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Pronase E

Pronase E is a highly versatile enzyme used in a variety of biochemical and molecular biology applications.
This proteolytic enzyme is derived from the bacterium Streptomyces griseus and is known for its broad substrate specificity, efficiently cleaving peptide bonds within protein structures.
Pronase E has proven invaluable in processes such as DNA and RNA extraction, cell lysis, and the preparation of protein samples for analysis.
Researchers can leverage the power of PubCompare.ai, an AI-driven platform, to identify the most accurate and reproducible Pronase E protocols from the scientific literature, pre-prints, and patents, ensuring reliable and reproducible results in their experiments.
With PubCompare.ai's powerful comparison tools, scientists can easily locate the best methods for their Pronase E research, taking their studies to new heights.

Most cited protocols related to «Pronase E»

Murine Tracheal Epithelial Cell Culture

Cited 9 times

NIH/3T3 and 293T cells were grown in DME with 10% FBS (Invitrogen). MTEC culture was based on You et al. (2002) (link). Mice were killed at 4–6 mo of age, and trachea were excised, trimmed of excess tissue, opened longitudinally to expose the lumen, and placed in 1.5 mg/ml pronase E in F-12K nutrient mixture (Invitrogen) at 4°C overnight. Tracheal epithelial cells were dislodged by gentle agitation and collected in F-12K with 10% FBS. Cells were treated with 0.5 mg/ml DNase I for 5 min on ice and centrifuged at 4°C for 10 min at 400 g. Cells were resuspended in DME/F-12 (Invitrogen) with 10% FBS and plated in a tissue culture dish for 3 h at 37°C and 5% CO₂ to adhere contaminating fibroblasts. Nonadhered cells were resuspended in an appropriate volume of MTEC Plus medium (You et al., 2002 (link)) and seeded onto Transwell-Clear (Corning) permeable filter supports at 10⁵ cells/cm². The ALI was created ∼2 d after cells reached confluence, by feeding MTEC Serum-free or MTEC NuSerum medium (You et al., 2002 (link)) only from below the filter. Cells were cultured at 37°C and 5% CO₂ and fed fresh medium every 2 d. Beating cilia were observed by phase microscopy 2–3 d after ALI creation. All chemicals were obtained from Sigma-Aldrich unless otherwise indicated. All media were supplemented with 100 U/ml penicillin, 100 mg/ml streptomycin, and 0.25 mg/ml Fungizone (all obtained from Invitrogen).

Vladar E.K, & Stearns T. (2007). Molecular characterization of centriole assembly in ciliated epithelial cells. The Journal of Cell Biology, 178(1), 31-42.

Publication 2007

Cells Cilia Deoxyribonuclease I Deoxyribonucleases Epithelial Cells Fibroblasts Fungizone HEK293 Cells Hyperostosis, Diffuse Idiopathic Skeletal Microscopy Mus NIH 3T3 Cells Nutrients Penicillins Permeability Pronase E Serum Somatostatin-Secreting Cells Streptomycin Tissues Trachea

Osteoclast Formation from Murine Cell Coculture

Cited 9 times

Osteoblasts obtained from the calvaria of newborn ddY mice and bone marrow cells from ddY mice were cocultured in αMEM containing 10% fetal bovine serum, 1α,25-dihydroxyvitamin D₃ [1α,25(OH)₂D₃] (10⁻⁸ M) (Wako Pure Chemical Co.), and prostaglandin E₂ (10⁻⁶ M) (Sigma Chemical Co.) in 100-mm–diameter dishes coated with Type I collagen gels (Nitta Gelatin Co.) as described previously 38. Osteoclasts formed within 6 d were recovered from the dishes by treating with 0.2% collagenase (crude osteoclasts). To purify osteoclasts, the crude osteoclast preparation was replated and cultured for 8 h. Osteoblasts were then removed by treating with PBS containing 0.001% pronase E and 0.02% EDTA 38. Some of the cultures were then stained for TRAP. The other cultures were further incubated for 36 h in the presence or absence of mouse TNF-α (20 ng/ml), human TNF-α (20 ng/ml), IL-1α (10 ng/ml), or sODF/sRANKL (100 ng/ml), and stained for TRAP. TRAP-positive multinucleated cells containing more than three nuclei were counted as living osteoclasts.

