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Lyticase

Lyticase is an enzyme used to degrade bacterial cell walls.
It is commonly employed in molecular biology research, particularly for the extraction and purification of DNA and RNA from bacterial samples.
Lyticase acts by hydrolyzing the peptidoglycan layer, allowing for the release of cellular contents.
Researchers can utilize Lyticase to optimize their protocols, enhancing accuracy and reproducibility of their experiments.
This powerful enzyme is a valuable tool for genetic analysis and biotechnology applications.

Most cited protocols related to «Lyticase»

Detecting Apoptosis and Oxidative Stress in Yeast

Cited 42 times

Electron microscopy, annexin V labeling, and DAPI staining were performed as described previously (Madeo et al., 1997 (link)). For the TdT-mediated dUTP nick end labeling (TUNEL) test, cells were prepared as described (Madeo et al., 1997 (link)), and the DNA ends were labeled using the In Situ Cell Death Detection Kit, POD (Boehringer Mannheim). Yeast cells were fixed with 3.7% formaldehyde, digested with lyticase, and applied to a polylysine-coated slide as described for immunofluorescence (Adams and Pringle, 1984 (link)). The slides were rinsed with PBS and incubated with 0.3% H₂O₂ in methanol for 30 min at room temperature to block endogenous peroxidases. The slides were rinsed with PBS, incubated in permeabilization solution (0.1% Triton X-100 and 0.1% sodium citrate) for 2 min on ice, rinsed twice with PBS, incubated with 10 μl TUNEL reaction mixture (terminal deoxynucleotidyl transferase 200 U/ml, FITC-labeled dUTP 10 mM, 25 mM Tris-HCl, 200 mM sodium cacodylate, 5 mM cobalt chloride; Boehringer Mannheim) for 60 min at 37°C, and then rinsed 3× with PBS. For the detection of peroxidase, cells were incubated with 10 μl Converter-POD (anti-FITC antibody, Fab fragment from sheep, conjugated with horseradish peroxidase) for 30 min at 37°C, rinsed 3× with PBS, and then stained with DAB-substrate solution (Boehringer Mannheim) for 10 min at room temperature. A coverslip was mounted with a drop of Kaiser's glycerol gelatin (Merck). As staining intensity varies, only samples from the same slide were compared.
Free intracellular radicals were detected with dihydrorhodamine 123, dichlorodihydrofluorescein diacetate (dichlorofluorescin diacetate), or dihydroethidium (hydroethidine; Sigma Chemical Co.). Dihydrorhodamine 123 was added ad-5 μg per ml of cell culture from a 2.5-mg/ml stock solution in ethanol and cells were viewed without further processing through a rhodamine optical filter after a 2-h incubation. Dichlorodihydrofluorescein diacetate was added ad-10 μg per ml of cell culture from a 2.5 mg/ml stock solution in ethanol and cells were viewed through a fluorescein optical filter after a 2-h incubation. Dihydroethidium was added ad-5 μg per ml of cell culture from a 5 mg/ml aqueous stock solution and cells were viewed through a rhodamine optical filter after a 10-min incubation. For flow cytometric analysis, cells were incubated with dihydrorhodamine 123 for 2 h and analyzed using a FACS^® Calibur (Becton Dickinson) at low flow rate with excitation and emission settings of 488 and 525–550 nm (filter FL1), respectively.
Free spin trap reagents N-tert-butyl-α−phenylnitrone (PBN; Sigma-Aldrich) and 3,3,5,5,-tetramethyl-pyrroline N-oxide (TMPO; Sigma-Aldrich) were added directly to the cell cultures as 10-mg/ml aqueous stock solutions. Viability was determined as the portion of cell growing to visible colonies within 3 d.
To determine frequencies of morphological phenotypes (TUNEL, Annexin V, DAPI, dihydrorhodamine 123), at least 300 cells of three independent experiments were evaluated.

Madeo F., Fröhlich E., Ligr M., Grey M., Sigrist S.J., Wolf D.H, & Fröhlich K.U. (1999). Oxygen Stress: A Regulator of Apoptosis in Yeast. The Journal of Cell Biology, 145(4), 757-767.

