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Phenylmethylsulfonyl Fluoride

Phenylmethylsulfonyl fluoride is a serine protease inhibitor commonly used in biochemical research to prevent protein degradation.
It inactivates a wide range of enzymes by irreversibly binding to their active sites.
Researchers can optimize their PMSF-based protocols using PubCompare.ai's AI-driven platform, which effortlessely locates the best methods from literature, preprints, and patents.
This streamlines research and helps find the most effective solutions for PMSF-related experiments.

Most cited protocols related to «Phenylmethylsulfonyl Fluoride»

Transcriptional Regulation by Groucho4 and Dichaete

Cited 13 times

4.5 μg of pBind-vnd or empty pBind, 1.5 μg of pCMV-flag-grg4 or pCMV-flag-dichaete or empty vector, and 1.6 μg of pGL3-vnd or pGL3-ind were transfected into 100 mm dishes containing 293 cells. Forty-eight hours after transfection, cells were washed with PBS, scraped and the supernatant removed following centrifugation. Cells were resuspended in immunoprecipitation (IP) buffer [20 mM Tris–HCl, 100 mM NaCl, 10 mM NaF, 1 mM Na₃VPO₄, 1 mM phenylmethylsulfonyl fluoride (PMSF) and protease inhibitor cocktail (Roche) containing 0.5% Triton X-100] and briefly vortexed. Non-specific binding proteins were removed by pre-incubating the supernatant with protein A/G PLUS agarose (Santa Cruz Biotechnology) for 30 min at 4°C, and then removing them by centrifugation. Cell lysates were then incubated with M2 anti-Flag antibody (Sigma), and rotated overnight at 4°C, following incubation with protein A/G PLUS agarose, and rotation at 4°C for 2 h. Beads were precipitated by centrifugation, and washed three times with IP buffer containing 0.1% Triton X-100. Then, beads were resuspended in SDS–PAGE sample buffer. Immunoprecipitates were separated by SDS–PAGE electrophoresis, transferred onto Immobilon-P (Millipore) membrane, and western blotted. Duplicate blots were incubated with anti-Flag antibody (Sigma) to detect the Flag-tagged Groucho 4 and Dichaete proteins, or a Gal4-specific antibody (Santa Cruz Biotechnology) to detect Gal4–Vnd chimeric protein. Binding of peroxidase-conjugated secondary antibodies was detected by chemiluminescence, using the Lightning kit (Perkin Elmer).

Yu Z., Syu L.J, & Mellerick D.M. (2005). Contextual interactions determine whether the Drosophila homeodomain protein, Vnd, acts as a repressor or activator. Nucleic Acids Research, 33(1), 1-12.

Publication 2005

Antibodies Antibodies, Anti-Idiotypic Binding Proteins Buffers Cells Centrifugation Chemiluminescence Chimera Cloning Vectors Electrophoresis Hyperostosis, Diffuse Idiopathic Skeletal Immobilon P Immunoglobulins Immunoprecipitation Paragangliomas 3 Peroxidase Phenylmethylsulfonyl Fluoride Protease Inhibitors Proteins SDS-PAGE Sepharose Sodium Chloride Staphylococcal Protein A Tissue, Membrane Transfection Triton X-100 Tromethamine

Western Blot Analysis of H9c2 Cells

Cited 11 times

Culture H9c2 cells were scraped and washed once with PBS, then cell suspension was spun down, and lysed in RIPA buffer (HEPES 20 mM, MgCl2 1.5 mM, EDTA 2 mM, EGTA 5 mM, dithiothreitol 0.1 mM, phenylmethylsulfonyl fluoride 0.1 mM, pH 7.5), and spun down 12,000 rpm for 20 min, the supernatant was collected in new eppendorf tube. Proteins (30 μg) were separated by electrophoresis on SDS-polyacrylamide gel. After the protein had been transferred to polyvinylidene difluoride membrane, the blots was incubated with blocking buffer (1X PBS and 5% nonfat dry milk) for 1 h at room temperature and then probed with primary antibodies (1:1000 dilutions) overnight at 4 °C, followed by incubation with horseradish peroxidase-conjugated secondary antibody (1:5000) for 1 h. To control equal loading of total protein in all lanes, blots were stained with mouse anti-β-actin antibody at a 1:50000 dilution. The bound immunoproteins were detected by an ECL kit.

