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Cathepsin B

Q: What is Cathepsin B and what are its key functions?

Cathepsin B is a lysosomal cysteine protease that plays a crucial role in protein degradation and turnover. It is involved in various physiological and pathological processes, including inflammation, cancer, and neurodegeneration. This enzyme is a valuable target for research and therapeutic development.

Cathepsin B is a lysosomal cysteine protease that plays a key role in protein degradation and turnover.
It is involved in various physiological and pathological processes, including inflammation, cancer, and neurodegeneration.
This enzyme is a valuable target for research and therapeutic development.
PubCompare.ai's AI-driven platform can help streamline your Cathepsin B research by identifying the most reliable protocols from literature, preprints, and patents.
Leverage data-driven comparisons to optimize research methods and products, enhancing reproducibility and accuracy.
Discover the power of PubCompare.ai to advance your Cathepsin B research needs.

Most cited protocols related to «Cathepsin B»

Caspase-1 and IL-1β Activation Assay

Cited 21 times

Cell culture supernatants were precipitated by adding an equal volume of methanol and 0.25 volumes of chloroform, vortexed and centrifuged at 20.000 × g for 10 min. The upper phase was discarded and 500 µl of methanol was added to the interphase. This mixture was centrifuged at 20.000 × g for 10 min and the protein pellet dried at 55 °C, resuspended in Laemmli buffer and boiled at 99°C for 5 min. Samples were separated by SDS-PAGE (15%) and transferred onto nitrocellulose membranes. As indicated, blots were incubated with rabbit polyclonal antibody to anti murine caspase-1 p10 (sc-514, Santa Cruz Biotechnology, Santa Cruz, CA), rabbit polyclonal anti human caspase-1 p10 (sc-515, Santa Cruz Biotechnology), rabbit polyclonal anti human cleaved IL-1β (Asp116) (Cell Signaling, Boston, MA) or rabbit polyclonal anti murine cathepsin B (R&D Systems, Minneapolis, MN).

Hornung V., Bauernfeind F., Halle A., Samstad E.O., Kono H., Rock K.L., Fitzgerald K.A, & Latz E. (2008). Silica crystals and aluminum salts mediate NALP-3 inflammasome activation via phagosomal destabilization. Nature immunology, 9(8), 847-856.

Publication 2008

Caspase 1 Cathepsin B Cell Culture Techniques Chloroform Homo sapiens Immunoglobulins Interleukin-1 beta Interphase Laemmli buffer Methanol Mus Nitrocellulose Proteins Rabbits SC 514 SDS-PAGE Tissue, Membrane

Synthesis and Characterization of PEGylated Conjugates

Cited 7 times

N-α-Fmoc protected amino acids, 2-(1H-benzotriazol-1-yl)-1,1,3,3-tetramethyluronium hexafluorophosphate (HBTU) and 2-Cl-trityl chloride resin (100–200 mesh, 1.27 mmol/g) were from EMD Biosciences (San Diego, CA). Papain (EC 3.4.22.2, from papaya latex) and cathepsin B (EC 3.4.22.1, from bovine spleen) were from Sigma-Aldrich (St. Louis, MO). Bis-MAL-dPEG3 (bis-[1,13-(3-maleimidopropionyl)amido]-4,7,10-trioxatridecane, CAS# 756525-89-0) was purchased from Quanta Biodesign (Powell, OH). 1-Hydroxybenzotriazole (HOBt) was purchased from AnaSpec (Fremont, CA). N,N′-Diisopropylcarbodiimide (DIC), 2,2,2-trifluoroethanol (TFE) and all other reagents and solvents were from Sigma-Aldrich (St. Louis, MO). Doxorubicin (DOX) was a kind gift from Meiji Seika Kaisha Ltd. Tokyo, Japan. HPMA,14 4-cyanopentanoic acid dithiobenzoate15 were synthesized according to literature. N-Methacryloylglycylphenylalanylleucylglycyl-doxorubicin (MA-GFLG-DOX) was prepared by the reaction N-methacryloylglycylphenylalanylleucylglycine 4-nitrophenyl ester (MA-GFLG-ONp) with doxorubicin hydrochloride in DMF in the presence of diisopropylethylamine according to the described procedure.16
UV-vis spectra were measured on a Varian Cary 400 Bio UV-visible spectrophotometer. Mass spectra were measured on an FTMS mass spectrometer (LTQ-FT, ThermoElectron, Waltham, MA). ¹H-NMR spectra were recorded on a Mercury400 spectrometer using DMSO-d₆ as the solvent. Polymerization conversion was determined by the measurement of remaining HPMA monomer concentration at different time points using RP-HPLC (Agilent Technologies 1100 series, Zorbax C8 column 4.6×150 mm) with gradient elution from 2 to 90% of Buffer B within 30 min at flow rate of 1.0 mL/min (Buffer A: deionized water (DI H₂O) with 0.1% TFA, Buffer B: acetonitrile with 0.1% TFA). The molecular weight and polydispersity index (PDI) of polymers were measured on an ÄKTA FPLC (fast protein liquid chromatography) system (GE Healthcare, formerly Amersham) equipped with miniDAWN TREOS and OptilabEX detectors (Wyatt Technology, Santa Barbara, CA) using a Superose 6 or 12 HR10/30 column with PBS (pH 7.3) as the mobile phase. Narrow polydispersity polyHPMA fractions prepared by size exclusion chromatography, whose molecular weights were characterized by multiangle light scattering, were used as molecular weight standards. The multiblock polymers were fractionated on the same FPLC system using Superose 6 HR16/60 preparative column. PBS was used as the mobile phase. The flow rate was 1 mL/min. the fraction was collected every 10 min. The salt in the fractions was removed by dialysis. The narrow polydispersity polymer fractions were obtained after freeze-drying.

