Cells were routinely grown in LB medium containing 1% Bacto Tryptone (Difco), 0.5% yeast extract (Difco), and 0.5% NaCl with or without antibiotics at 50 μg/ml for ampicillin (Wako, Osaka, Japan) and 30 μg/ml for kanamycin (Wako, Osaka, Japan). Glucose, L -arabinose, and other chemicals were from Wako (Osaka, Japan). DpnI was from New England Biolabs (MA, USA); Taq polymerase, TaKaRa Ex Taq, and agarose, SeaKem GTG Agarose from Takara Shuzo Inc. E-Gel 96 systems were from Invitrogen. MOPS medium was prepared as described elsewhere (Wanner, 1994 ).
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Chemicals & Drugs
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Antibiotic
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Kanamycin
Kanamycin
Kanamycin is an aminoglycoside antibiotic derived from the bacterium Streptomyces kanamyceticus.
It is commonly used in molecular biology and genetics research to select for cells that have been succesfully transfected or transformed with recombinant DNA.
Kanamycin works by inhibiting protein synthesis in bacterial cells, making it an effective selection marker.
Researchers can use kanamycin-resistance genes as selectable markers when engineering plasmids or other vectors.
This allows them to identify and isolate cells that have incorporated the desired genetic material.
Kanamycin is also used clinically to treat certain bacterial infections, though its usage is more limited due to potential toxicity and the rise of antibiotic resistance.
Optimizing kanamycin protocols is crucial for streamlining genetic engineering workflows and ensuring the success of experimental procedures.
It is commonly used in molecular biology and genetics research to select for cells that have been succesfully transfected or transformed with recombinant DNA.
Kanamycin works by inhibiting protein synthesis in bacterial cells, making it an effective selection marker.
Researchers can use kanamycin-resistance genes as selectable markers when engineering plasmids or other vectors.
This allows them to identify and isolate cells that have incorporated the desired genetic material.
Kanamycin is also used clinically to treat certain bacterial infections, though its usage is more limited due to potential toxicity and the rise of antibiotic resistance.
Optimizing kanamycin protocols is crucial for streamlining genetic engineering workflows and ensuring the success of experimental procedures.
Most cited protocols related to «Kanamycin»
Ampicillin
Antibiotics, Antitubercular
Arabinose
Cells
Glucose
Kanamycin
morpholinopropane sulfonic acid
Sepharose
Sodium Chloride
Taq Polymerase
Yeast, Dried
Nicotiana benthamiana plants were grown in a glasshouse at 22°C and using natural light with daylight extension to 16 h. Plants were grown until they had six leaves and the youngest leaves over 1 cm long were infiltrated with Agrobacterium and maintained in the glasshouse for the duration of the experiment.
Agrobacterium tumefaciens, GV3101(MP90) [25 ] were cultured on Lennox agar (Invitrogen) supplemented with 50 μg.ml-1 kanamycin (Sigma) and incubated at 28°C. A 10 μl loop of confluent bacterium were re-suspended in 10 ml of infiltration media (10 mM MgCl2, 0.5 μM acetosyringone), to an OD600 of 0.2, and incubated at room temperature without shaking for 2 h before infiltration. Infiltrations were performed according to the methods of Voinnet et al. (2003) [5 (link)]. Approximately 300 μl of this Agrobacterium mixture was infiltrated into a young leaf of N. benthamiana and transient expression was assayed from three to 14 days after inoculation.
Each of the promoter-LUC fusions in pGreenII 0800-LUC were used in transient transformation by mixing 100 μl of Agrobacterium transformed with the reporter cassette and 900 μL of a second Agrobacterium strain transformed with a cassette that contained the TF gene fused to the 35S promoter in either a pART27-derived or pGreenII 62-SK binary vectors described below.
Agrobacterium tumefaciens, GV3101(MP90) [25 ] were cultured on Lennox agar (Invitrogen) supplemented with 50 μg.ml-1 kanamycin (Sigma) and incubated at 28°C. A 10 μl loop of confluent bacterium were re-suspended in 10 ml of infiltration media (10 mM MgCl2, 0.5 μM acetosyringone), to an OD600 of 0.2, and incubated at room temperature without shaking for 2 h before infiltration. Infiltrations were performed according to the methods of Voinnet et al. (2003) [5 (link)]. Approximately 300 μl of this Agrobacterium mixture was infiltrated into a young leaf of N. benthamiana and transient expression was assayed from three to 14 days after inoculation.