Kobayashi K., Takahashi N., Jimi E., Udagawa N., Takami M., Kotake S., Nakagawa N., Kinosaki M., Yamaguchi K., Shima N., Yasuda H., Morinaga T., Higashio K., Martin T.J, & Suda T. (2000). Tumor Necrosis Factor α Stimulates Osteoclast Differentiation by a Mechanism Independent of the Odf/Rankl–Rank Interaction. The Journal of Experimental Medicine, 191(2), 275-286.

Publication 2000

Bone Marrow Cells Calvaria Cell Nucleus Cells Collagen Type I dihydroxy-vitamin D3 Dinoprostone Edetic Acid Fetal Bovine Serum Gelatins Gels Homo sapiens Hyperostosis, Diffuse Idiopathic Skeletal Infant, Newborn Mus Neutrophil Collagenase Osteoblasts Osteoclasts Pronase E Tumor Necrosis Factor-alpha

Isolation of Primary Mouse Hepatic Stellate Cells

Cited 6 times

Primary mouse HSCs were isolated according to established protocols [9] (link), [21] (link), [22] (link). Briefly, livers were perfused in situ with EGTA for 5 min, pronase E (0.4 mg/ml, EMD Chemicals Inc., Gibbstown, NJ) for 5 min and collagenase D (0.5 mg/ml, Roche Diagnostics) for 8 min, respectively, at a flow rate of 5 ml/min. After excision of the liver from the body, the liver digests were filtered through a cell strainer and washed with Gey's Balanced Salt Solution (Sigma, St. Louis, MO) containing DNase I (2 mg/ml, Roche Diagnostics). For the WT C57 mice, HSCs were purified from the remainder of non-parenchymal cells and hepatocyte-derived debris by floatation through 9% (w/v) Nycodenz (Axis-Shield PoC AS, Oslo, Norway) in Gey's Balanced Salt Solution (without NaCl). Subsequently, the cells were separated by FACS using FACS Calibur (Becton Dickinson, Franklin Lakes, NJ), and vitamin A auto-fluorescent cells were collected based on their emission at 460 nm. This method of HSC isolation yields approximately 10% of the total HSCs estimated to be in the liver. For the collagen-GFP mice, parenchymal cells and debris were separated from non-parenchymal cells by centrifugation at 50 g for 2 minutes. The remaining non-parenchymal cell suspension was then separated by FACS, and GFP-positive cells were collected based on their emission at 530 nm. This method of HSC isolation yields approximately 10% of the total HSCs estimated to be in the liver.

D'Ambrosio D.N., Walewski J.L., Clugston R.D., Berk P.D., Rippe R.A, & Blaner W.S. (2011). Distinct Populations of Hepatic Stellate Cells in the Mouse Liver Have Different Capacities for Retinoid and Lipid Storage. PLoS ONE, 6(9), e24993.

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Publication 2011

Cells Centrifugation Collagen Collagenase Deoxyribonuclease I Diagnosis Egtazic Acid Epistropheus Hepatectomy Hepatocyte Human Body isolation Liver Mus Nycodenz Pronase E Sodium Chloride Stem Cells, Hematopoietic Vitamin A

RSV Antigen Immunohistochemistry on Paraffin Sections

Cited 6 times

Immunohistochemistry for RSV antigen was performed on paraffin-embedded tissue as described previously (Meyerholz, et al., 2004 (link)). Briefly, sections were cut at 5μm thickness onto positively charged slides. Following routine deparaffinization, sections were treated with Pronase E (Protease Type XIV from Streptomyces griseus, Sigma) for 12 minutes at 37°C. Nonspecific binding was blocked by incubation in 20% normal swine serum. The sections were incubated with polyclonal goat anti-RSV antibody (BioDesign/Meridian) overnight at a concentration of 1:50 with 5% normal swine serum. The slides were rinsed and then incubated with biotinylated rabbit anti-goat secondary antibody (KPL) at a concentration of 1:300 in 5% normal sheep serum. A peroxidase block with 3% peroxide was followed by incubation with peroxidase-conjugated streptavidin (BioGenex) for 45 minutes. After two PBS washes, the color was developed with Nova Red. The slides were then counterstained with Harris' hematoxylin, dehydrated and cover-slipped.