Pan H., Yang J., Kopečková P, & Kopeček J. (2010). Backbone Degradable Multiblock N-(2-Hydroxypropyl)methacrylamide Copolymer Conjugates via Reversible Addition Fragmentation Chain Transfer Polymerization and Thiol-ene Coupling Reaction. Biomacromolecules, 12(1), 247-252.

Publication 2010

1-hydroxybenzotriazole 1H NMR acetonitrile Acids Amino Acids Bos taurus Buffers Carica papaya Cathepsin B Dialysis Doxorubicin Duxon Esters Gel Chromatography High-Performance Liquid Chromatographies Hydrochloride, Doxorubicin hydroxypropyl methacrylate Latex Light Liquid Chromatography Mass Spectrometry Papain Polymerization Polymers Proteins Resins, Plant Sodium Chloride Solvents Spleen Sulfoxide, Dimethyl Trifluoroethanol trityl chloride

Cathepsin Protein Expression in Dupuytren's Disease

Cited 5 times

Total protein was extracted from snap-frozen samples of DD cords and nodules from 3 of the original cohort of 10 patients used for DAB IHC staining, by pestle homogenization (cat# PES-15-B-SI, Corning, N.Y.) in ice-cold Radioimmunoprecipitation assay buffer buffer (cat# R0278, Sigma-Aldrich, St. Louis, Mass.) supplemented with 1× HALT protease and phosphatase inhibitor cocktail (cat# 78440, Pierce Biotechnology, Rockford, Ill.) and 10 mM dithiothreitol (cat# 43816, Sigma-Aldrich). Soluble proteins were precipitated with ProteoExtract Protein Precipitation Kit (cat# 539180, Merck Millipore, Billerica, Mass.) and then resuspended at 70°C in Bolt 1× lithium dodecyl sulfate sample buffer (reduced sample) (cat# B0007, Thermo Fisher Scientific, Waltham, Mass.) at -20°C for 1 hour. Equal amounts of protein (~30 μg total protein per sample) were heated at 70^oC and resolved by 4–12% 1D-PAGE (cat# NW04120BOX, Thermo Fisher Scientific) and transferred to a polyvinylidene fluoride membrane (cat# IB24001, Invitrogen, Carlsbad, Calif.) using an iBlot 2 (cat# IB21001, Thermo Fisher Scientific). Blotted membranes were blocked using 10 mL of 1× iBind Flex FD solution (cat# SLF2019, Thermo Fisher Scientific) for 5 minutes at room temperature and probed using the iBind Flex device (cat# SLF2000, Thermo Fisher Scientific) for cathepsin B (1:250; cat# SC-6490-R, Santa Cruz), cathepsin D (1:250; cat# SC-6486, Santa Cruz), cathepsin G (1:250; cat# ab197354, Abcam, Cambridge, United Kingdom), and β-actin (1:500; cat# ab8226 and ab8229, Abcam). Appropriate secondary antibodies were goat anti- rabbit Alexa Fluor 647 (1:2000; cat# A21244, Life Technologies) for cathepsins B and D, chicken anti-goat Alexa Fluor 647 (1:2000; cat# A21469, Life Technologies) for β-actin ab8229, goat anti-mouse Alexa Fluor 488 (1:2000; cat# A21202, Life Technologies) for β-actin ab8226, and goat anti-rabbit horseradish peroxidase (1:2000; cat# ab6721, Abcam) for cathepsin G. Clarity Western ECL (cat# 1705061, Bio-Rad) was used as the substrate for visualizing horseradish peroxidase detected protein bands and the Chemi Doc MP Imaging System (Bio-Rad) and Image Lab 5.0 software (Bio-Rad) were used for band detection and analysis. All experiments were performed in triplicate. Snap-frozen tonsillar tissue was used as control tissue for cathepsin B^{27 (link)} and cathepsin D^{28 (link)} and a recombinant cathepsin G protein (cat# H00001511-Q01, Novus Biologicals, Littleton, Colo.) was used as an appropriate positive control. Matched mouse (1:500; cat# ab18443, Abcam) and rabbit (1:500; cat# ab171870, Abcam) isotype controls were used as appropriate negative controls.

