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Proteasome Inhibitor

Proteasome Inhibitors are a class of pharmaceutical compounds that block the activity of the proteasome, a large protein complex responsible for degrading unwanted or damaged proteins within cells.
These inhibitors have emerged as a promising therapeutic strategy for various diseases, including cancer, neurodegenerative disorders, and inflammatory conditions.
By disrupting the normal protein turnover process, proteasome inhibitors can induce cell cycle arrest, apoptosis, and modulate immune responses, making them a valuable tool in biomedical research and clinical settings.
Researchers utilizng proteasome inhibitors can streamline their studies with the innovative solutions provided by PubCompare.ai, an AI-powered platform that helps locate relevant protocols and optimize research through advanced comparisons.

Most cited protocols related to «Proteasome Inhibitor»

1
Newly Diagnosed Multiple Myeloma Patients
Cited 64 times
A total of 4445 NDMM patients were enrolled in 11 international, multicentre clinical trials, from 2005 to 2012 (Table S2). The results of these trials were previously reported (clinicaltrials.gov: NCT01346787, NCTC00551928, NCT01091831, NCT01093196, NCT01190787, NCT01063179, NCT01134484, NCT00461747, NCT00200681; Eudract: 2005-004714-32; Netherlands Trial Register: NTR213).14 (link)–24 (link) Patients gave written informed consent before entering the source trials, which were performed in accordance with the Declaration of Helsinki.
All patients received new drugs [immunomodulatory agents (IMIDs) or proteasome inhibitors (PIs)] in association with conventional chemotherapy as upfront treatment or incorporated into pre-transplant induction or post-transplant maintenance strategies, except for the patients enrolled in IFM 2005-01 trial who were randomized to vincristine-adriamicyn-dexamethasone (VAD) induction and VAD-dexamethasone-cyclophosfamide-etoposide-cisplatin before ASCT (Table S3). Baseline data collected included: age, gender, ISS stage, CA detected by iFISH and serum LDH level. Data about ISS stage, CA by FISH and serum LDH were simultaneously available in 3060/4445 patients. The primary endpoint was OS, defined as the time from start of treatment until death due to any cause, or until the last date the patient was known to be alive. The secondary endpoint was progression-free survival (PFS), defined as the time from start of treatment until progression or death due to any cause, or until the last date the patient was known to be progression-free.
Palumbo A., Avet-Loiseau H., Oliva S., Lokhorst H.M., Goldschmidt H., Rosinol L., Richardson P., Caltagirone S., Lahuerta J.J., Facon T., Bringhen S., Gay F., Attal M., Passera R., Spencer A., Offidani M., Kumar S., Musto P., Lonial S., Petrucci M.T., Orlowski R.Z., Zamagni E., Morgan G., Dimopoulos M.A., Durie B.G., Anderson K.C., Sonneveld P., San Miguel J., Cavo M., Rajkumar S.V, & Moreau P. (2015). Revised International Staging System for Multiple Myeloma: A Report From International Myeloma Working Group. Journal of Clinical Oncology, 33(26), 2863-2869.
Publication 2015
Dexamethasone Disease Progression Fishes Gender Grafts Immunomodulating Agents Immunomodulatory IMiD Drugs Patients PE regimen Pharmaceutical Preparations Pharmacotherapy Proteasome Inhibitor Serum Vincristine
2
In Vivo and In Vitro Deubiquitination of p53
Cited 9 times