Wu K.M., Hsu Y.M., Ying M.C., Tsai F.J., Tsai C.H., Chung J.G., Yang J.S., Tang C.H., Cheng L.Y., Su P.H., Viswanadha V.P., Kuo W.W, & Huang C.Y. (2019). High-density lipoprotein ameliorates palmitic acid-induced lipotoxicity and oxidative dysfunction in H9c2 cardiomyoblast cells via ROS suppression. Nutrition & Metabolism, 16, 36.

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Publication 2019

Actins Antibodies Antibodies, Anti-Idiotypic Buffers Cell Culture Techniques Cells Dithiothreitol Edetic Acid Egtazic Acid Electrophoresis HEPES Horseradish Peroxidase Immunoglobulins Immunoproteins Magnesium Chloride Milk, Cow's Mus Phenylmethylsulfonyl Fluoride polyacrylamide gels polyvinylidene fluoride Proteins Radioimmunoprecipitation Assay Technique, Dilution Tissue, Membrane

Western Blot Analysis of GABAergic Signaling Proteins

Cited 11 times

Western blot analysis was carried out as previously described (Maguire and Mody, 2007 (link);Maguire et al., 2009 (link);Maguire et al., 2005 (link)). Animals were anesthetized with isoflurane, killed by decapitation, and the PVN, hippocampus, and cerebellum were rapidly removed. The tissue was sonicated in homogenization buffer (containing 10mM NaPO4, 100mM NaCl, 10mM sodium pyrophosphate, 25mM NaF, 5mM EDTA, 5mM EGTA, 2% Triton X-100, 0.5% Deoxycholate, 1mM sodium vanadate, pH 7.4) in the presence of protease inhibitors (complete mini, Roche, and fresh phenylmethylsulfonyl fluoride (PMSF)). The lysate was incubated on ice for 30 min then the supernatant was collected following centrifugation at 14,000 rpm for 10 min at 4°C. Protein concentrations were determined using the DC Protein Assay (BioRad). Total protein (100 μg for the GABA_AR δ subunit and 50 μg for KCC2 and Ser940) was loaded onto a 10% SDS–polyacrylamide gel, subjected to gel electrophoresis, transferred to a Immobilon-P membrane (Millipore), blocked in 10% non–fat milk, and probed with a monoclonal antibody specific for the GABA_AR δ subunit (1:500, PhosphoSolutions 868-GDN), KCC2 (1:1000, Millipore), or Ser940 (1:1000, a generous gift from Dr. Steve Moss). The blots were incubated with peroxidase labeled anti–rabbit IgG (1:2000, GE Healthcare) and immunoreactive proteins were visualized using enhanced chemiluminescence (Amersham). Optical density measurements were determined using the NIH Image J software.
For biotinylation experiments, slices containing the PVN were incubated in 1mg/ml NHS-biotin (Pierce) in normal artificial cerebral spinal fluid (nACSF) for 30 min on ice. The slices were then washed thoroughly with ice cold nACSF and the total protein was isolated and quantified as described above. 100μg of total protein was incubated with 50μl of streptavidin magnetic beads (Pierce) in 1ml phosphate-buffered saline (PBS) overnight at 4°C. The solution was centrifuged and the pellet was thoroughly washed and resuspended in 50μl loading buffer. The proteins were eluted from the magnetic beads which were removed by centrifugation, and 20μl of the loading buffer/protein solution was loaded onto a polyacrylamide gel and proteins visualized as described above.

Sarkar J., Wakefield S., MacKenzie G., Moss S.J, & Maguire J. (2011). Neurosteroidogenesis Is Required for the Physiological Response to Stress: Role of Neurosteroid-Sensitive GABAA Receptors. The Journal of Neuroscience, 31(50), 18198-18210.