Publication 1999

3,3,5,5-tetramethyl-1-pyrroline N-oxide Annexin A5 Antibodies, Anti-Idiotypic Cacodylate Cardiac Arrest Cell Culture Techniques Cell Death Cells cobaltous chloride DAPI deoxyuridine triphosphate dichlorofluorescin dihydroethidium dihydrorhodamine 123 DNA Nucleotidylexotransferase Domestic Sheep Electron Microscopy Ethanol Flow Cytometry Fluorescein Fluorescein-5-isothiocyanate Formaldehyde Free Radicals Gelatins Glycerin Horseradish Peroxidase hydroethidine Immunofluorescence Immunoglobulins, Fab In Situ Nick-End Labeling lyticase Methanol Oxides Peroxidase Peroxidases Peroxide, Hydrogen Phenotype Polylysine Protoplasm pyrroline Rhodamine Sodium Sodium Citrate TERT protein, human Triton X-100 Tromethamine Yeast, Dried

Detecting Apoptosis in Yeast Cells

Cited 28 times

Exposed phosphatidylserine was detected by reaction with FITC-coupled annexin V (ApoAlert Annexin V Apoptosis Kit; CLONETECH Laboratories, Inc., Palo Alto, CA). Yeast cells were washed in sorbitol buffer (1.2 M sorbitol, 0.5 mM MgCl₂, 35 mM potassium phosphate, pH 6.8), digested with 5.5% glusulase (Boehringer Mannheim) and 15 U/ml lyticase (Sigma Chemical Co.) in sorbitol buffer for 2 h at 28°C, harvested, washed in binding buffer (10 mM Hepes/NaOH, pH 7.4, 140 mM NaCl, 2.5 mM CaCl₂; CLONETECH Laboratories, Inc.) containing 1.2 M sorbitol buffer, harvested and resuspended in binding buffer/sorbitol. 2 μl annexin-FITC (CLONETECH Laboratories, Inc.) and 2 μl propidium iodide (500 μg/ml) were added to 38 μl cell suspension, and then incubated for 20 min at room temperature. The cells were harvested, suspended in binding buffer/sorbitol, and applied to a microscopic slide.

Madeo F., Fröhlich E, & Fröhlich K.U. (1997). A Yeast Mutant Showing Diagnostic Markers of Early and Late Apoptosis. The Journal of Cell Biology, 139(3), 729-734.

Publication 1997

Annexin A5 Annexins Apoptosis Buffers Cells Fluorescein-5-isothiocyanate glusulase HEPES lyticase Magnesium Chloride Microscopy Phosphatidylserines potassium phosphate Propidium Iodide Sodium Chloride Sorbitol Yeast, Dried

TUNEL Assay for Detecting DNA Strand Breaks

Cited 23 times

DNA strand breaks were demonstrated by labeling free 3′-OH termini with FITC-labeled deoxyuridine, which was detected with alkaline phosphatase–coupled, anti-fluorescein antibody, and the formation of a dye precipitate with a phosphatase substrate (In Situ Cell Death Detection Kit, AP; Boehringer Mannheim, Mannheim, Germany). Yeast cells were fixed with 3.7% formaldehyde, digested with lyticase, and applied to a polylysine-coated slide as described for immunofluorescence (Adams and Pringle, 1984 (link)). The slides were rinsed with PBS, incubated in permeabilization solution (0.1% Triton X-100, 0.1% sodium citrate) for 2 min on ice, rinsed twice with PBS, incubated with 10 μl TUNEL reaction mixture (200 U/ml terminal deoxynucleotidyl transferase, 10 mM FITC-labeled dUTP, 25 mM Tris/HCl, 200 mM sodium cacodylate, 5 mM cobalt chloride; Boehringer Mannheim) for 60 min at 37°C, rinsed three times with PBS, incubated with 50 μl Converter AP solution (alkaline phosphatase– labeled, anti-FITC antibody; Boehringer Mannheim) for 30 min at 37°C, rinsed three times with PBS, and stained by incubation with 50 μl naphthol) AS-MX phosphate (Sigma Chemical Co., Munich, Germany), 0.8 mg/ml, fast red TR salt (Sigma Chemical Co.), 1 mg/ml, 2% dimethylformamide, 1 mM levamisole in 100 mM Tris/HCl, pH 8.2, for 30 min at room temperature. A coverslip was mounted with a drop of Kaiser's glycerol gelatin (Merck, Darmstadt, Germany).