Each of the promoter-LUC fusions in pGreenII 0800-LUC were used in transient transformation by mixing 100 μl of Agrobacterium transformed with the reporter cassette and 900 μL of a second Agrobacterium strain transformed with a cassette that contained the TF gene fused to the 35S promoter in either a pART27-derived or pGreenII 62-SK binary vectors described below.
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A-Loop
acetosyringone
Agar
Agrobacterium
Agrobacterium tumefaciens
Bacteria
Cloning Vectors
Genes
Kanamycin
Light
Magnesium Chloride
Nicotiana
Plant Leaves
Plants
Strains
Transients
Vaccination
Ampicillin
Arabinose
Cell Culture Techniques
Cells
Chloramphenicol
Cloning Vectors
Electroporation
Escherichia coli
Genes
Genes, Reporter
Genome
Insertion Mutation
Inverse PCR
Kanamycin
Plasmids
Proteins
Recombination, Genetic
Replication Origin
Strains
Transcription Initiation Site
The Luria-Bertani (LB) media (10 g/L tryptone, 5 g/L yeast extract, 10 g/L NaCl) is obtained from Fisher Scientific (Pittsburgh, PA). The supplemented minimal media contains M9 minimal salts (6.8 g/L Na2PO4, 3 g/L KH2PO4, 0.5 g/L NaCl, 1 g/L NH4Cl) from Sigma, 2 mM MgSO4 (Fischer Scientific), 100 μM CaCl2 (Fischer Scientific), 0.4% glucose (Sigma), 0.05 g/L leucine (Acros Organics, Belgium), 5 μg/mL chloramphenicol (Acros Organics), and an adjusted pH of 7.4. The expression system is a ColE1 vector with chloramphenicol resistance (derived from pProTet, Clontech). The expression cassette contains a σ70 constitutive promoter (BioBrick J23100), the RBS sequence, followed by the mRFP1 fluorescent protein reporter. XbaI and SacI restriction sites are located before the RBS and after the start codon. An RBS with a desired sequence is inserted into the expression vector using standard cloning techniques. Pairs of complementary oligonucleotides are designed with XbaI and SacI overhangs and the vector is digested with XbaI and SacI restriction enzymes (NEB, Ipswich, MA). Ligation of the annealed oligonucleotides with cut vector results in a nicked plasmid, which is transformed into E. coli DH10B cells. Sequencing is used to verify a correct clone.
The AND gate genetic circuit is composed of three plasmids: pBACr-AraT7940, pBR939b, and pAC-SalSer914 with kanamycin, ampicillin, and chloramphenicol resistance markers, respectively. The PBAD promoter maximum expression level was modified by inserting designed synthetic RBSs on plasmid pBACr-AraT7940. Plasmid pBACr-AraT7940 was digested with BamHI and ApaLI enzymes and pairs of oligonucleotides were designed to contain the desired RBS sequence and corresponding overhangs. Ligation, transformation, selection, and sequencing proceeded as described above.
The AND gate genetic circuit is composed of three plasmids: pBACr-AraT7940, pBR939b, and pAC-SalSer914 with kanamycin, ampicillin, and chloramphenicol resistance markers, respectively. The PBAD promoter maximum expression level was modified by inserting designed synthetic RBSs on plasmid pBACr-AraT7940. Plasmid pBACr-AraT7940 was digested with BamHI and ApaLI enzymes and pairs of oligonucleotides were designed to contain the desired RBS sequence and corresponding overhangs. Ligation, transformation, selection, and sequencing proceeded as described above.
Ampicillin
Cells
Chloramphenicol
Chloramphenicol Resistance
Clone Cells
Cloning Vectors
Codon, Initiator
DNA Restriction Enzymes
Enzymes
Escherichia coli
Gene Circuits
Glucose
Kanamycin
Leucine
Ligation
Mrfp1 protein
Oligonucleotides
Plasmids
Saccharomyces cerevisiae
Salts
Sodium Chloride
Sulfate, Magnesium
General cloning techniques were used to generate each of the vectors. Detailed protocols are available upon request. All the lentiviral Destination vectors are derived from the p156RRL-sinPPT-CMV-GFP-PRE/Nhe I vector [82] (link), [83] (link) and all the retroviral Destination vectors are derived from the pQCXI series (Clontech). For the lentiviral vectors, a linker was inserted between the Kpn I and Eco RI sites to clone the drug selection cassettes following the Woodchuck post-transcriptional response element (WPRE). All Destination vectors were propagated in the E.coli strain DB3.1 (Invitrogen) under appropriate antibiotic selection (see plasmid maps for details). All Entry vectors were propagated in the E.coli strain TOP10F' (Invitrogen) under kanamycin selection. After the LR recombination reaction, lentiviral vectors were propagated in the E.coli strain Stbl3 (Invitrogen) and retroviral vectors in TOP10F', all under ampicillin selection, except for the pLenti CMV/TO Zeo DEST (zeocin).