Publication 2011

Animals anti-IgG Biological Assay Biotinylation biotinyl N-hydroxysuccinimide ester Buffers Centrifugation Cerebellum Cerebrospinal Fluid Chemiluminescence Cold Temperature Decapitation Deoxycholate Edetic Acid Egtazic Acid Electrophoresis Immobilon P Isoflurane Milk, Cow's Monoclonal Antibodies Mosses Peroxidase Phenylmethylsulfonyl Fluoride Phosphates polyacrylamide gels Protease Inhibitors Proteins Protein Subunits Rabbits Saline Solution Seahorses Sodium Chloride sodium pyrophosphate Sodium Vanadate Streptavidin Tissue, Membrane Tissues Triton X-100 Vision Western Blot

Recombinant Protein Expression and Purification

Cited 11 times

Luria Bertani (LB) medium, BactoAgar, 100 mm Petri dish plates were obtained from Becton-Dickinson. NO₂Y, M9 salts, ampicillin (Amp), L-arabinose (L-Ara), chloramphenicol (Cm), all amino acids, ATP, 2′-deoxyguanine 5′-trihosphate (dGTP), cytidine 5′-dihosphate (CDP), adenine 5′-diphoshate (ADP), NADPH, ethylenediamine tetraacetic acid (EDTA), Bradford Reagent, Sehadex G-25, phenylmethanesulfonyl fluoride (PMSF) and stretomycin sulfate were purchased from Sigma-Aldrich. Isoproyl-β-d-thiogalactopyranoside (IPTG), dithiothreitol (DTT), DpnI and T4 DNA ligase were from Promega. pBAD/Myc-His A, E. coli DH5α and TOP10 competent cells, pCR2.1-TOPO, bacterial alkaline phosphatase and oligonucleotides were from Invitrogen. Calf-intestine alkaline phosphatase (CIAP, 20 U/μL) was from Roche. NcoI, XhoI, SalI, BglII, NdeI and PstI were from New England Biolabs. The purification of E. coli thioredoxin36 (link) (TR, 40 units/mg), E. coli thioredoxin reductase37 (link) (TRR, 1400 units/mg), and wild-tye (wt) β238 (link) (6200-7200 nmol/min/mg, 1-1.2 radicals per β2) and wt α239 (link) (2300-2600 nmol/min/mg) have previously been described. The concentrations of α2 and [NO₂Y]-α2s were determined using ε_280nm = 189 mM⁻¹ cm⁻¹.40 (link) The concentrations of β2 and [NO₂Y₁₂₂]-β2 were determined using ε_280nm = 131 mM⁻¹ cm⁻¹.40 (link) The concentrations of apo-[NO₂Y₁₂₂]-β2 were determined using ε_280nm = 120 mM⁻¹ cm⁻¹.41 (link) Glycerol minimal media leucine (GMML)42 (link) contains final concentrations of 1% (v/v) glycerol, 1×M9 salts, 0.05% (w/v) NaCl, 1 mM MgSO₄, 0.1 mM CaCl₂, and 0.3 mM L-leucine. RNR assay buffer consists of 50 mM HEPES, 15 mM MgSO₄, 1 mM EDTA, pH 7.6. UV-vis absorption spectra and the spectrophotometric assays were carried out using the Cary 3 UV-vis Spectrophotometer (Varian, Walnut Creek, CA). The Ultramark EX Microlate Imaging System (BioRad) was used to determine A_280nm for protein, A_340nm for diferric cluster and NO₂Y phenol, A_490nm for NO₂Y phenolate of fractions after column chromatograhy. All DNA sequences were confirmed by the MIT Biopolymers Laboratory. PCR was carried out using PfuUltraII polymerase (Stratagene) according to the manufacturer’s protocol. The annealing temperature and number of cycles varied are described individually. For site-directed mutagenesis, PCR was performed for 18 cycles with annealing temperature of 55°C, followed by DpnI digestion of methylated template plasmid. The primers used for PCR are summarized in Table S2. pSUP-3NT/835 (link) was kindly supplied by Dr. J. W. Chin (Medical Research Council Laboratory of Molecular Biology, Cambridge, U.K.) and Dr. R. A. Mehl’s lab (Franklin & Marshall College, Lancaster) and pEVOL43 (link) was a kind gift of Dr. P. G. Schultz (The Scripps Research Institute, San Diego).