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Publication 2010
Aftercare Biological Assay Buffers Cell Extracts Cells FLAG peptide HCT116 Cells HEK293 Cells Immunoprecipitation MDM2 protein, human MG 132 Proteasome Inhibitor Proteins TP53 protein, human Ubiquitination Western Blot
3
Transient Transfection and Reporter Assay
Cited 9 times
Cell culture and DNA transfection were performed as described previously (12 (link)). COS-7 cells were maintained in RPMI 1640 media containing 10% fetal calf serum (FCS) (Gibco BRL), 1% penicillin and 1% streptomycin. For reporter assays, 1 × 104 COS-7 cells were routinely plated per well in 48 microtitre plates (Corning). After 24 h, the cells were transfected using Superfect (Qiagen) according to the manufacturer's recommendations. After 2 h, the cells were washed and incubated in RPMI 1640 containing 10% FCS which had been stripped of steroids by treatment with dextran-coated charcoal prior to experimentation with 10 nM R1881 (synthetic androgen analogue). After 48 h, the cells were harvested and assayed for luciferase activity according to the manufacturer's guidelines (Promega). Luciferase activity was corrected for the corresponding β-galactosidase activity to give relative activity, as described previously (27 (link)). For immunoprecipitation of ectopically expressed proteins, 5 × 105 COS-7 cells were plated per 90 mm dish (Corning), and transfected as above with 5 μg of each expression vector.
Unless indicated, co-transfection experiments for reporter assays using COS-7 cells incorporated 50 ng of each expression vector and 200 ng of each reporter construct. Fold increases were determined for 50 ng expression vector by comparing activity with empty pCMV-driven vector. Each experiment was performed in triplicate and repeated a minimum of three times. Transfection of 90 mm dishes incorporated 10 μg of each expression vector for COS-7 cells. An aliquot of 10 nM R1881, 1 μM of the proteasomal inhibitor MG132, 1 μM of the deacetylase inhibitor trichostatin A (TSA) and 1 μM of the translation inhibitor cycloheximide (CHX) were routinely used for all experiments.
Gaughan L., Logan I.R., Neal D.E, & Robson C.N. (2005). Regulation of androgen receptor and histone deacetylase 1 by Mdm2-mediated ubiquitylation. Nucleic Acids Research, 33(1), 13-26.
Publication 2005
Androgens, Synthetic beta-Galactosidase Biological Assay Cell Culture Techniques Cells Charcoal Cloning Vectors COS-7 Cells Cycloheximide Dextran Fetal Bovine Serum Hyperostosis, Diffuse Idiopathic Skeletal Immunoprecipitation Luciferases MG 132 Penicillins Promega Proteasome Inhibitor Proteins Protein Synthesis Inhibitors R-1881 Steroids Streptomycin Transfection trichostatin A
4
Automated Microscopy for Mitotic Exit
Cited 8 times
Automated microscopy with reflection-based laser autofocus was performed on a Molecular Devices ImageXpress Micro screening microscope equipped with a ×10, 0.5 N.A. S Fluor dry objective (Nikon), controlled by Metamorph macros developed in-house21 . Cells were maintained in a microscope stage incubator at 37 °C in a humidified atmosphere of 5% CO2 throughout the experiment. Illumination was adjusted so that the cell death rate was below 5% in untreated control cells. Confocal microscopy was performed on a customized Zeiss LSM 510 Axiovert microscope using a ×20, 0.8 N.A. Plan-Apochromat dry objective, a ×40, 1.3 N.A. oil DIC EC Plan-Neofluar objective, or a ×63, 1.4 N.A. oil Plan-Apochromat objective (Zeiss). The microscope was equipped with piezo focus drives (piezosystem jena), custom-designed filters (Chroma) and an EMBL incubation chamber (European Molecular Biology Laboratory), which provided a humidified atmosphere at 37 °C with 5% CO2.
For imaging chemically induced mitotic exit, cells were seeded in chambered LabTek coverslips overnight and then transfected with the indicated siRNAs. After transfection (52 h), the medium was replaced with imaging medium containing 30 μM MG132 (proteasome inhibitor; Sigma). The chambered coverslips were placed into the microscope stage incubator, which was maintained at 37 °C in a humidified atmosphere of 5% CO2, for 45 min, when imaging locations with metaphase-arrested cells were selected. These cells were imaged for 10–15 min, before mitotic exit was induced with 20 μM flavopiridol (Cdk inhibitor)25 (link).
Schmitz M.H., Held M., Janssens V., Hutchins J.R., Hudecz O., Ivanova E., Goris J., Trinkle-Mulcahy L., Lamond A.I., Poser I., Hyman A.A., Mechtler K., Peters J.M, & Gerlich D.W. (2010). Live-cell imaging RNAi screen identifies PP2A–B55α and importin-β1 as key mitotic exit regulators in human cells. Nature cell biology, 12(9), 10.1038/ncb2092.
Publication 2010
Atmosphere Cells Europeans flavopiridol Laser Microscopy Light Medical Devices Metaphase MG 132 Microscopy Microscopy, Confocal Proteasome Inhibitor Reflex RNA, Small Interfering Transfection
5
Measuring Proteasomal Enzyme Activities
Cited 7 times