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Ampicillin
Antibiotics
Clone Cells
Cloning Vectors
Deoxyribonuclease EcoRI
Escherichia coli
Kanamycin
Marmota
Microtubule-Associated Proteins
Pharmaceutical Preparations
Plasmids
Recombination, Genetic
Response Elements
Retroviridae
Strains
Transcription, Genetic
Zeocin
Most recents protocols related to «Kanamycin»
Example 6
TbpB and NMB0313 genes were amplified from the genome of Neisseria meningitidis serotype B strain B16B6. The LbpB gene was amplified from Neisseria meningitidis serotype B strain MC58. Full length TbpB was inserted into Multiple Cloning Site 2 of pETDuet using restriction free cloning ((F van den Ent, J. Löwe, Journal of Biochemical and Biophysical Methods (Jan. 1, 2006)).). NMB0313 was inserted into pET26, where the native signal peptide was replaced by that of pelB. Mutations and truncations were performed on these vectors using site directed mutagenesis and restriction free cloning, respectively. Pairs of vectors were transformed into E. coli C43 and were grown overnight in LB agar plates supplemented with kanamycin (50 μg/mL) and ampicillin (100 μg/mL).
tbpB genes were amplified from the genomes of M. catarrhalis strain 035E and H. influenzae strain 86-028NP and cloned into the pET52b plasmid by restriction free cloning as above. The corresponding SLAMs (M. catarrhalis SLAM 1, H. influenzae SLAM1) were inserted into pET26b also using restriction free cloning. A 6His-tag was inserted between the pelB and the mature SLAM sequences as above. Vectors were transformed into E. coli C43 as above.
Cells were harvested by centrifugation at 4000 g and were twice washed with 1 mL PBS to remove any remaining growth media. Cells were then incubated with either 0.05-0.1 mg/mL biotinylated human transferrin (Sigma-aldrich T3915-5 MG), α-TbpB (1:200 dilution from rabbit serum for M. catarrhalis and H. influenzae; 1:10000 dilution from rabbit serum for N. meningitidis), or α-LbpB (1:10000 dilution from rabbit serum-obtained a gift from J. Lemieux) or α-fHbp (1:5000 dilution from mouse, a gift from D. Granoff) for 1.5 hours at 4° C., followed by two washes with 1 mL of PBS. The cells were then incubated with R-Phycoerythrin-conjugated Streptavidin (0.5 mg/ml Cedarlane) or R-phycoerythrin conjugated Anti-rabbit IgG (Stock 0.5 mg/ml Rockland) at 25 ug/mL for 1.5 hours at 4° C. The cells were then washed with 1 mL PBS and resuspended in 200 uL fixing solution (PBS+2% formaldehyde) and left for 20 minutes. Finally, cells were washed with 2×1 mL PBS and transferred to 5 mL polystyrene FACS tubes. The PE fluorescence of each sample was measured for PE fluorescence using a Becton Dickinson FACSCalibur. The results were analyzed using FLOWJO software and were presented as mean fluorescence intensity (MFI) for each sample. For N. meningtidis experiments, all samples were compared to wildtype strains by normalizing wildtype fluorescent signals to 100%. Errors bars represent the standard error of the mean (SEM) across three experiments. Results were plotted statistically analysed using GraphPad Prism 5 software. The results shown in
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ADRB2 protein, human
Agar
Ampicillin
anti-IgG
Cells
Centrifugation
Cloning Vectors
Culture Media
Escherichia coli
Fluorescence
Formaldehyde
Genes
Genome
Haemophilus influenzae
Homo sapiens
Kanamycin
Lipoproteins
Membrane Proteins
Moraxella catarrhalis
Mus
Mutagenesis, Site-Directed
Mutation
Neisseria
Neisseria meningitidis
Phycoerythrin
Plasmids
Polypeptides
Polystyrenes
prisma
Rabbits
Serum
Signaling Lymphocytic Activation Molecule Family Member 1
Signal Peptides
Strains
Streptavidin
Technique, Dilution
Transferrin
Translocation, Chromosomal
Virulence Factors
Example 9
NEBT7EL-pA06238 was grown on LB with 50 μg/ml kanamycin. A 600 ml culture of TBkan50 was inoculated with NEBT7EL-pA06238 and incubated overnight at 37° C. at 200 rpm. The next morning, a 10 L fermentor was prepared with 9.5 L of TB and then inoculated with 500 ml of the overnight culture. The culture was grown at 37° C. The pH was maintained at 6.2 with NaOH and the dO2 was maintained ≥20%. After 2 hours of growth, the temperature was dropped to 25° C. The culture was grown for an additional 1 hour with the OD600 around 7. IPTG was added to a final concentration of 1 mM and CoCl2 was added to 25 μM. Additional CoCl2 was added 1 and 2 hours after induction to bring the final concentration to 300 μM. The cells were grown for 20 hours at which point the fermentor was chilled to 10° C. and the cells were harvested by centrifugation. The cell pellet was stored at −80° C. until use.