Madeo F., Fröhlich E, & Fröhlich K.U. (1997). A Yeast Mutant Showing Diagnostic Markers of Early and Late Apoptosis. The Journal of Cell Biology, 139(3), 729-734.

Publication 1997

Alkaline Phosphatase Antibodies, Anti-Idiotypic Cacodylate Cell Death Cells cobaltous chloride Deoxyuridine deoxyuridine triphosphate Dimethylformamide DNA Breaks DNA Nucleotidylexotransferase fast red TR salt Fluorescein Fluorescein-5-isothiocyanate Fluorescent Antibody Technique Formaldehyde Gelatins Glycerin In Situ Nick-End Labeling Levamisole Hydrochloride lyticase Naphthols Phosphates Phosphoric Monoester Hydrolases Polylysine Sodium Sodium Citrate Triton X-100 Tromethamine Yeast, Dried

Genomic DNA Extraction and Sequencing

Cited 17 times

To extract genomic DNA, ∼10⁹ cells grown overnight in YPD at 30°C were processed using the Qiagen Genomic Buffer Set and the Qiagen Genomic-tip 100/G. Lyticase (Sigma, L2524) was used to enzymatically digest the fungal cell wall. Two libraries were constructed with average insert sizes of 197 bases and 2.5 kilobases (Supplemental Table S2) as previously described (Fisher et al. 2011 (link); Grad et al. 2012 (link)) and were sequenced on an Illumina HiSeq to generate 101 base paired-end reads.
For SNP calling, reads were aligned to the SC5314 genome (version A21-s02-m01-r01; http://www.candidagenome.org) using BWA 0.5.9 (Li and Durbin 2010 (link)) and variants identified with GATK (McKenna et al. 2010 (link)). Genomic regions exhibiting copy number variation were identified from GC normalized read depth. Potential inversions and translocations identified from alignments of the de novo assemblies were validated by evaluating read support using BreakDancer (Chen et al. 2009 (link)).
The Illumina reads for each strain were assembled using ALLPATHS-LG (Gnerre et al. 2011 (link)), and genes were predicted for each assembly. Both the assemblies and SNPs were used to evaluate variation in gene content and sequence. For detailed DNA sequence analysis methods, see Supplemental Material.

Hirakawa M.P., Martinez D.A., Sakthikumar S., Anderson M.Z., Berlin A., Gujja S., Zeng Q., Zisson E., Wang J.M., Greenberg J.M., Berman J., Bennett R.J, & Cuomo C.A. (2015). Genetic and phenotypic intra-species variation in Candida albicans. Genome Research, 25(3), 413-425.

Publication 2015

Buffers Cells Cell Wall Copy Number Polymorphism Genes Genetic Diversity Genome Inversion, Chromosome lyticase Sequence Analysis, DNA Single Nucleotide Polymorphism Strains Translocation, Chromosomal