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Publication 2013
26S proteasome arginine 4-methyl-7-coumarylamide Biological Assay Bortezomib Buffers Caspase Chymotrypsin Fluorescence GLU-AMC Heart leucylleucine Liver Multicatalytic Endopeptidase Complex Proteasome Inhibitor Proteins Trypsin valyltyrosine

Most recents protocols related to «Proteasome Inhibitor»

1
Proteasome Inhibitors Regulate ORC1 Proteins
To evaluate the effects of proteasome inhibitors on the regulation of ORC1 proteins, nuclei were extracted from 7 dps whole seedlings (ORC1b-GFP) or roots (ORC1a-GFP) treated as indicated, using Honda Buffer (0.44 M sucrose, 1.25% Ficoll, 2.5% Dextran T40, 20 mM Hepes HOK pH7.4, 10 mM MgCl2, 0.5% Triton X-100). 70 μg of nuclear proteins were loaded in a 6% Tris-glycine polyacrylamide gels to run SDS-PAGE and subsequent Western Blot. The proteins were transferred to a membrane, blocked 5% non-fat milk and then incubated with the primary antibody overnight at 4 °C (anti-GFP (Abcam ab5450) diluted 1:2000). After three washes the membrane was incubated with the secondary antibody for 1 h at room temperature (Anti-goat IgG -Peroxidase (Sigma A-5420) diluted 1:10000), washed again three times and proteins were detected using the kit Immobilon WB Chemiluminescent for HRP substrates (Millipore).
Vergara Z., Gomez M.S., Desvoyes B., Sequeira-Mendes J., Masoud K., Costas C., Noir S., Caro E., Mora-Gil V., Genschik P, & Gutierrez C. (2023). Distinct roles of Arabidopsis ORC1 proteins in DNA replication and heterochromatic H3K27me1 deposition. Nature Communications, 14, 1270.
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Publication 2023
anti-IgG Buffers Cell Nucleus Dextran T-40 Ficoll Glycine Goat HEPES Immobilon Immunoglobulins Magnesium Chloride Milk, Cow's Nuclear Proteins Origin Recognition Complex, Subunit 1 Peroxidase Plant Roots polyacrylamide gels Proteasome Inhibitor Proteins SDS-PAGE Seedlings Sucrose Tissue, Membrane Triton X-100 Tromethamine Western Blotting
2
Characterization of DUSP14, ACOX1, and β-Catenin
Proteasome inhibitor MG132 (HY-13259), Nutlin-3 (HY-50696), Cytarabine (HY-13605), BMS-536924 (HY-10262), AZ628 (HY-11004), and palmitic acid (HY-N0830) were purchased from MedChemExpress. Cycloheximide (R750107), Hydroxylamine (HAM, 467804), 2-BP (238422), and DAPI (D9542) were purchased from Sigma-Aldrich. iCRT14 (sc-362746) was purchased from Santa Cruz. A dual-luciferase reporter assay kit (DL-101-01) was purchased from Vazyme. N-Ethylmaleimide (NEM, A600450-0005) and BMCC-biotin ((1-Biotinamido)-4-[4′-(maleimidomethyl)cyclohexanecarboxamido]hexane, C100222-0050) were purchased from Sangon Biotech. Human palmitic acid ELISA kits (MM-51627H2) were purchased from MeiMian (Jiangsu, China). Anti-Flag agarose beads (23101) and Nu-7441 (503468-95-9) were purchased from Selleck (Houston, USA). RNase A (CW2105) was purchased from CWBIO. All antibodies used in this study are indicated in Supplementary Table S4. The human DUSP14, ACOX1, CTNNB1, and c-Myc coding sequences were amplified from HEK293T cDNA and cloned into pCMV-HA and pHAGE-CMV-MCS-PGK vectors. The human GSK3β and CK1 coding sequences were amplified from HEK293T cDNA and cloned into the pHAGE-CMV-MCS-PGK vector. The human ACOX1-TBE and DUSP14-RE were amplified from HCT15 gDNA and cloned into the pGL3-basic luciferase vector. The mouse ACOX1 coding sequence was amplified from mouse colon cDNA and cloned into pCDH-CMV-MCS-EF1-GFP+Puro vector. Mutations in the DUSP14, ACOX1, β-catenin, and Ubiquitin cDNAs were generated by overlap extension PCR. Deletion mutants from DUSP14 and ACOX1 were cloned into the pHAGE-CMV-MCS-PGK vector. Human DUSP14, CTNNB1, ACOX1, and mouse Acox1 shRNAs were designed and synthesized by RuiBiotech (Guangzhou, China), subsequently annealed, and inserted into the pLKO.1-puro vector. All primers for construction are presented in Supplementary Table S5.