Olivier A., Gallup J., de Macedo M.M., Varga S.M, & Ackermann M. (2009). Human respiratory syncytial virus A2 strain replicates and induces innate immune responses by respiratory epithelia of neonatal lambs. International Journal of Experimental Pathology, 90(4), 431-438.

Publication 2009

Antibodies, Anti-Idiotypic Antigens Domestic Sheep Goat Hematoxylin Immunohistochemistry Meridians Paraffin Embedding Peroxidase Peroxides Pigs Pronase Pronase E Rabbits Serum Streptavidin Streptomyces griseus Tissues

Isolation and Culture of Androgen-Dependent Prostate Tumor Cells

Cited 6 times

Suspension of CWR22Pc cells was prepared from androgen-dependent human primary prostate tumor xenograft, CWR22P (a gift from Dr. Thomas Pretlow, Case Western Reserve University) using a method described previously for the dissociation of human prostate cancer tissue (9 (link)). Briefly, under sterile conditions, six tumors were dissected from the mice and minced. The minced tumor was washed three times in RPMI 1640 (Life Technologies, Inc., Gaithersburg, MD) supplemented with 20% fetal bovine serum (FBS) (Life Technologies) and the tumor tissue was digested serially with 0.1% Pronase E (EMD Pharmaceuticals, Gibbstown NJ) in Joklik-modified MEM (Sigma, St. Louis, MO). The Pronase E digest fractions were filtered through a single layer of a NITEX 250-micron porosity membrane (Safer America, Depew, NY), and centrifuged at 97 x g for 7.5 minutes at 4°C. The pellets were resuspended in RPMI 1640 supplemented with 20% fetal bovine serum. The cells were counted and the cell viability was confirmed by trypan blue exclusion. The cells were cultured in RPMI 1640 medium containing 10% FBS, 2.5 mM L-glutamine and penicillin-streptomycin (100 IU/ml and 100 μg/ml, respectively) in the presence of 0.8 nM dihydrotestosterone (DHT) (5α-androstan-17β-ol-3-one, Sigma) at 37 °C with 5% CO₂. CWR22Rv1, LNCaP and DU145 cells (ATCC, Manassas, VA) were cultured in RPMI 1640 (Biofluids) containing 10% FBS, 2.5 mM L-glutamine, and penicillin-streptomycin (100 IU/ml and 100 μg/ml, respectively) at 37 °C with 5% CO₂. LNCaP cells were cultured in the presence of 0.8 nM DHT. For testing of inducibility of Stat5a/b and Stat3 by cytokines, the cell lines were serum-starved 16 h after which the cells were stimulated with 10 nM human prolactin (hPrl) or 4 nM interleukin-6 (IL6) (Upstate, Lake Placid, NY) before harvesting the cells for immunoprecipitations.

Dagvadorj A., Tan S.H., Liao Z., Cavalli L.R., Haddad B.R, & Nevalainen M.T. (2008). Androgen-regulated and highly tumorigenic human prostate cancer cell line established from a transplantable primary CWR22 tumor. Clinical cancer research : an official journal of the American Association for Cancer Research, 14(19), 6062-6072.

Publication 2008

Androgens androstan-3-one Cell Lines Cell Survival Culture Media Cytokine Dihydrotestosterone Fetal Bovine Serum Glutamine Homo sapiens Immunoprecipitation Interleukin-6 Mus Neoplasms NOS2A protein, human Pellets, Drug Penicillins Pharmaceutical Preparations Prolactin Pronase E Prostate Cancer Prostatic Neoplasms Safety Serum STAT3 Protein STAT5A protein, human Sterility, Reproductive Streptomycin Tissue, Membrane Tissues Trypan Blue Xenografting

Most recents protocols related to «Pronase E»