Tan K., Brasch H.D., van Schaijik B., Armstrong J.R., Marsh R.W., Davis P.F., Tan S.T, & Itinteang T. (2018). Expression and Localization of Cathepsins B, D, and G in Dupuytren’s Disease. Plastic and Reconstructive Surgery Global Open, 6(2), e1686.

Publication 2018

Actins alexa fluor 488 Alexa Fluor 647 Antibodies Biological Factors Buffers Cathepsin B Cathepsin D Cathepsins Chickens Cold Temperature Cone-Rod Dystrophy 2 CTSB protein, human CTSG protein, human Dithiothreitol dodecyl sulfate, lithium salt Freezing Goat Horseradish Peroxidase Immunoglobulin Isotypes Medical Devices Mus Novus Palatine Tonsil Patients Peptide Hydrolases Phosphoric Monoester Hydrolases polyvinylidene fluoride Proteins Rabbits Radioimmunoprecipitation Assay Recombinant Proteins Tissue, Membrane Tissues

In Vivo Protease Activity Quantification Using NIR-Fluorescence

Cited 5 times

The early events of inflammation within the joints involving protease activity were quantified according to a previously established method using Near-Infrared (NIR)-fluorescence imaging (21 (link)). Briefly, 24 hours prior to the time of imaging, animals were administered an i.v. injection of the protease substrate, Prosense (2 nmol/150 μl volume; ViseEn Medical, Woburn, MA). Prosense is a NIR fluorescent protease substrate that is incorporated into bone tissue and allows us to specifically visualize ongoing in vivo protease activity of cathepsins B, C, D, G, K, L and S, plasmin, and plasma kallikrein. NIR-fluorescence scanning of dissected knees was performed at the time of sacrifice using the Licor-Odessey infrared imaging system with a MousePod attachment. Images were then analyzed using commercially available software (Licore-Odessey, Lincoln, NE) for regions of interest within each knee and the mean differences in fluorescent intensity were quantified. Data are represented as mean fold induction relative the saline controls, which were scanned and analyzed at the same time.

Rosenzweig H.L., Jann M.J., Vance E.E., Planck S.R., Rosenbaum J.T, & Davey M.P. (2010). NOD2 and TLR2 function independently in a murine model of arthritis triggered by intra-articular peptidoglycan. Arthritis and rheumatism, 62(4), 1051-1059.