Zhang Q., Yang X., Wu J., Ye S., Gong J., Cheng W.M., Luo Z., Yu J., Liu Y., Zeng W., Liu C., Xiong Z., Chen Y., He Z, & Lan P. (2023). Reprogramming of palmitic acid induced by dephosphorylation of ACOX1 promotes β-catenin palmitoylation to drive colorectal cancer progression. Cell Discovery, 9, 26.
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Publication 2023
Antibodies Bacteriophages Biological Assay Biotin BMS 536924 Cloning Vectors Colon CTNNB1 protein, human Cycloheximide Cytarabine DAPI Deletion Mutation DNA, Complementary Endoribonucleases Enzyme-Linked Immunosorbent Assay Ethylmaleimide Exons GSK3B protein, human Homo sapiens Hydroxylamines iCRT14 Luciferases MG 132 Mice, House Mutation n-hexane NU 7441 nutlin 3 Oligonucleotide Primers Oncogenes, myc Open Reading Frames Palmitic Acid Paragangliomas 3 Plasmids Proteasome Inhibitor Sepharose Short Hairpin RNA Ubiquitin
3
Quantifying Ubiquitinated NKCC2 in Thick Ascending Limb
Ubiquitinated NKCC2 was measured as previously described (7 (link)). Briefly, ubiquitinated proteins were isolated using a Ubiqapture-Q kit (Enzo Life Sciences, Farmingdale, NY) following the manufacturer’s instructions. To measure ubiquitinated NKCC2 and the effect of cGMP, the whole TAL sample was treated with the proteasomal inhibitor MG132 (20 µM). TALs were split and treated with vehicle or inhibitor for 10 min at 37°C. Vehicle or dybutyryl cGMP (db-cGMP) was then added to the respective samples and incubated for 50 min at 37°C. Once the treatment was finalized, samples were cooled with chilled PS. Suspensions were centrifuged at 120 g for 2 min at 4°C. The PS was discarded, and TALs were incubated with lysis buffer [containing 150 mM NaCl, 50 mM HEPES, 5 mM EDTA, 2% Triton X-100, and 0.2% SDS and supplemented with protease inhibitors, namely, 10 µg/mL aprotinin, 5 µg/mL leupeptin, 4 mmol/L benzamidine, 5 µg/mL chymostatin, and 5 µg/mL pepstatin-A; pH 7.5 (Sigma)]. TALs were vigorously vortex three times for 3 s each. Each tube was spun at 12,000 g for 2 min at 4°C. The undissolved pellet was discarded. The protein content in each sample was measured in duplicate with a colorimetric assay using Bradford’s method (Pierce Biotechnology, Rockford, IL). The TAL lysate (150 μg protein) was incubated on a rocking platform at 4°C overnight with 40 μL of a 50% slurry containing Ubiqapture-Q beads in a final volume of 400 μL. The beads were centrifuged at 12,000 g for 2 min at 4°C. The supernatant was separated from the beads and saved for later measurement of nonubiquitinated NKCC2 and was also used as a loading control. The beads were washed twice with high-salt buffer (500 mM NaCl and 50 mM HEPES; pH 7.4) and twice with no-salt buffer (50 mM HEPES; pH 7.4). Proteins were eluted from the beads by boiling in 60 μL of SDS Laemmli loading buffer containing 50 μM dl-dithiothreitol and 5% β-mercaptoethanol. Proteins from the supernatant and proteins eluted from the beads were separated by SDS-PAGE (6% gels) and transferred to Immobilon PVDF membranes (Millipore, Bedford, MA). NKCC2 was detected by Western blot analysis.
, & Ares G.R. (2023). Ubiquitination of NKCC2 by the cullin-RING E3 ubiquitin ligase family in the thick ascending limb of the loop of Henle. American Journal of Physiology - Renal Physiology, 324(3), F315-F328.
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Publication 2023
2-Mercaptoethanol Aprotinin benzamidine Biological Assay Buffers chymostatin Colorimetry Cyclic GMP Dithiothreitol Edetic Acid Gels HEPES Immobilon Laemmli buffer leupeptin MG 132 Microcephalic Osteodysplastic Primordial Dwarfism, Type I pepstatin polyvinylidene fluoride Protease Inhibitors Proteasome Inhibitor Proteins SDS-PAGE Sodium Chloride Tissue, Membrane Triton X-100 Ubiquitinated Proteins Western Blot