The cell pellet from the fermentation was lysed by stirring in buffer with lysozyme and DNAse. Cell debris was removed by centrifugation and the supernatant was filtered through a 0.45 micron filter. Filtered supernatant was incubated with Ni-NTA agarose resin and then enzyme was eluted with imidazole. Purified FC4E pA06238 was immobilized onto 5.25 grams of ECR8204F resin using the standard published protocol from Purolite.
The immobilized enzyme was loaded into a 11×300 mm glass fixed bed reactor and run for approximately 200 h at constant temperature (60° C.) with a constant feed composition of 30 wt % fructose+70 wt % aqueous buffer solution (20 mM KPO4, 50 mM NaCl, 300 uM CoCl2). Feed rate was held constant at 140 uL/min throughout the run. The fixed bed reaction reached a maximal conversion of approximately 30% tagatose and had a half-life of −50 hours (
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ARID1A protein, human
Buffers
Cells
Centrifugation
Deoxyribonucleases
Enzymes
Enzymes, Immobilized
Fermentation
Fermentors
Fructose
imidazole
Isopropyl Thiogalactoside
Kanamycin
Muramidase
Resins, Plant
Sepharose
Sodium Chloride
tagatose
Example 8
In selecting genomes for a given bacterial species where a SLAM homolog was identified, preference was given to reference genomes that contained fully sequenced genomes. SLAM homologs were identified using iterative Blast searches into closely related species to Neisseria to more distantly related species. For each of the SLAM homologs identified in these species, the corresponding genomic record (NCBI genome) was used to identify genes upstream and downstream along with their corresponding functional annotations (NCBI protein database, Ensembl bacteria). In a few cases, no genes were predicted upstream or downstream of the SLAM gene as they were too close to the beginning or end of the contig, respectively, and thus these sequences were ignored.
Neighbouring genes were analyzed for 1) an N-terminal lipobox motif (predicted using LipoP, SignalP), and 2) a solute binding protein, Tbp-like (InterPro signature: IPR or IPR011250), or pagP-beta barrel (InterPro signature: IPR011250) fold. If they contained these elements, we identified the adjacent genes as potential SLAM-dependent surface lipoproteins.
A putative SLAM (PM1515, SEQ ID NO: 1087) was identified in Pasteurella multocida using the Neisseria SLAM as a search. The putative SLAM (PM1515, SEQ ID NO: 1087) was adjacent to a newly predicted lipoprotein gene with unknown function (PM1514, SEQ ID NO: 1083) (
The putative SLAM (PM1515, SEQ ID NO: 1087) and its adjacent lipoprotein (PM1514, SEQ ID NO: 1083) were cloned into pET26b and pET52b, respectively, as previously described and transformed into E. coli C43 and grown overnight on LB agar supplemented with kanamycin (50 ug/ml) and ampicillin (100 ug/ml).