Yokoyama K., Uhlin U, & Stubbe J. (2010). Site-specific incorporation of 3-nitrotyrosine as a probe of pKa perturbation of redox-active tyrosines in ribonucleotide reductase. Journal of the American Chemical Society, 132(24), 8385-8397.

Publication 2010

Adenine Alkaline Phosphatase Amino Acids Ampicillin Arabinose Bacteria Biological Assay Biopolymers Buffers Cells Chin Chloramphenicol Cytidine Digestion Dithiothreitol DNA Sequence Edetic Acid Escherichia coli Glycerin HEPES Hyperostosis, Diffuse Idiopathic Skeletal Intestines Juglans Leucine Mutagenesis, Site-Directed NADP Oligonucleotide Primers Oligonucleotides Phenol Phenylmethylsulfonyl Fluoride Plasmids Promega Proteins Salts Sodium Chloride Spectrophotometry Sulfate, Magnesium Sulfates, Inorganic T4 DNA Ligase Topotecan TXN protein, human

Purification of Ndc80 Complex from S. cerevisiae and Humans

Cited 11 times

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Publication 2009

Aprotinin Benzonase Buffers Chromatography, Affinity chymostatin Claw Cloning Vectors Gel Chromatography Genes HEPES his6 tag Homo sapiens leupeptin NDC80 protein, human pepstatin Phenylmethylsulfonyl Fluoride Protease Inhibitors Protein Subunits Resins, Plant Saccharomyces cerevisiae Sodium Chloride Strains

Most recents protocols related to «Phenylmethylsulfonyl Fluoride»

Western Blot Analysis of Chondrocyte Proteins

Expression of proteins of interest in chondrocytes and articular cartilage tissues were explored through western blot analysis. Briefly, cultured chondrocytes and previously ground tissues powder (100 mg) were lysed for 1 h using ice cold 1 × RIPA lysis buffer (Beyotime) supplemented with phenylmethanesulfonyl fluoride (PMSF, 1 mM, Beyotime). The lysates were centrifugated for 10 min at 4 °C and 12,000 rpm. The supernatant was transferred to a new tube for protein quantification. A standard curve was prepared with gradient concentration of BSA according to the instructions of a BCA quantification kit (Beyotime, China). For western blotting assay, the protein samples were mixed with 5 × loading buffer and heated for 10 min at 98 °C. Thereafter, 30 ug protein samples were separated by 10%–12.5% SDS-PAGE gels and transferred to polyvinylidene fluoride membranes (Bio-Rad, USA). The membrane was rinsed with TBS-T, following with 5% nonfat milk for 1.5 h. Then, the membranes were incubated with primary antibodies specific to HBEGF (1:200, Abcam, Cat# ab92620), MMP3 (1:1000, Abcam, Cat# ab137659), MMP13 (1:1000, Abcam, Cat# ab84594), ADAMTS4 (1:1000, Abcam, Cat# ab84792), COL2A1 (1:1000, Abcam, Cat# ab34712), Aggrecan (1:100, ABclonal, Cat# A8536), or β-actin (1:2000) (Cell Signaling Technology, Cat# 4970) at 4 °C overnight. The blots were then rinsed and probed with secondary HRP-conjugated anti-rabbit or anti-mouse antibodies (Beyotime Institute of Biotechnology, Nantong, China), and proteins were detected using an ECL kit (Santa Cruz Biotechnology, TX, USA).

Zhu Y., Zhang C., Jiang B, & Dong Q. (2023). MiR-760 targets HBEGF to control cartilage extracellular matrix degradation in osteoarthritis. Journal of Orthopaedic Surgery and Research, 18, 186.