Publication 2010

Animals Bone Tissue Cathepsin B Cathepsins endopeptidase B Endopeptidases Fluorescence Inflammation Joints Knee Knee Joint Plasma Kallikrein Plasmin protease V Saline Solution

Western Blot Analysis of Melanoma Proteins

Cited 4 times

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Publication 2011

bryostatin 1 Cathepsin B Cells Ethanol Melanoma MMP9 protein, human SDS-PAGE

Most recents protocols related to «Cathepsin B»

Cathepsin B Activity Assay with TCEP

A slightly modified protocol
from the commercially available assay (BPS Bioscience) was used. Dithiothreitol
was substituted with tris(2-carboxyethyl)phosphine (TCEP), the latter
of which was found not to alter the activity of the enzyme in the
assay. The cathepsin B enzyme was thawed on ice and activated by dilution
to 10.0 ng/μL with assay buffer. The enzyme solution was further
diluted with assay buffer to 0.02 ng/μL. Twenty microliters
of the enzyme solution was mixed with 5 μL of increasing concentrations
of the complex [2% (v/v) DMSO] diluted in assay buffer in the dark.
The mixture was incubated for 10 min at 37 °C with slow shaking.
The substrate (Z-Leu-Arg-AMC) was diluted to 10 μM, and 25 μL
was added to the enzyme mixture. This yields a mixture containing
10 mM Tris-HCl, 0.05% glycerol, 300 μM TCEP, and 10 μM
cathepsin B substrate. The mixture was incubated for 60 min at 37
°C with slow shaking. The generated fluorescence signal (λ_ex = 360 nm; λ_em = 460 nm) was recorded with
a Synergy H4 (BioTek) microplate reader. As a positive control, the
known inhibitor E-64 (IC₅₀ = 4 ± 2 nM) was used.

Karges J, & Cohen S.M. (2023). Rhenium(V) Complexes as Cysteine-Targeting Coordinate Covalent Warheads. Journal of Medicinal Chemistry, 66(4), 3088-3105.

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Publication 2023

arginine 4-methyl-7-coumarylamide Biological Assay Buffers Cathepsin B enzyme activity Enzymes Fluorescence Glycerin phosphine Sulfoxide, Dimethyl tris(2-carboxyethyl)phosphine Tromethamine

Engineered Salmonella Typhimurium Strains

The nirB and pagC promoters, as well as the SspH1 and Cathepsin B (codon-optimized for expression in S. Typhimurium) sequences, were utilized in this study^{8 (link),82 (link)}. The frr promoter was obtained from YS1646 S. Typhimurium by PCR. The pGP-Tn7-Cm plasmid backbone^{11 (link)} was digested using FastDigest restriction enzymes EcoRI and KpnI (Thermo Fisher Scientific). The promoter, secretory signal, and antigen sequences were inserted using the pEASY—Uni Seamless Cloning and Assembly kit (TransGen Biotech, Beijing, China). Following the construction of novel Tn7 plasmids, DAP⁻E. coli MGN-617 was transformed to generate 3 novel conjugative donor strains. The transformed E. coli strains were then used for conjugation experiments with a YS1646 strain containing the temperature-sensitive pSTNSK plasmid which encodes the Tn7 transposase system and confers Km resistance^{11 (link)}. Donor E. coli and recipient YS1646 were resuspended in LB supplemented with Km and DAP. About 100 μL of the donor strain and 50 μL of the recipient strain were centrifuged together and then resuspended in 10 μL at 30 °C for 5 h. Mixed culture was later grown on LB Km-Cm plates at 37 °C, and YS1646 colonies that grew in the absence of DAP, but that had lost resistance to antibiotic markers present on the pSTNSK plasmid but gained Cm resistance associated with the attTn7 targeting sequence were selected. Chromosomal integration at the attTn7 was then confirmed by PCR. The temperature-sensitive pCP20 plasmid, encoding the recombinase flippase (FLP) and conferring Amp and Cm resistance, was transformed into YS1646 strains. The Cm resistance cassette, integrated at the attTn7 site, was flanked by two FRT regions. Loss of the Cm resistance cassette is mediated by FLP-FRT recombination. Transformants were selected on LB-Amp plates at 30 °C to maintain pCP20 activity and then serially passaged on LB-Amp at 30 °C as well as LB-Cm and LB at 37 °C to screen for loss of the pCP20 plasmid and antibiotic susceptibility. Loss of Cm resistance was further confirmed by PCR. Following a similar strategy as outlined above, mCherry-expressing strains were generated for confocal microscopy experiments.