Biosynthesis of Polyketide Natural Products

Isotopically labeled reagents and OminPur® Pronase E (4,000 U/mg) were purchased from Sigma Aldrich. GCMS data were acquired with an Agilent 7890 GC with a 30-m × 250-μm × 0.25-mm HP 5-ms UI capillary column and Agilent G7081B MSD. High-resolution mass spectrometry data were acquired with an Agilent 6230 TOF LC/MS System (Agilent Technologies) equipped with a ZORBAX Eclipse XDB C18 column (5 μm, 150 × 4.6 mm). NMR data were recorded at 400 MHz for ¹H and 100 MHz for ¹³C with a Varian Inova NMR spectrometer (Agilent). ¹³C NMR for [2,4,6,8,10,12,14,17,19,21,23,25,27-¹³C]TNM A was acquired using a Bruker NEO 600 MHz (14.1 T) NMR spectrometer equipped with four-channel, 24 slot SampleCase, and a triple resonance (HCN) CryoProbe. The gene encoding SgcE was coexpressed in pET30Xa-LIC vector with SgcE10 in pCDF-F2-EK-LIC vector as previously described (19 (link)). The gene encoding DynE8 was coexpressed in pET30Xa-LIC vector with SgcE10 in pCDF-2-EK-LIC vector. The TNM A-producing strain Streptomyces sp. CB03234 and the generation of the PKSE (ΔtmnE) mutant strain SB20001 were previously described (16 (link)). The DYN A-producing strain Micromonospora chersina ATCC 53710 and the generation of the PKSE (ΔdynE7) mutant strain were previously described (15 ).

Bhardwaj M., Cui Z., Daniel Hankore E., Moonschi F.H., Saghaeiannejad Esfahani H., Kalkreuter E., Gui C., Yang D., Phillips GN J.r., Thorson J.S., Shen B, & Van Lanen S.G. (2023). A discrete intermediate for the biosynthesis of both the enediyne core and the anthraquinone moiety of enediyne natural products. Proceedings of the National Academy of Sciences of the United States of America, 120(9), e2220468120.

Publication 2023

Capillaries Carbon-13 Magnetic Resonance Spectroscopy Cloning Vectors Gas Chromatography-Mass Spectrometry Genes Mass Spectrometry Micromonospora chersina Pronase E Strains Streptomyces Vibration

RNA-seq Analysis of Blastocyst Transcriptomes

Single blastocysts from WT and KO group were collected on day 7. The zona pellucida of blastocysts was discarded with 0.5% pronase E. The RNA-seq libraries were constructed according to Smart-seq2 procedure as previously described (Picelli et al. 2014 (link)). In brief, polyadenylated RNAs were captured and reverse transcribed with an Oligo(dT) primer, then the cDNA was pre-amplified using KAPA HiFi HotStart ReadyMix (kk2601). Pre-amplified cDNA was purified with Ampure XP beads (1:1 ratio) and fragmented by Tn5 enzyme (Vazyme, TD502). PCR amplification for 15–18 cycles was performed to prepare sequencing libraries, which were subject to paired-end 150 bp sequencing on a NovaSeq (Illumina) platform by Novogene. The raw sequencing reads were trimmed with Trimmomatic (version 0.39) (Bolger et al. 2014 (link)) to generate clean data and mapped to ARS-UCD1.2 with Hisat2 (version 2.1.0) (Kim et al. 2015 (link)). The raw counts were calculated with featureCounts (version 1.6.3) (Liao et al. 2014 (link)) and underwent differential expression analysis using DESeq2 (Love et al. 2014 (link)). The differentially expressed WT and KO gene groups were identified using an false discovery rate (FDR)-adjusted P-value (P_adj) less than 0.05. Foldchange ≥1.5 or ≤0.6. Fragments per kilobase million (FPKM) for each sample was calculated with Cufflinks (Trapnell et al. 2012 (link)) for heatmap visualization, and heatmaps were generated using a pheatmap package in R. Gene ontology analysis was performed with the Database for Annotation, Visualization and Integrated Discovery (Huang da et al. 2009a,b (link, link)). All RNA-seq files are available from the Gene Expression Omnibus database (accession number GSE216123).

Shi Y., Hu B., Wang Z., Wu X., Luo L., Li S., Wang S., Zhang K, & Wang H. (2023). Functional role of GATA3 and CDX2 in lineage specification during bovine early embryonic development. Reproduction (Cambridge, England), 165(3), 325-333.