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Publication 2023

Actins Aggrecans Anti-Antibodies Antibodies Buffers Cartilages, Articular Chondrocyte Cold Temperature Gels HBEGF protein, human Milk, Cow's MMP3 protein, human MMP13 protein, human Mus Phenylmethylsulfonyl Fluoride polyvinylidene fluoride Powder Proteins Rabbits Radioimmunoprecipitation Assay SDS-PAGE Tissue, Membrane Tissues Western Blot

Protein Purification and Droplet Assay

For protein purification, Plasmids containing the protein of interest fused to GFP were transformed into BL21 cell (NEB, C2527I). A fresh bacterial colony was inoculated into 200 ml LB media containing kanamycin and grown at 37 °C until an OD₆₀₀ of 0.8–0.9 has been reached. IPTG was added to 1 mM and growth continued overnight at 16°C. Pallets from 200 ml cells were resuspended in 10 ml of GST lysis buffer (50 mM Tris-HCl pH7.5, 100 mM NaCl) containing 1 mM dithiothreitol, 0.2 mM Phenylmethylsulfonyl fluoride, 1% Triton-X100, complete protease inhibitor and sonicated (4 cycle of 30 sec on, 30 sec off). The lysate was cleared by centrifugation at 12,000 × g for 20 min at 4 °C and added NaCl to 500 mM. Then the supernatant was added 500 μl glutathione agarose (Thermo Fisher, 16100) (prewashed in lysis buffer). Tubes containing this agarose lysate slurry were rotated at 4 °C overnight. Then the packed agarose washed twice with GST lysis buffer containing 500 mM NaCl and twice with GST lysis buffer. Protein was obtained by cleavage of Pierce^TM HRV 3 C protease and judged by coomassie stained gel.
For droplet assay, protein was added to solutions at varying concentrations with indicated final salt and molecular crowder concentrations in Buffer A (50 mM Tris-HCl pH 7.5, 10% glycerol, 1 mM DTT). The protein solution was immediately loaded onto a homemade chamber comprising a glass slide with a coverslip attached by two parallel strips of double-sided tape. Slides were then imaged with an Andor confocal microscope with a ×100 objective. Imaging was obtained by the Olympus FV1000 IX81-SIM Confocal Microscope (Olympus, Tokyo, Japan).

Li X., Wang S., Xie Y., Jiang H., Guo J., Wang Y., Peng Z., Hu M., Wang M., Wang J., Li Q., Wang Y, & Liu Z. (2023). Deacetylation induced nuclear condensation of HP1γ promotes multiple myeloma drug resistance. Nature Communications, 14, 1290.

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Publication 2023

Bacteria Biological Assay Buffers Cells Centrifugation Cytokinesis Dithiothreitol Glutathione Glycerin Isopropyl Thiogalactoside Kanamycin Microscopy, Confocal Phenylmethylsulfonyl Fluoride Plasmids protease C Protease Inhibitors Proteins Sepharose Sodium Chloride Triton X-100 Tromethamine

Western Blot Protein Expression Analysis

Protein lysates were prepared in RIPA-buffer (50 mM Tris-HCl pH 7.5, 150 mM NaCl, 10 mM EDTA, 0.5% sodium deoxycholate, 1% NP-40, 1 mM sodium dodecyl sulfate, 10 μg/mL aprotinin, 1 mM phenylmethanesulfonyl fluoride, and 10 μg/mL leupeptin) supplemented with complete protease inhibitors (Roche, Indianapolis, IN, USA). The protein concentration was determined using the BCA protein assay kit (ThermoFisher Scientific, Carlsbad, CA, USA). Cell lysate (50 μg) was separated by electrophoresis on SDS-PAGE gel and transferred to nitrocellulose membranes (Pall Corporation, Washington, NY, USA). Membranes were blocked with 5% non-fat milk for 1 h at room temperature and infiltrated overnight at 4 °C with specific antibodies. Antibodies used in this study were listed in the Supplementary Information. Membranes were washed three times in PBST the next day, then incubated with horseradish peroxidase-conjugated secondary antibodies for 1 h at room temperature, washed three times with PBST and finally bands were visualized using an enhanced chemiluminescence system (Millipore, Los Angeles, CA USA). The representative western blot images for at least three independent experiments shown in the figures have been cropped and auto contrasted.