Quantifying 5-FU Incorporation in DNA and RNA

Cited 16 times

Yeast were grown to logarithmic phase, diluted to 5 × 10⁶ cells/ml into media +/− 150 µM 5-FU, and incubated for varying times (wt, 6 h, ung1, 6 h, apn1, 3 h) at 30°C with agitation in order to kill 70–90% of the wt and apn1 cells and achieve maximum cell killing with the ung1 yeast at this 5-FU concentration. Small aliquots were diluted and plated, and the remaining cells were spun down, lysed with lyticase (Sigma) and genomic DNA was isolated using Genomic-tips (Qiagen). Each sample (3 µg) was digested overnight at room temperature with 3 nM Escherichia coli uracil DNA glycosylase (Ung) and 3 nM human AP endonuclease (Ape1) in buffer containing 50 mM Tris–HCl, pH 7.5, 1 mM EDTA, 50 mM NaCl and 10 mM MgCl₂. Half of each reaction was run on a 0.8% agarose gel, which was stained with 1 µg/ml EtBr prior to imaging.
For GC-MS, yeast cells were grown to logarithmic phase and diluted to 5 × 10⁶ cells/ml into 5-FU to achieve 70–90% cell killing across all samples (wt, 150 µM 5-FU for 6 h, ung1, 3 mM 5-FU for 4 h, and apn1, 150 µM 5-FU for 3 h). Aliquots were diluted and plated, and the genomic DNA was purified and digested with 10 nM Ung overnight at room temperature in buffer containing 10 mM Tris–HCl, pH 7.5, 2.5 mM MgCl₂ and 25 mM NaCl. Following digestion, aliquots of uracil-¹³C₄, ¹⁵N₂ and 5-FU-¹³C₄, ¹⁵N₂ were added as internal standards (stable isotope labeled U and 5-FU were purchased from Cambridge Isotope Laboratories). Then the DNA was precipitated with 70% EtOH, centrifuged and the supernatant and pellet fractions were separated. Ethanol was removed from supernatant fractions under vacuum in a SpeedVac at room temperature. Aqueous supernatant fractions were frozen in liquid nitrogen, lyophilized to dryness for 18 h, and then trimethylsilylated and analyzed by GC-MS as described (32 (link)–34 (link)). For identification and quantification, selected-ion monitoring was used to monitor the characteristic ions of the trimethylsilyl derivatives of uracil (m/z 256 and m/z 241), uracil-¹⁴C₄,¹⁵N₂ (m/z 262 and m/z 247), 5-FU (m/z 274 and m/z 259) and 5-FU-¹³C₄,¹⁵N₂ (m/z 280 and m/z 265) during GC/MS analysis. (In each case, the first ion is the molecular ion and the second one is the ion that results from the loss of methyl radical from the molecular ion.)
For RNA 5-FU incorporation analysis, wt yeast were grown to logarithmic phase, diluted to 5 × 10⁶ cells/ml into YEPD +/− one EC₅₀ of 5-FU, and shaken at 30°C for 6 h. Cellular RNA was then isolated using the RNeasy Kit (Qiagen). RNA (10 µg) was digested to nucleosides using mung bean nuclease (10 U) and calf intestinal phosphatase (10 U) overnight at 37°C in buffer containing 10 mM Tris–HCl, pH 7.9, 10 mM MgCl₂, 50 mM NaCl and 1 mM DTT (all reagents from New England Biolabs). High-performance liquid chromatography (HPLC) was carried out using an analytical Aqua reversed-phase C18 column (Phenomenex) and isocratic elution with 3% acetonitrile in aqueous 0.1 M TEAA, pH 7.0, at a flow rate of 1 ml/min.

Seiple L., Jaruga P., Dizdaroglu M, & Stivers J.T. (2006). Linking uracil base excision repair and 5-fluorouracil toxicity in yeast. Nucleic Acids Research, 34(1), 140-151.

Publication 2006

Most recents protocols related to «Lyticase»

Recombinant Lyticase Expression and Purification

A plasmid for the expression of recombinant lyticase was kindly provided by Craig Peterson (pCP330). Expression and purification of recombinant lyticase was performed as described in (14 (link)).

Tod N.P., Vogelauer M., Cheng C., Karimian A., Schmollinger S., Camacho D, & Kurdistani S.K. (2024). The role of histone H3 leucine 126 in fine-tuning the copper reductase activity of nucleosomes. The Journal of Biological Chemistry, 300(6), 107314.