Hassan A.S., Houle S., Labrie L., Perera D.J., Dozois C.M., Ward B.J, & Ndao M. (2023). Salmonella Typhimurium expressing chromosomally integrated Schistosoma mansoni Cathepsin B protects against schistosomiasis in mice. NPJ Vaccines, 8, 27.

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Publication 2023

Antibiotic Resistance, Microbial Antibiotics Antigens Cathepsin B Chromosomes Codon Deoxyribonuclease EcoRI Escherichia coli Microscopy, Confocal Plasmids Recombinase Recombination, Genetic secretion Strains Susceptibility, Disease Tissue Donors Transposase

Multimodal Salmonella-based Vaccine for Schistosomiasis

Female 6–8-week-old C57BL/6 mice were immunized orally (PO) with recombinant S. enterica Typhimurium YS1646 derivative wherein the chromosomally integrated (CI) nirB promoter was used for expression and S. mansoni Cathepsin B that was secreted by fusion of CatB to an SspH1 Salmonella-specific type three secretory signal sequence (YS1646::NHC). This construct was selected for further in vivo investigation based on preliminary animal studies. PO dosing, consisting of 200 μL containing 1 × 10⁹ cfu/dose, was administered by oral gavage every other day for 3 days (D1, D3, and D5). The multimodal vaccination schedule also included a simultaneous intramuscular (IM) dose on D1 of 20 μg recombinant CatB (rCatB) in 50 μL PBS^{9 (link)} (Supplemental Fig. 1). Briefly, purified recombinant S. mansoni CatB was cloned and expressed in Pichia pastoris^{17 (link)}. All experiments included a PBS control group with IM-only (wild-type (WT) + rCatB) and PO-only (YS1646::NHC) groups as additional controls. The number of animals used at each experimental endpoint is indicated in the Figure legends.

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Publication 2023

Animals Cathepsin B Females Mice, Inbred C57BL Multimodal Imaging Pichia Salmonella secretion Signal Peptides Tube Feeding Vaccination

Protein Analysis of Snap-Frozen Kidneys

Snap-frozen kidneys were used for protein analysis. Tissue lysates were prepared in tissue protein extraction reagent (Thermo Fisher Scientific; Waltham, MA, USA) containing Halt protease and phosphatase inhibitors (Thermo Fisher Scientific) using an Omni TH homogenizer (Warrenton, VA, USA). The tissue lysates were centrifuged at 13,000 rpm at 4 °C for 30 min, and the supernatant was sonicated twice for 10 s intervals while on ice. Protein concentration was determined using a Bicinchoninic acid protein assay (Thermo Fisher Scientific). Fifty micrograms of protein were loaded onto 4–20% Tris·HCl polyacrylamide gels and resolved using the Criterion electrophoresis system (BioRad; Hercules, CA, USA). The resolved proteins were electrically transferred onto nitrocellulose blotting membranes (GE Healthcare, Piscataway, NJ, USA) using the Criterion transfer system (Bio-Rad). After blocking with 5% nonfat milk 1× Tris-buffered saline (1×TBS) (Bio-Rad), the membranes were incubated with primary antibodies (anti-ENaC alpha 59 antibody [25 (link)], cathepsin B antibody (Cell Signaling Tech, 3383), anti-HSP70 antibody (4872; Cell Signaling; Danvers, MA, USA), caveolin-1 antibody (3267; Cell Signaling), annexin A2 antibody (8235; Cell Signaling), and lamin A/C antibody (4777; Cell Signaling) at a dilution of 1:1,000 in BSA in 1× TBS (5% wt/vol) or actin HRP antibody (A3854; Sigma-Aldrich, St. Louis, MO, USA) at a dilution of 1:20,000 while on a rocker at 4°C overnight. The membranes were then incubated with horseradish peroxidase-conjugated goat anti-rabbit secondary antibody at a dilution of 1:3000 prepared in blocking solution while on a rocker at room temperature for 1 h. The membranes were developed with SuperSignal West Pico reagent (Thermo Scientific) for 5 min, and then imaged on a Bio-Rad imager.

Scindia Y.M., Gholam M.F., Waleed A., Liu L.P., Chacko K.M., Desai D., Lopez J.P., Malik Z., Schramm W.C., Morales A.G., Carson-Marino M, & Alli A.A. (2023). Metformin Alleviates Diabetes-Associated Hypertension by Attenuating the Renal Epithelial Sodium Channel. Biomedicines, 11(2), 305.