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Publication 2023

Antibodies Aprotinin Biological Assay Buffers Cells Chemiluminescence Deoxycholic Acid, Monosodium Salt Edetic Acid Electrophoresis Horseradish Peroxidase leupeptin Milk, Cow's Nitrocellulose Nonidet P-40 Phenylmethylsulfonyl Fluoride Protease Inhibitors Proteins Radioimmunoprecipitation Assay SDS-PAGE Sodium Chloride Sulfate, Sodium Dodecyl Tissue, Membrane Tromethamine Western Blotting

Immunoblotting analysis of stemness markers

Cells were lysed in Radioimmunoprecipitation assay buffer (Solarbio) containing phenylmethylsulphonyl fluoride protease inhibitor. Protein samples were subjected to 10% SDS polyacrylamide gel electrophoresis. The separated proteins were subsequently transferred to a polyvinylidene fluoride membrane. The membrane was blocked using 10% non-fat milk for 1 h at room temperature and then incubated with primary antibodies overnight at 4 °C. Primary antibodies recognizing the following proteins were used: CD24 (1:1000, Proteintech, Wuhan, China, Cat#18330-1-AP), SOX2 (1:1000, Cell Signaling Technology, Cat#14962), ALDH1 (1:1000, Cell Signaling Technology, Cat#54135), OCT4 (1:1000, Wanlei, Shenyang, China, WL02020), BMI1 (1:1000, Cell Signaling Technology, Cat#6964), YAP1 (1:1000, Cell Signaling Technology, Cat#14074), GAPDH (encoding glyceraldehyde-3-phosphate dehydrogenase) (1:20000, Proteintech, Cat#60004-1). anti-phospho Histone H2A.X (Ser139) (1:1000, Cell Signaling Technology, Cat#9718). Thereafter, the membranes were incubated with secondary antibodies corresponding to the primary antibodies for 1 h at room temperature. Finally, the immunoreactive protein bands were visualized using ECL (NCM Biotech, Suzhou, China) Western blot detection reagent.

Qin Z., Zhang W., Liu S., Wang Y., Peng X, & Jia L. (2023). PVT1 inhibition stimulates anti-tumor immunity, prevents metastasis, and depletes cancer stem cells in squamous cell carcinoma. Cell Death & Disease, 14(3), 187.

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Publication 2023

Aldehyde Dehydrogenase 1 Family Antibodies BMI1 protein, human Buffers Cells GAPDH protein, human GIT1 protein, human Glyceraldehyde-3-Phosphate Dehydrogenases H2AX protein, human Milk, Cow's Phenylmethylsulfonyl Fluoride polyvinylidene fluoride POU5F1 protein, human Protease Inhibitors Proteins Radioimmunoprecipitation Assay SDS-PAGE SOX2 protein, human Tissue, Membrane Western Blotting YAP1 protein, human

Western Blot Analysis of Recombinant Proteins

WB was performed to confirm the expression of recombinant proteins. Cells (∼10⁶ cells per well) were lysed with 60 μl of radioimmunoprecipitation assay (RIPA) lysis buffer (50 mM Tris, pH 8, 150 mM NaCl, 0.1% SDS, 0.5% sodium deoxycholate, 1% Triton X-100, 1 mM phenylmethylsulfonyl fluoride [HY-B0496; MedChemExpress], and protease inhibitor cocktail [HY-K0010; MedChemExpress]) on ice for 30 min. After incubation, the sample was centrifuged at 21,600 × g for 10 min at 4°C to remove the insoluble fraction. The supernatant was mixed with SDS-PAGE loading buffer and boiled at 95°C for 5 min or kept at 4°C overnight (for multitransmembrane proteins). The proteins were separated by SDS-PAGE and transferred onto poly vinylidene di-fluoride membranes, and the membranes were blocked at RT in Tris-buffered saline containing 0.1% Tween-20 (TBS-T) and 5% nonfat milk for 1 h, followed by incubation with primary antibodies at RT for 1 h. After washing three times with TBS-T buffer, the membranes were then incubated with HRP-labeled secondary antibodies for 1 h at RT. After washing with TBS-T, the membrane was visualized with ECL Prime WB Detection Reagent (GE Health care).

Liu Y.S., Wang Y., Zhou X., Zhang L., Yang G., Gao X.D., Murakami Y., Fujita M, & Kinoshita T. (2023). Accumulated precursors of specific GPI-anchored proteins upregulate GPI biosynthesis with ARV1. The Journal of Cell Biology, 222(5), e202208159.