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Publication 2024

Pulsed-Field Gel Electrophoresis for Yeast Genomic DNA

DNA plugs for PFGE were prepared according to the manufacturer’s instructions (Bio-Rad) and Ishii et al., 2008 (link). Fresh yeast cells were inoculated in 50 ml YPD and incubated at 30°C until the OD₆₀₀ reached approximately 1.0. The cells were subsequently harvested, washed twice with cold EDTA buffer (50 mM, pH 8.0), and resuspended in 300 μl of CSB buffer (10 mM pH 7.2 Tris–Cl, 20 mM NaCl, 100 mM pH 8.0 EDTA, 4 mg/ml lyticase) and blended with 300 μl of 2% low-melt agarose (Bio-Rad). Then, 100 μl of resuspended cells were added to each plug and incubated at 4°C for 30 min until the agarose plugs were solidified. The solidified agarose plugs were incubated in lyticase buffer (10 mM pH 7.2 Tris–Cl, 100 mM pH 8.0 EDTA, 1 mg/ml lyticase) at 37°C for 3 hr, followed by incubation in Proteinase K Reaction Buffer (100 mM pH 8.0 EDTA, 0.2% sodium deoxycholate, 1% sodium lauryl sarcosine) containing 1 mg/ml Proteinase K at 50°C for 12 hr. The plugs were washed four times in 25 ml of wash buffer (20 mM Tris, pH 8.0, 50 mM EDTA) for 1 hr each time at room temperature with gentle agitation. The plugs were then fixed into a pulsed field agarose gel (Bio-Rad), and the CHEF-DR II Pulsed Field Electrophoresis System (Bio-Rad) was used for gel electrophoresis. The electrophoresis conditions for separation were as follows: 0.8% agarose gel, 1× TBE buffer, 14°C temperature, first run: initial switch time 1200 s; final switch time 1200 s; run time 24 hr; voltage gradient 2 V/cm; angle 96°; second run: initial switch time 1500 s; final switch time 1500 s; run time 24 hr; voltage gradient 2 V/cm; angle 100°; third run: initial switch time 1800 s; final switch time 1800 s; run time 24 hr; voltage gradient 2 V/cm; angle 106°. The gel was stained with GelstainRed nucleic acid dye (US Everbright), and PFGE Gels were imaged by Tanon 2500.

Hu C., Zhu X.T., He M.H., Shao Y., Qin Z., Wu Z.J, & Zhou J.Q. (2024). Elimination of subtelomeric repeat sequences exerts little effect on telomere essential functions in Saccharomyces cerevisiae. eLife, 12, RP91223.

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Publication 2024

Optimized Yeast Genomic DNA Extraction

Not available on PMC !

Genomic DNA was isolated according to the method published by Denis et al. 31 (link) with following modifications: yeast culture was grown until cells reached OD=5-10, zymolyase was replaced with lyticase (Sigma Aldrich, 600 U per 1 mL of OD=1) and all centrifugation steps were performed at 4000 g (Supplementary Method 1). The adapted protocol was also tested in minimized scale, making use of 2 mL of yeast culture and proportionally reduced reagents.

Ciurkot K., Lu X., Malyshava A., Soro L., Lees A., Gorochowski T.E., & Ellis T. (2024). Combinatorial Design Testing in Genomes with POLAR-seq.

Publication 2024

Optimized Preparation of Microalgae Chromosomal DNA

Genomic DNA agarose plugs were generated based on the protocol of Hage and Houseley [71 (link)]. Briefly, P. SENEW3 cells were cultured in f/2 medium to mid exponential growth phase cell density of 2×10⁷ cells ml⁻¹. Ten ml cell-culture aliquots were centrifuged at 3200 g for 15 mins, cell pellets were washed in 1 ml of wash buffer (10 mM Tris pH 7.6, 50 mM ethylenediaminetetraacetic acid [EDTA]) and resuspended in 50 µl of wash buffer with 1 mg ml⁻¹ lyticase. Cells were heated to 55 °C for 5 mins and mixed with 55 µl of melted 1.6 % SeaKem LE agarose in dH₂O at 55 °C and set in PFGE combe wells at 4 °C for 1 h. Solid plugs were transferred to 1.5 ml microcentrifuge tubes, digested in 500 µl wash buffer with 1 mg ml⁻¹ lyticase for 3 h at 37 °C and then in 500 µl PK buffer (100 mM EDTA, 0.2 % sodium deoxycholate, 1 % sodium lauryl sarcosine) with 1 mg ml⁻¹ proteinase K (Sigma-Aldrich P6556) overnight at 55 °C. Digested cell plugs were washed three times in 1 ml wash buffer for 30 mins at room temperature, resuspended in 500 µl wash buffer and stored at 4 °C.
P. SENEW3 chromosomal DNA was separated using a Bio-Rad CHEF Mapper XA PFGE system. Four agarose plugs and a NEB Yeast Chromosome PFGE marker (N0345S) plug were inserted into a 1 % SeaPlaque Low Melting Point Agarose (Lonza: 50101–25 g) gel, prepared with 0.5 X Tris/Borate/EDTA (TBE) buffer. Each plug was run in parallel for 24, 28, 32 and 36 h, respectively (Table S1, available in the online version of this article). Following each time point, each lane was excised and visualized with a blue light gel box.