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Publication 2023

Actins Annexin A2 Antibodies Antibodies, Anti-Idiotypic bicinchoninic acid Biological Assay Cathepsin B Caveolin 1 Electricity Electrophoresis Epithelial Sodium Channel, alpha Subunit Freezing Goat Heat-Shock Proteins 70 Horseradish Peroxidase Immunoglobulins inhibitors Kidney LMNA protein, human Milk, Cow's Nitrocellulose Peptide Hydrolases Phosphoric Monoester Hydrolases polyacrylamide gels Proteins Rabbits Saline Solution Technique, Dilution Tissue, Membrane Tissues

Protein Expression Analysis in A253 Cells

A253 cells were lysed in RIPA Lysis and Extraction Buffer with protease and phosphatase inhibitors (all from Thermo Fisher Scientific) and cleared by centrifugation at 17,000 g at 4°C for 25 minutes. Supernatants were heated at 97°C in NuPAGE LDS Sample Buffer for 10 minutes, resolved by SDS-PAGE, and electrophoretically transferred to polyvinylidene difluoride membranes (all from Thermo Fisher Scientific). Membranes were blocked with 2% non-fat dried milk at 25°C for 1 hour, and then incubated at 4°C overnight with one of the following primary antibodies: anti-cathepsin B (#AF953, R&D system, USA), anti-LAMP1 (#21997-1-AP, Proteintech, USA) or anti-α-tubulin (#T6199, Sigma-Aldrich, USA). After washing three times, membranes were incubated with rabbit or mouse IgG horseradish peroxidase-linked whole antibody (Sigma-Aldrich) at 25°C for 1 hour. Signals were visualized using Super Signal West Pico Chemiluminescent Substrate or Super Signal West Pico PLUS Chemiluminescent Substrate (both from Thermo Fisher Scientific).

Nakamura H., Tanaka T., Ji Y., Zheng C., Afione S.A., Warner B.M., Oliveira F.R., Motta A.C., Rocha E.M., Noguchi M., Atsumi T, & Chiorini J.A. (2023). Salivary gland LAMP3 mRNA expression is a possible predictive marker in the response to hydroxychloroquine in Sjögren’s disease. PLOS ONE, 18(2), e0282227.

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Publication 2023

alpha-Tubulin Antibodies Buffers Cathepsin B Cells Centrifugation IGG-horseradish peroxidase Immunoglobulins inhibitors lysosomal-associated membrane protein 1, human Milk, Cow's Mus Peptide Hydrolases Phosphoric Monoester Hydrolases polyvinylidene fluoride Rabbits Radioimmunoprecipitation Assay SDS-PAGE Tissue, Membrane

Top products related to «Cathepsin B»

Cathepsin b by Merck Group

Sourced in United States, United Kingdom

Cathepsin B is a laboratory equipment product manufactured by Merck Group. It is a proteolytic enzyme that plays a role in various cellular processes. The core function of Cathepsin B is to cleave peptide bonds within proteins.

Ca 074 me by Merck Group

Sourced in United States

CA-074 Me is a laboratory reagent produced by Merck Group. It is a cathepsin B inhibitor with a core function of inhibiting the enzymatic activity of cathepsin B. No further details on intended use are provided.

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.

Bafilomycin a1 by Merck Group

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

Bafilomycin A1 is a macrolide compound that acts as a potent and specific inhibitor of vacuolar-type H+-ATPases (V-ATPases). V-ATPases are involved in the acidification of various intracellular compartments, making Bafilomycin A1 a useful tool for studying cellular processes that rely on pH regulation.

Lysotracker red dnd 99 by Thermo Fisher Scientific

Sourced in United States, United Kingdom, Germany, Japan, France, China, Spain

LysoTracker Red DND-99 is a fluorescent dye that selectively stains acidic organelles, such as lysosomes, in live cells. It can be used to visualize and monitor the distribution and activity of lysosomes within the cellular environment.

Cathepsin b by Santa Cruz Biotechnology

Sourced in United States

Cathepsin B is a lysosomal cysteine protease enzyme involved in the degradation of proteins. It plays a role in various physiological and pathological processes.