Cells were grown in auto-induction media for 18 hours at 37 C and then harvested, washed twice in PBS containing 1 mM MgCl2, and labeled with α-Flag (1:200, Sigma) for 1 hr at 4 C. The cells were then washed twice with PBS containing 1 mM MgCl2 and then labeled with R-PE conjugated α-mouse IgG (25 ug/mL, Thermo Fisher Scientific) for 1 hr at 4 C. following straining, cells were fixed in 2% formaldehyde for 20 minutes and further washed with PBS containing 1 mM MgCl2. Flow Cytometry was performed with a Becton Dickinson FACSCalibur and the results were analyzed using FLOWJO software. Mean fluorescence intensity (MFI) was calculated using at least three replicates was used to compare surface exposure the lipoprotein in strains either containing or lacking the putative SLAM (PM1515) and are shown in
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Agar
Ampicillin
Antibodies
Bacteria
Binding Proteins
Biological Assay
Cells
Escherichia coli
Flow Cytometry
Fluorescence
Formaldehyde
Genes
Genome
Kanamycin
Lipoprotein (a-)
Lipoproteins
Magnesium Chloride
Mus
Neisseria
Neisseria meningitidis
Pasteurella multocida
Proteins
Staphylococcal Protein A
Strains
Example 12
Plant transformation—The Arabidopsis thaliana var Columbia (To plants) were transformed according to the Floral Dip procedure [Clough S J, Bent A F. (1998) Floral dip: a simplified method for Agrobacterium-mediated transformation of Arabidopsis thaliana. Plant J. 16(6): 735-43; and Desfeux C, Clough S J, Bent A F. (2000) Female reproductive tissues were the primary targets of Agrobacterium-mediated transformation by the Arabidopsis floral-dip method. Plant Physiol. 123(3): 895-904] with minor modifications. Briefly, Arabidopsis thaliana Columbia (C010) T0 plants were sown in 250 ml pots filled with wet peat-based growth mix. The pots were covered with aluminum foil and a plastic dome, kept at 4° C. for 3-4 days, then uncovered and incubated in a growth chamber at 18-24° C. under 16/8 hours light/dark cycles. The T0 plants were ready for transformation six days before anthesis.
Single colonies of Agrobacterium carrying the binary vectors harboring the genes of some embodiments of the invention were cultured in YEBS medium (Yeast extract 1 gr/L, Beef extract 5 gr/L, MgSO4*7H2O, Bacto peptone 5 gr/L) supplemented with kanamycin (50 mg/L) and gentamycin (50 mg/L). The cultures were incubated at 28° C. for 48 hours under vigorous shaking to desired optical density at 600 nm of 0.85 to 1.1. Before transformation into plants, 60 μl of Silwet L-77 was added into 300 ml of the Agrobacterium suspension.
Transformation of T0 plants was performed by inverting each plant into an Agrobacterium suspension such that the above ground plant tissue was submerged for 1 minute. Each inoculated T0 plant was immediately placed in a plastic tray, then covered with clear plastic dome to maintain humidity and was kept in the dark at room temperature for 18 hours to facilitate infection and transformation. Transformed (transgenic) plants were then uncovered and transferred to a greenhouse for recovery and maturation. The transgenic T0 plants were grown in the greenhouse for 3-5 weeks until siliques were brown and dry, then seeds were harvested from plants and kept at room temperature until sowing.
For generating T1 and T2 transgenic plants harboring the genes of some embodiments of the invention, seeds collected from transgenic T0 plants were surface-sterilized by exposing to chlorine fumes (6% sodium hypochlorite with 1.3% HCl) for 100 minutes. The surface-sterilized seeds were sown on culture plates containing half-strength Murashig-Skoog (Duchefa); 2% sucrose; 0.5% plant agar; 50 mg/L kanamycin; and 200 mg/L carbenicylin (Duchefa). The culture plates were incubated at 4° C. for 48 hours and then were transferred to a growth room at 25° C. for three weeks. Following incubation, the T1 plants were removed from culture plates and planted in growth mix contained in 250 ml pots. The transgenic plants were allowed to grow in a greenhouse to maturity. Seeds harvested from T1 plants were cultured and grown to maturity as T2 plants under the same conditions as used for culturing and growing the T1 plants.