da Roza P.A., Muller H., Sullivan G.J., Walker R.S., Goold H.D., Willows R.D., Palenik B, & Paulsen I.T. (2024). Chromosome-scale assembly of the streamlined picoeukaryote Picochlorum sp. SENEW3 genome reveals Rabl-like chromatin structure and potential for C4 photosynthesis. Microbial Genomics, 10(4), 001223.

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Publication 2024

Isolation of Yeast Organelles

For preparation of crude organelles, 3 to 6 liter cultures were grown in synthetic medium containing appropriate amino acids for selection to logarithmic phase (OD₆₀₀ = 0.8–1) at 30°C. Cells were harvested and suspended in 25 ml 100 mM Tris/HCl buffer (pH 9.4) per liter of starting culture containing 10 mM DTT. The suspension was incubated for 10 min at room temperature and centrifuged at 600 × g for 5 min. Cell pellets were suspended in 25 ml lyticase buffer (0.7 M sorbitol, 0.75xYP, 0.5% glucose, 10 mM Hepes/OH, 1 mM DTT (pH 7.4)) per liter of starting culture and lyticase (10⁵ units per liter starting culture) was added. Suspensions were incubated for 30 to 45 min at 30°C and the efficiency of spheroplast formation was determined by measuring the decline of OD₆₀₀ after suspension of samples in H₂O. Spheroplasts were washed 3 times with 25 ml 2xJR buffer (0.4 M sorbitol, 100 mM KOAc, 40 mM Hepes/OH (pH 7.4), 4 mM EDTA, 2 mM DTT) per liter starting culture, suspended in 5 ml 2xJR (containing a protease inhibitor cocktail: 1 mM 4-aminobenzamidinedihydrochloride, 1 μg/ml aprotinin, 1 μg/ml leupeptin, 1 mM phenylmethylsulfonyl fluoride, 10 μg/ml N-tosyl-L-phenylalanine chloromethyl ketone, and 1 μg/ml pepstatin) per liter starting culture and frozen at −80°C. Cells were thawed in iced water and disrupted by 20 strokes with a Potter-Elvehjem homogenizer. Nuclei were removed from homogenates by centrifugation 2 times at 600 × g. For differential centrifugation, 1 mg post-nuclear supernatant (PNS) fraction was used. PNS (100 μl) fractions were centrifuged at 13k × g for 5 min. The resulting supernatant was centrifuged at 100k × g for 20 min. All fractions were analyzed by SDS-PAGE and immunoblot in amounts representing the initial volume.

Bittner E., Stehlik T., Lam J., Dimitrov L., Heimerl T., Schöck I., Harberding J., Dornes A., Heymons N., Bange G., Schuldiner M., Zalckvar E., Bölker M., Schekman R, & Freitag J. (2024). Proteins that carry dual targeting signals can act as tethers between peroxisomes and partner organelles. PLOS Biology, 22(2), e3002508.

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Publication 2024

Top products related to «Lyticase»

Lyticase by Merck Group

Sourced in United States, Germany, China, France

Lyticase is a laboratory enzyme used for the digestion of bacterial cell walls. It is derived from the fungus Arthrobacter luteus and is commonly used in molecular biology and microbiology experiments to facilitate the extraction of cellular contents, including DNA and RNA.