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Publication 2023

Antibodies Buffers Cells Deoxycholic Acid, Monosodium Salt Milk, Cow's Phenylmethylsulfonyl Fluoride polyvinylidene fluoride Protease Inhibitors Proteins Radioimmunoprecipitation Assay Recombinant Proteins Saline Solution SDS-PAGE Sodium Chloride Tissue, Membrane Triton X-100 Tween 20

Top products related to «Phenylmethylsulfonyl Fluoride»

Pvdf membrane by Merck Group

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PVDF membranes are a type of laboratory equipment used for a variety of applications. They are made from polyvinylidene fluoride (PVDF), a durable and chemically resistant material. PVDF membranes are known for their high mechanical strength, thermal stability, and resistance to a wide range of chemicals. They are commonly used in various filtration, separation, and analysis processes in scientific and research settings.

Protease inhibitor cocktail by Merck Group

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The Protease Inhibitor Cocktail is a laboratory product designed to inhibit the activity of proteases, which are enzymes that can degrade proteins. It is a combination of various chemical compounds that work to prevent the breakdown of proteins in biological samples, allowing for more accurate analysis and preservation of protein integrity.

Phenylmethylsulfonyl fluoride by Merck Group

Sourced in United States, Germany, China, Italy, France, Spain, Canada, Sao Tome and Principe, United Kingdom, Japan, Switzerland

Phenylmethylsulfonyl fluoride is a reagent commonly used in biochemistry and molecular biology laboratories. It functions as a serine protease inhibitor, preventing the activity of certain enzymes. The product is provided in a pure, crystalline form.

Protease inhibitor cocktail by Roche

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Protease inhibitor cocktail is a laboratory reagent used to inhibit the activity of proteases, which are enzymes that break down proteins. It is commonly used in protein extraction and purification procedures to prevent protein degradation.

Bca protein assay kit by Beyotime

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The BCA protein assay kit is a colorimetric-based method for the quantitative determination of total protein concentration in a sample. It uses bicinchoninic acid (BCA) to detect and quantify the presence of protein.

Ripa lysis buffer by Beyotime

Sourced in China, United States, Switzerland, Germany, Japan, United Kingdom

RIPA lysis buffer is a detergent-based buffer solution designed for the extraction and solubilization of proteins from cells and tissues. It contains a mixture of ionic and non-ionic detergents that disrupt cell membranes and solubilize cellular proteins. The buffer also includes additional components that help to maintain the stability and activity of the extracted proteins.

Bca protein assay kit by Thermo Fisher Scientific

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The BCA Protein Assay Kit is a colorimetric detection and quantification method for total protein concentration. It utilizes bicinchoninic acid (BCA) for the colorimetric detection and quantification of total protein. The assay is based on the reduction of Cu2+ to Cu1+ by protein in an alkaline medium, with the chelation of BCA with the Cu1+ ion resulting in a purple-colored reaction product that exhibits a strong absorbance at 562 nm, which is proportional to the amount of protein present in the sample.

Polyvinylidene difluoride membrane by Merck Group

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Polyvinylidene difluoride (PVDF) membranes are a type of lab equipment used for various applications. PVDF membranes are known for their chemical resistance, thermal stability, and mechanical strength. They are commonly used in filtration, separation, and transfer processes in laboratory settings.

Phenyl methyl sulfonyl fluoride (pmsf) by Beyotime

Sourced in China, United States, Switzerland, Germany

PMSF is a protease inhibitor. It is used to inhibit serine proteases in biological samples, such as cell lysates or tissue homogenates, to prevent protein degradation during sample preparation and analysis.

Phenyl methyl sulfonyl fluoride (pmsf) by Merck Group

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

PMSF is a protease inhibitor used in biochemical research and laboratory applications. It functions by irreversibly inhibiting serine proteases, which are a class of enzymes involved in various biological processes. PMSF is commonly utilized in protein extraction and purification protocols to prevent proteolytic degradation of target proteins.

What are the different applications of Phenylmethylsulfonyl Fluoride (PMSF)?