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Agar
Agrobacterium
Aluminum
Animals, Transgenic
Arabidopsis
Arabidopsis thalianas
Bacto-peptone
Beef
Chlorine
Cloning Vectors
Culture Media
Decompression Sickness
Females
Genes
Genes, Plant
Gentamicin
Humidity
Infection
Kanamycin
Marijuana Abuse
Plant Diseases
Plant Embryos
Plants
Plants, Transgenic
Reproduction
Saccharomyces cerevisiae
silwet L-77
Sodium Hypochlorite
Sucrose
Sulfate, Magnesium
Tissues
Example 1
Expression strain generation. The TdT mouse gene may be generated from the pET28 plasmid described in [Boulé et al., 1998, Mol. Biotechnol. 10, 199-208]. For example, the gene may be amplified by using the following primers:
Expression. The Ec-CTdT and Ec-DSi or Ec-DSi′ strains may be used for inoculating 250 mL erlens with 50 mL of LB media supplemented with appropriate amount of kanamycin. After overnight growth at 37° C., appropriate volumes of these pre-cultures are used to inoculate 5 L erlens with 2 L LB media with kanamycin. The initial OD for the 5 L cultures is chosen to be 0.01. The erlens are put at 37° C. under strong agitation and the OD of the different cultures are regularly checked. After reaching an OD comprised between 0.6 and 0.9 each erlen is supplemented by the addition of 1 mL of 1M IPTG (Isopropyl β-D-1-thiogalactopyranoside, Sigma). The erlens are put back to agitation under a controlled temperature of 37° C. After overnight expression, the cells are harvested in several pellets. Pellets expressing the same variants are pooled and stored at −20° C., eventually for several months.
Extraction. Previously prepared pellets are thawed in 30 to 37° C. water bath. Once fully thawed, pellets are resuspended in lysis buffer composed of 50 mM tris-HCL (Sigma) pH 7.5, 150 mM NaCl (Sigma), 0.5 mM mercaptoethanol (Sigma), 5% glycerol (Sigma), 20 mM imidazole (Sigma) and 1 tab for 100 mL of protease cocktail inhibitor (Thermofisher). Careful resuspension is carried out in order to avoid premature lysis and remaining of aggregates. Resuspended cells are lysed through several cycles of French press, until full color homogeneity is obtained. Usual pressure used is 14,000 psi. Lysate is then centrifuged for 1 h to 1h30 at 10,000 rpm. Centrifugate is pass through a 0.2 μm filter to remove any debris before column purification.
Purification. A one-step affinity procedure is used to purify the produced and extracted polymerase enzymes. A Ni-NTA affinity column (GE Healthcare) is used to bind the polymerases. Initially the column has been washed and equilibrated with 15 column volumes of 50 mM tris-HCL (Sigma) pH 7.5, 150 mM NaCl (Sigma) and 20 mM imidazole (Sigma). Polymerases are bound to the column after equilibration. Then a washing buffer, composed of 50 mM tris-HCL (Sigma) pH 7.5, 500 mM NaCl (Sigma) and 20 mM imidazole (Sigma), is applied to the column for 15 column volumes. After wash the polymerases are eluted with 50 mM tris-HCL (Sigma) pH 7.5, 500 mM NaCl (Sigma) and 0.5M imidazole (Sigma). Fractions corresponding to the highest concentration of polymerases of interest are collected and pooled in a single sample. The pooled fractions are dialyzed against the dialysis buffer (20 mM Tris-HCl, pH 6.8, 200 mM Na Cl, 50 mM MgOAc, 100 mM [NH4]2SO4). The dialysate is subsequently concentrated with the help of concentration filters (Amicon Ultra-30, Merk Millipore). Concentrated enzyme is distributed in small aliquots, 50% glycerol final is added, and those aliquots are then frozen at −20° C. and stored for long term. 5 μL of various fraction of the purified enzymes are analyzed in SDS-PAGE gels.
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2-Mercaptoethanol
Agar
Bath
Buffers
Cells
Clone Cells
Cloning Vectors
Dialysis
Dialysis Solutions
Enzymes
Escherichia coli
Freezing
Gels
Genes
Glycerin
imidazole
Isopropyl Thiogalactoside
Kanamycin
Mus
Mutagenesis, Site-Directed
Oligonucleotide Primers
Pellets, Drug
Plasmids
Point Mutation
Premature Birth
Pressure
SDS-PAGE
SERPINA1 protein, human
Sodium Chloride
Tromethamine
Vertebral Column
Top products related to «Kanamycin»
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Kanamycin is a broad-spectrum antibiotic derived from the bacterium Streptomyces kanamyceticus. It is commonly used as a selective agent in molecular biology and microbiology laboratories for the growth and selection of bacteria that have been genetically modified to express a gene of interest.