Sorbitol by Merck Group

Sourced in United States, Germany, United Kingdom, China, Denmark, France, Italy, New Zealand

Sorbitol is a sugar alcohol that is commonly used in various laboratory applications. It serves as a humectant, sweetener, and cryoprotectant in various formulations and processes. Sorbitol is a crystalline powder with a mild, sweet taste.

Miseq platform by Illumina

Sourced in United States, China, Germany, United Kingdom, Spain, Australia, Italy, Canada, Switzerland, France, Cameroon, India, Japan, Belgium, Ireland, Israel, Norway, Finland, Netherlands, Sweden, Singapore, Portugal, Poland, Czechia, Hong Kong, Brazil

The MiSeq platform is a benchtop sequencing system designed for targeted, amplicon-based sequencing applications. The system uses Illumina's proprietary sequencing-by-synthesis technology to generate sequencing data. The MiSeq platform is capable of generating up to 15 gigabases of sequencing data per run.

Qiaamp dna mini kit by Qiagen

Sourced in Germany, United States, France, United Kingdom, Netherlands, Spain, Japan, China, Italy, Canada, Switzerland, Australia, Sweden, India, Belgium, Brazil, Denmark

The QIAamp DNA Mini Kit is a laboratory equipment product designed for the purification of genomic DNA from a variety of sample types. It utilizes a silica-membrane-based technology to efficiently capture and purify DNA, which can then be used for various downstream applications.

β mercaptoethanol by Merck Group

Sourced in United States, Germany, United Kingdom, China, France, Canada, Sao Tome and Principe, Spain, Macao, Italy, Belgium, Japan, Switzerland, Austria, Australia, Poland, Netherlands, Israel, India, Brazil, Denmark

β-mercaptoethanol is a reducing agent commonly used in biochemical applications. It is a clear, colorless liquid with a characteristic odor. β-mercaptoethanol is used to break disulfide bonds in proteins and peptides, and to maintain a reducing environment in biological samples.

Lysozyme by Merck Group

Sourced in United States, Germany, United Kingdom, Japan, China, Poland, Ireland, Switzerland, Italy, Sao Tome and Principe, India, Canada, France, Belgium, Australia, Netherlands, Singapore, Denmark, Macao, Portugal

Lysozyme is an enzyme that catalyzes the hydrolysis of 1,4-beta-linkages between N-acetylmuramic acid and N-acetyl-D-glucosamine residues in peptidoglycan, which is a major component of the cell walls of gram-positive bacteria. This function makes lysozyme an effective antimicrobial agent.

Hiseq 2500 by Illumina

Sourced in United States, China, Germany, United Kingdom, Canada, Switzerland, Sweden, Japan, Australia, France, India, Hong Kong, Spain, Cameroon, Austria, Denmark, Italy, Singapore, Brazil, Finland, Norway, Netherlands, Belgium, Israel

The HiSeq 2500 is a high-throughput DNA sequencing system designed for a wide range of applications, including whole-genome sequencing, targeted sequencing, and transcriptome analysis. The system utilizes Illumina's proprietary sequencing-by-synthesis technology to generate high-quality sequencing data with speed and accuracy.

Qiaamp dna stool mini kit by Qiagen

Sourced in Germany, United States, United Kingdom, Spain, France, Netherlands, China, Canada, Japan, Italy, Australia, Switzerland

The QIAamp DNA Stool Mini Kit is a laboratory equipment product designed for the purification of genomic DNA from stool samples. It is a tool for extracting and isolating DNA from biological specimens.

Dneasy blood and tissue kit by Qiagen

Sourced in Germany, United States, United Kingdom, Spain, Canada, Netherlands, Japan, China, France, Australia, Denmark, Switzerland, Italy, Sweden, Belgium, Austria, Hungary

The DNeasy Blood and Tissue Kit is a DNA extraction and purification product designed for the isolation of genomic DNA from a variety of sample types, including blood, tissues, and cultured cells. The kit utilizes a silica-based membrane technology to efficiently capture and purify DNA, providing high-quality samples suitable for use in various downstream applications.