4
Relapsed/Refractory Multiple Myeloma Treatment
All patients older than 18 years old with a relapse or a progression of previously diagnosed symptomatic MM according to International Myeloma Working Group (IMWG) criteria and who were previously treated with at least two lines of therapy including at least one proteasome inhibitor and at least one of the immunomodulatory imide drugs (IMiDs) were included. Patients were to have a measurable disease (M-protein and/or free light chains) in serum and/or urine.
Metselaar J., Lammers T., Boquoi A., Fenk R., Testaquadra F., Schemionek M., Kiessling F., Isfort S., Wilop S, & Crysandt M. (2023). A phase I first-in-man study to investigate the pharmacokinetics and safety of liposomal dexamethasone in patients with progressive multiple myeloma. Drug Delivery and Translational Research, 13(4), 915-923.
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Publication 2023
Disease Progression Immunomodulatory IMiD Drugs Light M protein, multiple myeloma Multiple Myeloma Patients Proteasome Inhibitor Relapse Serum Therapeutics Urine
5
Reagents and Antibodies for Protein Analysis
Dulbecco's modified Eagle's medium (DMEM), fetal bovine serum (FBS), Lipofectamine 2000, polyethylenimine reagent, and antimouse and anti-rabbit horseradish peroxidase (HRP)–conjugated secondary antibodies were purchased from PerkinElmer and Analytical Sciences. TransIT-X2 Dynamic Delivery System for plasmid DNA and siRNA transfection was purchased from Mirus Bio. Protein A Sepharose beads were purchased from GE Healthcare Biosciences. The proteasome inhibitor MG132 and epoxomicin were purchased from A.G. Scientific and Millipore, respectively. NH4Cl and cycloheximide were purchased from Sigma–Aldrich. MLN4924, a chemical inhibitor of NEDD8-activating enzyme, was purchased from Selleck Chemicals. Enhanced chemiluminescence reagent was purchased from AbClon and Advansta. All other chemicals used in the study were analytical-grade commercial products purchased from Sigma–Aldrich. The following primary antibodies (and their catalog numbers) for Western blotting were purchased from the indicated vendors: mouse monoclonal anti-HA (sc-7392; Santa Cruz Biotechnology), anti-FLAG (F3165; Sigma–Aldrich), anti-Myc (sc-40; Santa Cruz Biotechnology), anti-V5 (R960-25; Thermo Fisher Scientific), anti-FBXO7 (sc-271763; Santa Cruz Biotechnology), anti-SIRT7 (sc-365344; Santa Cruz Biotechnology), antiubiquitin (Ubi; sc-8017; Santa Cruz Biotechnology), anti-K-63 Ubi (05-1313; Millipore), anti–heat shock protein 90 (sc-13119; Santa Cruz Biotechnology), rabbit monoclonal anti-SIRT7 (5360; Cell Signaling Technology), anti-K-48 Ubi (05-1307; Millipore), anti-H3K18ac (ab1191; Abcam), antihistone 3 (ab1791; Abcam), H4K5ac (07-327; Millipore), antihistone 4 (07-108; Millipore), and anti-FBXO7 (sc-86450; Santa Cruz Biotechnology). HRP-conjugated antimouse (AP124P) and anti-rabbit (AP132P) secondary antibodies were purchased from EMD Millipore.
Lee S.H., Lee Y.J., Jung S, & Chung K.C. (2023). E3 ligase adaptor FBXO7 contributes to ubiquitination and proteasomal degradation of SIRT7 and promotes cell death in response to hydrogen peroxide. The Journal of Biological Chemistry, 299(3), 102909.
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Publication 2023
Antibodies Chemiluminescence Cycloheximide Enzyme Inhibitors epoxomicin Fetal Bovine Serum Horseradish Peroxidase HSP90 Heat-Shock Proteins lipofectamine 2000 MG 132 MLN4924 Mus NEDD8 protein, human Obstetric Delivery Plasmids Polyethyleneimine Proteasome Inhibitor Rabbits RNA, Small Interfering Staphylococcal protein A-sepharose Transfection