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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.
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Kanamycin is an antibiotic used in molecular biology and microbiology laboratories. It is a broad-spectrum aminoglycoside antibiotic that inhibits bacterial protein synthesis by binding to the 30S subunit of the bacterial ribosome. Kanamycin is commonly used as a selective agent for the growth of bacteria that have been engineered to express a kanamycin resistance gene.
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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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Fetal Bovine Serum (FBS) is a cell culture supplement derived from the blood of bovine fetuses. FBS provides a source of proteins, growth factors, and other components that support the growth and maintenance of various cell types in in vitro cell culture applications.
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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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Streptomycin is a laboratory product manufactured by Merck Group. It is an antibiotic used in research applications.
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T4 DNA ligase is an enzyme that catalyzes the formation of phosphodiester bonds between adjacent 3'-hydroxyl and 5'-phosphate termini in DNA. It is commonly used in molecular biology for the joining of DNA fragments.
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Erythromycin is a macrolide antibiotic produced by the bacterium Saccharopolyspora erythraea. It functions as a protein synthesis inhibitor by binding to the 50S subunit of the bacterial ribosome, preventing the translocation of the peptidyl-tRNA from the A-site to the P-site during translation.
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The QIAprep Spin Miniprep Kit is a laboratory product designed for the rapid and efficient purification of plasmid DNA from bacterial cultures. It is a versatile tool used in various molecular biology applications.
More about "Kanamycin"
Kanamycin, an aminoglycoside antibiotic derived from the bacterium Streptomyces kanamyceticus, has become an indispensable tool in molecular biology and genetics research.
This versatile compound, also known as Kan, plays a crucial role in the selection and identification of cells that have been successfully transfected or transformed with recombinant DNA.
Kanamycin works by inhibiting protein synthesis in bacterial cells, making it an effective selection marker.
Researchers can utilize kanamycin-resistance genes as selectable markers when engineering plasmids or other vectors, allowing them to identify and isolate cells that have incorporated the desired genetic material.
This process is often used in conjunction with other antibiotics, such as Ampicillin, Chloramphenicol, Tetracycline, Streptomycin, and Erythromycin, each with their own unique properties and applications.
Optimizing kanamycin protocols is crucial for streamlining genetic engineering workflows and ensuring the success of experimental procedures.
By leveraging AI-driven platforms like PubCompare.ai, researchers can easily locate the best kanamycin protocols from literature, pre-prints, and patents, unlocking new insights and optimizing their research processes.
The use of kanamycin is not limited to genetic engineering; it is also used clinically to treat certain bacterial infections, though its usage is more limited due to potential toxicity and the rise of antibiotic resistance.
In addition to its role in molecular biology, kanamycin is commonly used in combination with FBS (Fetal Bovine Serum) and T4 DNA ligase, further enhancing its versatility in various experimental settings.
By understanding the nuances of kanamycin and its interactions with other commonly used reagents, researchers can create more effective and streamlined protocols, ultimately driving advancements in their fields of study.
This versatile compound, also known as Kan, plays a crucial role in the selection and identification of cells that have been successfully transfected or transformed with recombinant DNA.
Kanamycin works by inhibiting protein synthesis in bacterial cells, making it an effective selection marker.
Researchers can utilize kanamycin-resistance genes as selectable markers when engineering plasmids or other vectors, allowing them to identify and isolate cells that have incorporated the desired genetic material.
This process is often used in conjunction with other antibiotics, such as Ampicillin, Chloramphenicol, Tetracycline, Streptomycin, and Erythromycin, each with their own unique properties and applications.
Optimizing kanamycin protocols is crucial for streamlining genetic engineering workflows and ensuring the success of experimental procedures.
By leveraging AI-driven platforms like PubCompare.ai, researchers can easily locate the best kanamycin protocols from literature, pre-prints, and patents, unlocking new insights and optimizing their research processes.
The use of kanamycin is not limited to genetic engineering; it is also used clinically to treat certain bacterial infections, though its usage is more limited due to potential toxicity and the rise of antibiotic resistance.
In addition to its role in molecular biology, kanamycin is commonly used in combination with FBS (Fetal Bovine Serum) and T4 DNA ligase, further enhancing its versatility in various experimental settings.
By understanding the nuances of kanamycin and its interactions with other commonly used reagents, researchers can create more effective and streamlined protocols, ultimately driving advancements in their fields of study.