotech (China). Dulbecco’s-modified eagle medium (DMEM) and Fetal bovine serum (FBS) were purchased from Gibco (United States). The crystal violet, kanamycin, and gentamicin were obtained from Sangon Biotech Co. (China). Fluorescein isothiocyanate-labeled concanavalin A (FITC-ConA), 4′,6-diamidino-2-phenylindole (DAPI), Nile red, and SYPRO red were purchased from Sigma-Aldrich Co. (USA). The N-Phenyl-1-naphthylamine (NPN) and 3,3′- Dipropylthiadicarbocyanine iodide (DiSC₃-5) were purchased from Aladdin (China). All other chemicals and reagents used in this study were of reagent grade.
PEW300 peptide was produced by our previous established protein expression and purification system (Wang et al., 2018 (link)). In this system, a high yield of AMPs can be acquired by simple centrifugation, with no expensive steps like NTA affinity chromatography and high-performance liquid phase separation. Purified PEW300 was dialyzed to PBS buffer and stored at-80°C for further experiment.

Wang M., Deng Z., Li Y., Xu K., Ma Y., Yang S.T, & Wang J. (2022). Antibiofilm property and multiple action of peptide PEW300 against Pseudomonas aeruginosa. Frontiers in Microbiology, 13, 963292.

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Bacterial Cultivation and Antibiotic Selection

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The M. smegmatis and E. coli strains and plasmids used in this study are shown in Table S1. The E. coli strain DH5α was used for cloning. E. coli strains were grown on LB broth agar or in LB broth, 37 °C, 200 rpm. M. smegmatis mc² 155 was grown in 7H9 liquid medium (Difco) supplemented with 0.05% w/v Tween 80, 0.5% glycerol, and 0.5% glucose or was grown on 7H10 agar supplemented with 1% glycerol and 0.5% glucose. Restriction enzymes, T4 DNA ligases, and DNA polymerases were purchased from Takara. Ampicillin, kanamycin, hygromycin were bought from Sangon Biotech Co., whose stock solutions were freshly prepared and filter sterilized. When required, the following antibiotics were used at the final concentration: Ampicillin, 100 μg/mL; kanamycin, 500 μg/mL for E. coli or 200 μg/mL for M. smegmatis; hygromycin, 50 μg/mL. All cultures were incubated at 37 °C.

Duan X., Huang X., Xu J., Li X., Niu J., Du X., Wang X., Li J., Kelly M., Guo J., Zhang K., Huang Y., Kan B, & Xie J. (2022). ArsR Family Regulator MSMEG_6762 Mediates the Programmed Cell Death by Regulating the Expression of HNH Nuclease in Mycobacteria. Microorganisms, 10(8), 1535.

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Antibiotic Resistance Profiling of L. sakei

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The predicted antibiotic resistance gene information in the genome was obtained by comparing the amino acid sequences of the strains with the comprehensive antibiotic research database (CARD, http://arpcard.mcmaster.ca, accessed on 24 May 2021) [51 (link)]. The strains were clustered using HemI software [50 (link)].
The microbroth dilution method was used to determine antibiotic resistance of L. sakei according to ISO 10932:2010 [52 ]. The following 11 antibiotics were detected: chloramphenicol, rifampicin, streptomycin, kanamycin, gentamycin, tetracycline, clindamycin, neomycin, erythromycin, ciprofloxacin, and vancomycin (all purchased from Sangon Biotech Co., Ltd., Shanghai, China). OD₆₂₅ was determined using an enzyme-labeled instrument (Varioskan Lux, Thermo, Waltham, MA, USA) to determine the MIC of strain to antibiotics.

Chen Y., Li N., Zhao S., Zhang C., Qiao N., Duan H., Xiao Y., Yan B., Zhao J., Tian F., Zhai Q., Yu L, & Chen W. (2021). Integrated Phenotypic–Genotypic Analysis of Latilactobacillus sakei from Different Niches. Foods, 10(8), 1717.

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Glycerol-based Carbohydrate Protocols

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Glycerol was purchased from Greagent (Shanghai, China). Isopropyl-β-D-1-thiogalactopyr-anoside (IPTG) and the antibiotics, including ampicillin, streptomycin, and kanamycin, were all supplied from Sangon Biotech (Shanghai, China). D-Sorbose and D-allulose were purchased from Tokyo Chemical Industry (Tokyo, Japan). All other chemicals were of analytical grade and available from commercial sources.

Gao Y., Chen Z., Nakanishi H, & Li Z. (2023). Highly Efficient Synthesis of Rare Sugars from Glycerol in Endotoxin-Free ClearColi by Fermentation. Foods, 12(16), 3078.

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