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Publication 2023

Blastocyst DNA, Complementary Enzymes Genes Love MAP2 protein, human Oligonucleotide Primers Oligonucleotides Pronase E RNA, Polyadenylated RNA-Seq Zona Pellucida

Developmental Toxicity Screening in Zebrafish

For chronic developmental exposures
(Figures 2, 3, and 4B), zebrafish embryos
were obtained from natural group spawning and age-matched within the
first hour of fertilization. Enzymatic dechorionation took place at
4 h postfertilization (hpf), where ∼800 embryos were placed
in a round glass plate (10 cm diameter) with 25 mL system water (same
water in which fish were raised) to which 50 μL of 63.6 mg/mL
(∼11.12 U) Pronase E (protease from Streptomyces griseus, ≥ 3.5 U/mg, P5147 Sigma-Aldrich, St. Louis, Missouri) was
added. Constant manual plate agitation took place for 6 min following
a wash with 2 L of system water.^{49 (link)} Dechorionated
embryos were randomly placed in individual wells in 96-well plates
(Falcon, Fisher Scientific, Hampton, New Hampshire) with 100 μL
embryo medium (EM).⁵⁰ Chemical stocks (1000×)
were diluted to 2× in EM, and 100 μL was added to each
well, resulting in final concentrations 0.1, 0.3, 1, 3, and 10 μM
in 0.1% DMSO. Each experimental group included 16 fish per spawning
from three separate spawning events, resulting in a total of n = 48 per group. Plates were covered in Parafilm M (Bemis,
North America, Neenah, Wisconsin) and placed in a 28.5 °C light-controlled
(14 h light (∼300 lx):10 h dark) incubator for static waterborne
exposure through 5 dpf.
For acute developmental exposures (Figure 4A), embryos were
also obtained by natural group spawning. Embryos were raised in Petri
dishes without chemically induced dechorionation until 4 dpf, when
they were transferred to 96-well plates with 100 μL EM. At 5
dpf, exposures were conducted identically to chronic developmental
exposures (100 μL of compounds at 2× of the final concentration
was added to each well) with the exception that behavioral assessments
were conducted immediately after addition of chemical compounds to
wells containing zebrafish larvae.

Tombari R.J., Mundy P.C., Morales K.M., Dunlap L.E., Olson D.E, & Lein P.J. (2023). Developmental Neurotoxicity Screen of Psychedelics and Other Drugs of Abuse in Larval Zebrafish (Danio rerio). ACS Chemical Neuroscience, 14(5), 875-884.

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Publication 2023

Embryo Enzymes Fertilization Fishes Larva Light Peptide Hydrolases Pronase Pronase E protease E Streptomyces griseus Sulfoxide, Dimethyl Zebrafish

Quantifying Sperm Activation in Nematodes

Protocol full text hidden due to copyright restrictions

Open the protocol to access the free full text link

Publication 2023

Buffers Eye Males Monensin Pronase E Pseudopodia Sperm Spermatid

Enzymatic Hydrolysis of Angiotensin-Converting Enzyme

Alcalase^® 2.4 L (from Bacillus licheniformis), Pancreatic Trypsin Novo 6.0S, Protease type XIV, also known as Pronase E (from Streptomyces griseus) and Esperase^® 8.0 L (from Bacillus spp.) were obtained from Novozymes (Bagsværd, Denmark). Angiotensin-Converting Enzyme I (ACE, EC 3.4.15.1), aprotinin, vitamin B12, angiotensin II, hippuryl histidyl leucine (HHL) and glycine were obtained from Sigma Chemical Co., (St. Louis, MO, USA). Abz-GLY-PHe(NO₂)-Pro was obtained from Bachem Feinchemikalien (Bubendorf, Switzerland). All other chemicals and reagents used were of analytical grade and were purchased from Panreac Chemical Corp. (Barcelona, Spain).

Bougatef H., de la Vega-Fernández C., Sila A., Bougatef A, & Martínez-Alvarez O. (2023). Identification of ACE I-Inhibitory Peptides Released by the Hydrolysis of Tub Gurnard (Chelidonichthys lucerna) Skin Proteins and the Impact of Their In Silico Gastrointestinal Digestion. Marine Drugs, 21(2), 131.

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Publication 2023

Angiotensin II Aprotinin Bacillus Bacillus licheniformis Cobalamins Esperase Glycine glycylphenylalanine hippuryl-histidyl-leucine Pancreatic Hormones Peptidyl-Dipeptidase A Pronase Pronase E Streptomyces griseus Subtilisin Carlsberg Trypsin

Top products related to «Pronase E»

Pronase e by Merck Group

Sourced in United States, Germany, Belgium, China, United Kingdom

Pronase E is a highly purified protease enzyme derived from the bacterium Streptomyces griseus. It is a broad-spectrum enzyme that can hydrolyze a wide range of protein substrates, including casein, gelatin, and collagen. Pronase E is commonly used in various laboratory applications that require efficient protein digestion or removal.