Hoechst 33342 by Thermo Fisher Scientific

Sourced in United States, Germany, United Kingdom, Japan, China, France, Canada, Spain, Belgium, Italy, Australia, Austria, Denmark, Netherlands, Switzerland, Ireland, New Zealand, Portugal, Brazil, Argentina, Singapore, Poland, Ukraine, Macao, Thailand, Finland, Lithuania, Sweden

Hoechst 33342 is a fluorescent dye that binds to DNA. It is commonly used in various applications, such as cell staining and flow cytometry, to identify and analyze cell populations.

Dimethyl sulfoxide (dmso) by Merck Group

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DMSO is a versatile organic solvent commonly used in laboratory settings. It has a high boiling point, low viscosity, and the ability to dissolve a wide range of polar and non-polar compounds. DMSO's core function is as a solvent, allowing for the effective dissolution and handling of various chemical substances during research and experimentation.

Ca 074 by Merck Group

Sourced in Germany

CA-074 is a laboratory equipment product manufactured by Merck Group. It is a cathepsin B inhibitor used for research purposes. The core function of CA-074 is to inhibit the enzymatic activity of cathepsin B, a cysteine protease enzyme.

Chloroquine by Merck Group

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

Chloroquine is a laboratory chemical primarily used as a research tool in biochemical and cell biology applications. It is a white, crystalline solid that is soluble in water. Chloroquine is commonly used in experiments to study cellular processes, such as autophagy and endocytosis, by inhibiting the function of lysosomes. Its core function is to serve as a research reagent for scientific investigations, without making any claims about its intended use.

What is Cathepsin B and what are its key functions?

How can PubCompare.ai help with Cathepsin B research?

PubCompare.ai allows you to screen protocol literature more efficiently and leverage AI to pinpoint critical insights. The platform can help researchers identify the most effective protocols related to Cathespin B for their 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.

What are some common usage challenges with Cathepsin B?

One of the main challenges with Cathepsin B research is ensuring optimal experimental conditions and reproducibility across different studies. Researchers may struggle to identify the most reliable protocols from the vast amount of literature, preprints, and patents available. Tyical usage issues can include variability in enzyme activity, substrate specificity, and inhibitor effectiveness, which can impact the validity and comparability of research findings.

Are there different variations or types of Cathepsin B?

Yes, there are several different forms or isoforms of Cathepsin B that can exhibit varying catalytic properties and biological functions. These include secreted, membrane-bound, and intracellular forms of the enzyme. Researchers need to carefully select the appropriate Cathepsin B variant based on their specific research objectives and experimental model to ensure meaningful and reproducible results.

More about "Cathepsin B"

Cathepsin B, a vital lysosomal cysteine protease, plays a crucial role in protein degradation and turnover.
This versatile enzyme is involved in a wide array of physiological and pathological processes, including inflammation, cancer, and neurodegeneration.
As a valuable target for research and therapeutic development, Cathepsin B has garnered significant attention from the scientific community.
Exploring the various aspects of Cathepsin B can provide valuable insights.
CA-074 Me, a specific inhibitor of Cathepsin B, is often utilized in research to study the enzyme's function and its involvement in different cellular processes.
Furthermore, FBS (Fetal Bovine Serum) and Bafilomycin A1, a vacuolar-type H+-ATPase inhibitor, are commonly employed in Cathepsin B-related experiments to understand its regulation and localization within cells.
LysoTracker Red DND-99, a fluorescent dye, and Hoechst 33342, a nuclear stain, are frequently used in combination to visualize and analyze Cathepsin B activity and lysosomal dynamics.
DMSO (Dimethyl Sulfoxide) is another commonly used reagent in Cathepsin B research, serving as a solvent for various compounds.
Additionally, CA-074, another Cathepsin B inhibitor, and Chloroquine, a lysosomotropic agent, can provide further insights into the enzyme's role and regulation.
By leveraging the knowledge and tools available, researchers can delve deeper into the complexities of Cathepsin B and its significance in various biological processes.
PubCompare.ai's AI-driven platform can be a valuable resource, helping to identify the most reliable protocols and optimize research methods to enhance reproducibility and accuracy in Cathepsin B studies.