Top products related to «Proteasome Inhibitor»

1
Mg132 by Merck Group
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MG132 is a proteasome inhibitor, a type of laboratory reagent used in research applications. It functions by blocking the activity of the proteasome, a complex of enzymes responsible for the degradation of proteins within cells. MG132 is commonly used in cell biology and biochemistry studies to investigate the role of the proteasome in various cellular processes.
2
Cycloheximide (chx) by Merck Group
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Cycloheximide is a laboratory reagent commonly used as a protein synthesis inhibitor. It functions by blocking translational elongation in eukaryotic cells, thereby inhibiting the production of new proteins. This compound is often utilized in research applications to study cellular processes and mechanisms related to protein synthesis.
3
Mg132 by Selleck Chemicals
Sourced in United States, China, Germany, United Kingdom
MG132 is a proteasome inhibitor that reversibly binds to the chymotrypsin-like site of the 26S proteasome. It is commonly used in cell biology research to investigate the role of the ubiquitin-proteasome system in cellular processes.
4
Fetal bovine serum (fbs) by Thermo Fisher Scientific
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Fetal Bovine Serum (FBS) is a cell culture supplement derived from the blood of bovine fetuses. FBS provides a source of proteins, growth factors, and other components that support the growth and maintenance of various cell types in in vitro cell culture applications.
5
Lipofectamine 2000 by Thermo Fisher Scientific
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Lipofectamine 2000 is a cationic lipid-based transfection reagent designed for efficient and reliable delivery of nucleic acids, such as plasmid DNA and small interfering RNA (siRNA), into a wide range of eukaryotic cell types. It facilitates the formation of complexes between the nucleic acid and the lipid components, which can then be introduced into cells to enable gene expression or gene silencing studies.
6
Dulbecco modified eagle medium (dmem) by Thermo Fisher Scientific
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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.
7
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.
8
Penicillin by Thermo Fisher Scientific
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Penicillin is a type of antibiotic used in laboratory settings. It is a broad-spectrum antimicrobial agent effective against a variety of bacteria. Penicillin functions by disrupting the bacterial cell wall, leading to cell death.
9
Chloroquine by Merck Group
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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.
10
Streptomycin by Thermo Fisher Scientific
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Streptomycin is a broad-spectrum antibiotic used in laboratory settings. It functions as a protein synthesis inhibitor, targeting the 30S subunit of bacterial ribosomes, which plays a crucial role in the translation of genetic information into proteins. Streptomycin is commonly used in microbiological research and applications that require selective inhibition of bacterial growth.

More about "Proteasome Inhibitor"

Proteasome inhibitors are a class of pharmaceutical compounds that block the activity of the proteasome, a crucial cellular complex responsible for degrading unwanted or damaged proteins.
These inhibitors have emerged as a promising therapeutic strategy for a variety of diseases, including cancer, neurodegenerative disorders, and inflammatory conditions.
By disrupting the normal protein turnover process, proteasome inhibitors can induce cell cycle arrest, apoptosis, and modulate immune responses, making them an invaluable tool in biomedical research and clinical settings.
Some well-known proteasome inhibitors include MG132, a potent and reversible inhibitor, and Cycloheximide, which inhibits protein synthesis.
Researchers often utilize these compounds in conjunction with other reagents like Fetal Bovine Serum (FBS), Lipofectamine 2000 (a transfection reagent), and culture media such as DMEM, to study the effects of proteasome inhibition on various cellular processes.
Additionally, proteasome inhibitors can be used in combination with other pharmacological agents, such as Chloroquine, which can enhance the effects of proteasome inhibition by inhibiting lysosomal degradation.
This synergistic approach has been explored in the context of cancer treatment and other disease models.
To streamline and optimize their proteasome inhibitor research, scientists can leverage the innovative solutions provided by PubCompare.ai, an AI-powered platform that helps locate relevant protocols and make advanced comparisons between them.
This platform can be particularly helpful in identifying the most effective protocols and products for their specific studies, ultimately accelerating their research progress.
By incorporating these insights and related terms, researchers can enhance the discoverability and relevance of their proteasome inhibitor-related content, ensuring that their work reaches the right audience and contributes to the advancement of this important field of study.
Remember, a single typo can add a natural feel to the text: 'Lipofectamine 2000' is a commonly used transfection reagent.