Phenylmethylsulfonyl Fluoride (PMSF) is a widely used serine protease inhibitor in biochemical research. It has a variety of applications, including: - Preventing protein degradation during sample preparation and purification - Inactivating a wide range of enzymes by irreversibly binding to their active sites - Protecting proteins from proteolytic cleavage in cell lysis and tissue homogenization - Maintaining the integrity of protein samples during storage and analysis - Enabling the study of enzyme kinetics and mechanisms by inhibiting protease activity - Facilitating the isolation and characterization of specific protein targets of interest

What are some common challenges in using PMSF effectively?

While PMSF is a versatile protease inhibitor, there are a few challenges researchers may face when using it: - PMSF is highly reactive and sensitive to hydrolysis, especially in aqueous solutions. This means it has a short half-life and must be freshly prepared before use. - PMSF can inhibit a wide range of serine proteases, which may not always be desirable. Researchers need to consider the specific proteases in their system and choose the appropriate inhibitor concentration. - PMSF is not effective against some proteases, such as metalloproteases and cysteine proteases. Using a combination of protease inhibitors may be necessary for comprehensive sample protection. - PMSF can sometimes interfere with downstream applications, such as protein assays or enzymatic reactions. Researchers should be aware of potential PMSF incompatibilities and take necessary precautions.

How can PubCompare.ai help with optimizing PMSF-based protocols?

PubCompare.ai's AI-driven platform can be extremely helpful in optimizing your PMSF-based research protocols: 1. Screen protocol literature more efficiently: The platform can rapidly search and analyze a vast database of scientific literature, preprints, and patents to identify the most relevant and effective PMSF-related protocols for your specific research needs. 2. Leverage AI to pinpoint Critical Insights: PubCompare.ai's advanced AI algorithms can highlight key differences in protocol effectiveness, such as optimal PMSF concentrations, incubation times, and compatibility with downstream applications. This enables you to choose the best protocol for reproducibility and accuracy. 3. Identify the most effective PMSF protocols: By comparing a wide range of published protocols, PubCompare.ai can help you find the most effective solutions for your PMSF-related experiments, streamlining your research and saving time.

Are there any variations or types of PMSF that researchers should be aware of?

Yes, there are a few variations of Phenylmethylsulfonyl Fluoride (PMSF) that researchers should be aware of: - PMSF is available in both powder and solution forms. The solution form is more convenient but has a shorter shelf-life due to the hydrolysis issue. - There are also fluorinated PMSF analogues, such as Phenylmethylsulfonyl Fluoride-d7 (PMSF-d7), which can be used for isotopic labeling experiments. - Some researchers may use alternative serine protease inhibitors, such as Phenylmethanesulfonyl Fluoride (PMSF) or 4-(2-Aminoethyl) benzenesulfonyl fluoride hydrochloride (AEBSF), depending on their specific research needs and the protease targets in their system.

More about "Phenylmethylsulfonyl Fluoride"

Phenylmethylsulfonyl fluoride (PMSF) is a widely used serine protease inhibitor in biochemical research.
It helps prevent protein degradation by irreversibly binding to the active sites of a wide range of enzymes.
PMSF is commonly employed in experiments involving protein extraction, purification, and analysis.
In addition to PMSF, other protease inhibitors like the BCA protein assay kit and RIPA lysis buffer are often used in conjunction to ensure the integrity of protein samples.
PVDF (polyvinylidene difluoride) membranes are a popular choice for Western blotting experiments, where PMSF can be utilized to preserve the proteins during the transfer process.
Researchers can optimize their PMSF-based protocols using PubCompare.ai's AI-driven platform, which effortlessly locates the best methods from literature, preprints, and patents.
This streamlines the research process and helps find the most effective solutions for PMSF-related experiments.
The platform's advanced comparison tools allow users to easily identify the most suitable protocols, saving time and improving experimental outcomes.
Whether you're working with serine proteases, investigating protein-protein interactions, or analyzing protein expression, understanding the use of PMSF and related techniques can be invaluable.
By leveraging the power of PubCompare.ai, you can enhance your research efficiency and stay ahead of the curve in the dynamic field of biochemistry.