Lyticase from arthrobacter luteus by Merck Group

Sourced in Germany, United States

Lyticase is an enzyme derived from the bacterium Arthrobacter luteus. It functions as a lytic enzyme, capable of breaking down the cell walls of certain microorganisms.

What is Lyticase and how is it used in molecular biology research?

Lyticase is an enzyme that degrades the bacterial cell wall by hydrolyzing the peptidoglycan layer. It is commonly used in molecular biology research to extract and purify DNA and RNA from bacterial samples. Lyticase allows researchers to release the cellular contents, optimizing their protocols and enhancing the accuracy and reproducibility of their experiments. It is a valuable tool for genetic analysis and biotechnology applications.

What are some common challenges in using Lyticase effectively?

One of the key challenges in using Lyticase is identifying the most effective protocol for your specific research needs. Different protocols and variations of Lyticase can yield varying results in terms of DNA/RNA yield, purity, and downstream applications. Researchers need to carefully evaluate and compare multiple Lyticase protocols to determine the optimal approach for their experiments.

How can PubCompare.ai help researchers optimize their Lyticase protocols?

PubCompare.ai is a powerful AI-driven tool that can assist researchers in optimizing their Lyticase protocols. The platform allows you to efficiently screen protocol literature, including peer-reviewed papers, preprints, and patents, to identify the most effective Lyticase methods. PubCompare.ai's AI analysis can highlight key differences in protocol effectiveness, enabling you to choose the best option for reproducibility and accuracy in your research. This can help you save time, enhance your experimental outcomes, and ensure the reliability of your Lyticase-based experiments.

Are there different types or variations of Lyticase available?

Yes, there are several variations of Lyticase available, each with slightly different properties and applications. For example, some Lyticase preparations may be more effective at degrading specific bacterial cell wall types, while others may be optimized for particular downstream processes like DNA/RNA extraction. Researchers should carefully evaluate the different Lyticase options to determine the best fit for their specific research needs and sample types.

How can Lyticase be used in different biotechnology and genetic analysis applications?

Lyticase has a wide range of applications in biotechnology and genetic analysis. Beyond its use in DNA/RNA extraction, Lyticase can be employed in the preparation of bacterial protoplasts, the construction of bacterial expression systems, and the isolation of chromosomal DNA. It is also useful in the analysis of bacterial cell wall composition and structure. By leveraging the cell wall-degrading properties of Lyticase, researchers can optimize their experimental protocols and unlock new insights in areas such as microbiology, genetic engineering, and synthetic biology.

More about "Lyticase"

Lyticase is a crucial enzyme used in molecular biology research, particularly for the extraction and purification of nucleic acids like DNA and RNA from bacterial samples.
This powerful enzyme hydrolyzes the peptidoglycan layer in bacterial cell walls, allowing for the release of cellular contents.
Researchers can employ Lyticase to optimize their protocols, enhancing the accuracy and reproducibility of their experiments.
Lyticase is commonly used in conjunction with other enzymes and kits, such as Sorbitol, Lysozyme, β-mercaptoethanol, and various DNA extraction kits like the QIAamp DNA Mini Kit, QIAamp DNA Stool Mini Kit, and DNeasy Blood and Tissue Kit.
These tools and techniques work together to ensure efficient and reliable nucleic acid isolation from a variety of sample types, including bacterial cultures, tissue samples, and even stool.
The application of Lyticase extends beyond just DNA and RNA extraction.
It is also utilized in the analysis of bacterial genomes, particularly with the use of high-throughput sequencing platforms like the MiSeq and HiSeq 2500.
By leveraging Lyticase to lyse bacterial cells, researchers can optimize their sample preparation workflows and enhance the quality and reproducibility of their sequencing data.
To further optimize your Lyticase protocols, consider using AI-driven tools like PubCompare.ai.
This powerful platform can help you locate and analyze relevant protocols from peer-reviewed literature, preprints, and patents, allowing you to identify the best methods and products for your specific research needs.
Enhance your accuracy and reproducibility with the help of this innovative AI tool.