Pronase e by Roche

Sourced in Germany, Switzerland, China, United States

Pronase E is a proteolytic enzyme derived from the bacterium Streptomyces griseus. It is a broad-spectrum enzyme capable of hydrolyzing a wide range of protein substrates.

Dnase 1 by Roche

Sourced in United States, Switzerland, Germany, Japan, United Kingdom, France, Canada, Italy, Macao, China, Australia, Belgium, Israel, Sweden, Spain, Austria

DNase I is a lab equipment product that serves as an enzyme used for cleaving DNA molecules. It functions by catalyzing the hydrolytic cleavage of phosphodiester bonds in the DNA backbone, effectively breaking down DNA strands.

Collagenase 4 by Merck Group

Sourced in United States, Germany, United Kingdom, France, China, Sao Tome and Principe, Israel, Canada, Macao, Italy, Australia, Japan, Switzerland, Senegal

Collagenase IV is a purified enzyme used to dissociate and isolate cells from various tissue types. It is effective in breaking down collagen, a major structural component of the extracellular matrix.

Pepsin by Merck Group

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

Pepsin is a proteolytic enzyme produced by the chief cells in the stomach lining. It functions to break down proteins into smaller peptides during the digestive process.

Fetal bovine serum (fbs) by Thermo Fisher Scientific

Sourced in United States, China, United Kingdom, Germany, Australia, Japan, Canada, Italy, France, Switzerland, New Zealand, Brazil, Belgium, India, Spain, Israel, Austria, Poland, Ireland, Sweden, Macao, Netherlands, Denmark, Cameroon, Singapore, Portugal, Argentina, Holy See (Vatican City State), Morocco, Uruguay, Mexico, Thailand, Sao Tome and Principe, Hungary, Panama, Hong Kong, Norway, United Arab Emirates, Czechia, Russian Federation, Chile, Moldova, Republic of, Gabon, Palestine, State of, Saudi Arabia, Senegal

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.

Nycodenz by Merck Group

Sourced in United States

Nycodenz is a non-ionic, iso-osmotic density gradient medium. It is used for the separation and purification of cells, organelles, and macromolecules by density gradient centrifugation.

Pronase e from streptomyces griseus by Merck Group

Sourced in United States

Pronase E is a proteolytic enzyme derived from the bacterium Streptomyces griseus. It is a broad-spectrum enzyme that can cleave a wide range of peptide bonds in proteins and polypeptides.

Dulbecco modified eagle medium (dmem) by Thermo Fisher Scientific

Sourced in United States, China, United Kingdom, Germany, France, Australia, Canada, Japan, Italy, Switzerland, Belgium, Austria, Spain, Israel, New Zealand, Ireland, Denmark, India, Poland, Sweden, Argentina, Netherlands, Brazil, Macao, Singapore, Sao Tome and Principe, Cameroon, Hong Kong, Portugal, Morocco, Hungary, Finland, Puerto Rico, Holy See (Vatican City State), Gabon, Bulgaria, Norway, Jamaica

DMEM (Dulbecco's Modified Eagle's Medium) is a cell culture medium formulated to support the growth and maintenance of a variety of cell types, including mammalian cells. It provides essential nutrients, amino acids, vitamins, and other components necessary for cell proliferation and survival in an in vitro environment.

Nocodazole by Merck Group

Sourced in United States, Germany, United Kingdom, Japan, Sao Tome and Principe, Canada, China, Switzerland, France, Poland, Macao, Australia

Nocodazole is a synthetic compound that acts as a microtubule-destabilizing agent. It functions by binding to and disrupting the polymerization of microtubules, which are essential components of the cytoskeleton in eukaryotic cells. This property makes Nocodazole a valuable tool in cell biology research for studying cell division, cell motility, and other cellular processes that rely on the dynamics of the microtubule network.

What is Pronase E and how is it used in research?

Pronase E is a highly versatile enzyme derived from the bacterium Streptomyces griseus. It has broad substrate specificity, allowing it to efficiently cleave peptide bonds within protein structures. This makes Pronase E invaluable for numerous biochemical and molecular biology applications, such as DNA and RNA extraction, cell lysis, and the preparation of protein samples for analysis. Researchers can leverage the power of PubCompare.ai to identify the most accurate and reproducible Pronase E protocols from the scientific literature, pre-prints, and patents, ensuring reliable and reproducible results in their experiments.

What are some common challenges in using Pronase E?

One of the main challenges in using Pronase E is ensuring the optimal protocol selection for a specific research application. With the vast amount of scientific literature, pre-prints, and patents available, it can be time-consuming and difficult to identify the most effective and reproducible Pronase E methods. This is where PubCompare.ai can be invaluable. The platform's AI-driven analysis can help researchers pinpoint the critical insights needed to choose the best Pronase E protocol for their research goals, ensuring accuracy and reproducibility in their experiments.

Are there different types or variations of Pronase E?

While Pronase E typically refers to a single enzyme derived from Streptomyces griseus, there may be slight variations or formulations available from different manufacturers or suppliers. These variations could include differences in enzyme activity, purity, or specific applications. When selecting a Pronase E product, it's important to carefully review the product specifications and compare them to your research needs. PubCompare.ai can assist in this process by providing a comprehensive comparison of Pronase E protocols from various sources, helping researchers identify the most appropriate variation for their studies.

What are some specific applications of Pronase E?

Pronase E has a wide range of applications in biochemistry and molecular biology research. Some common uses include: - DNA and RNA extraction: Pronase E can be used to lyse cells and degrade protein contaminants, facilitating the isolation of high-quality nucleic acids. - Cell lysis: The enzyme's ability to cleave peptide bonds makes it effective for breaking down cell membranes and releasing cellular contents. - Protein sample preparation: Pronase E is often used to prepare protein samples for analysis, such as mass spectrometry or electrophoresis, by removing interfering substances. - Tissue digestion: Pronase E can be used to dissociate tissue samples, enabling the isolation of specific cell types or subcellular fractions.

How can PubCompare.ai help with the use of Pronase E?

PubCompare.ai allows researchers to screen protocol literature more efficiently and leverage AI to pinpoint critical insights. The platform can help identify the most effective Pronase E protocols related to your specific research goals. PubCompare.ai's AI-driven analysis can highlight key differences in protocol effectiveness, enabling you to choose the best option for reproducibility and accuracy. This ensures your Pronase E experiments deliver reliable and reproducible results, taking your research to new heights.

More about "Pronase E"

Pronase E, a highly versatile proteolytic enzyme derived from the bacterium Streptomyces griseus, has become an invaluable tool in various biochemical and molecular biology applications.
Known for its broad substrate specificity, Pronase E efficiently cleaves peptide bonds within protein structures, making it a crucial component in processes such as DNA and RNA extraction, cell lysis, and the preparation of protein samples for analysis.
Researchers can leverage the power of PubCompare.ai, an AI-driven platform, to identify the most accurate and reproducible Pronase E protocols from the scientific literature, preprints, and patents.
This innovative solution ensures reliable and reproducible results in their experiments by providing access to the best methods for Pronase E research.
Beyond Pronase E, other enzymes like DNase I, Collagenase IV, and Pepsin play important roles in various biological applications.
These enzymes, along with culture media like DMEM and serum supplements like FBS, are often used in conjunction with Pronase E to achieve desired experimental outcomes.
For instance, DNase I is commonly used in conjunction with Pronase E for the extraction and purification of nucleic acids, while Collagenase IV is employed for the dissociation of tissues and cell isolation.
Pepsin, on the other hand, is a proteolytic enzyme that can be used to pre-treat samples prior to Pronase E digestion, enhancing the efficiency of protein analysis.
Furthermore, researchers may utilize density gradient centrifugation techniques, such as Nycodenz, to separate and purify specific cell populations or organelles, complementing the use of Pronase E in their research workflows.
By leveraging the powerful comparison tools of PubCompare.ai, scientists can easily identify the most accurate and reproducible protocols for their Pronase E research, as well as other related enzymes and techniques, ensuring their experiments deliver reliable and reproducible results.
This innovative platform empowers researchers to take their studies to new heights, advancing scientific knowledge and discoveries.