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> Chemicals & Drugs > Inorganic Chemical > Orthovanadate

Orthovanadate

Orthovanadate is a chemical compound with the formula VO4^3-.
It is the conjugate base of orthovanadic acid and is commonly used in biochemical and materials science research.
Orthovanadate plays a crucial role in the study of protein tyrosine phosphatases, serving as a potent and specific inhibitor.
Additionally, orthovanadate is an important precursor in the synthesis of vanadium-based materials with applications in catalysis, energy storage, and electronichs.
This MeSH term provideds a concise overview of the key properties and uses of orthovanadate, a versatile compound of interest across multiple scientific disciplines.

Most cited protocols related to «Orthovanadate»

1
Gelatin Zymography for Cathepsin Activity

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Publication 2011
Acetic Acid Biological Assay Bromphenol Blue Buffers Cathepsins Cells Centrifugation Coomassie blue Edetic Acid Egtazic Acid Elastin Electrophoresis Enzymes Gelatins Gels Glycerin Glycerophosphates Homo sapiens Isopropyl Alcohol leupeptin Orthovanadate polyacrylamide gels Proteins Sodium Sodium Acetate Sodium Chloride sodium phosphate Stains Tissues Triton X-100 Tromethamine Tween 20
2
LPS-Induced NLRP3 Inflammasome Activation
BMDM were seeded at 106/ml in 6 well plates. The following day medium was replaced and cells were stimulated with 10 ng/ml LPS for 3 h. Medium was removed and replaced with SFM containing the indicated inhibitors or controls for 30 min, followed by the addition of 10 µM nigericin for 1 h. The supernatants were removed, cells were rinsed in ice-cold PBS and 500 µl ice-cold buffer (20 mM Hepes-KOH, pH 7.5, 150 mM KCL, 1%NP-40 0.1 mM PMSF, 1 mg/ml leupeptin, 11.5 mg/ml aprotinin and 1 mM sodium orthovanadate) was added. Cells were scraped and lysed by shearing 10 ィ through a 21 gauge needle. 50 µl of lysate was removed for Western blot analysis. Lysates were centrifuged at 330 × g for 10 min at 4 °C. The pellets were washed twice in 1 ml ice-cold PBS and resuspended in 500 µl PBS. 2 mM disuccinimydyl suberate (from a fresh 100 mM stock prepared from DSS equilibrated to RT and made up in dry DMSO) was added to the re-suspended pellets, which were incubated at RT for 30 min with rotation. Samples were then centrifuged at 330 × g for 10 min at 4 °C. The supernatant was removed and the cross-linked pellets were resuspended in 30 µl Laemmli sample buffer. Samples were boiled for 5 min at 99 °C and analysed by Western blotting.
Coll R.C., Robertson A.A., Chae J.J., Higgins S.C., Muñoz-Planillo R., Inserra M.C., Vetter I., Dungan L.S., Monks B.G., Stutz A., Croker D.E., Butler M.S., Haneklaus M., Sutton C.E., Núñez G., Latz E., Kastner D.L., Mills K.H., Masters S.L., Schroder K., Cooper M.A, & O’Neill L.A. (2015). A small molecule inhibitior of the NLRP3 inflammasome is a potential therapeutic for inflammatory diseases. Nature medicine, 21(3), 248-255.
Publication 2015
Aprotinin Buffers Cells Common Cold HEPES inhibitors Laemmli buffer leupeptin Needles Nigericin Nonidet P-40 Orthovanadate Pellets, Drug Sodium Sulfoxide, Dimethyl Western Blot
3
Investigating EGFR-GIV Protein Interactions
Cell lysates (∼1–2 mg of protein) were incubated 4 h at 4°C with either 2 μg of anti-EGFR (#225) mAb (endogenous EGFR), anti-FLAG mAb (Sigma-Aldrich) (FLAG-EGFR), and their respective preimmune control IgGs. Protein G-agarose beads (Invitrogen) were added and incubated at 4°C for an additional 60 min. Beads were washed then either resuspended and boiled in SDS sample buffer, or beads were incubated with purified His-GIV-CT (aa 1623–1870) overnight, washed, and then resuspended and boiled in SDS sample buffer. For immunoprecipitations involving ligand-activated EGFR, buffers used during all steps of the process were supplemented with 100 μM sodium orthovanadate.
For experiments investigating direct interaction between GIV and EGFR, recombinant EGFR kinase (Cell Signaling Technology) was used to phosphorylate GST-tagged EGFR C terminus (EGFR-T, aa 1064–1210) in vitro according to the manufacturer's protocol. In brief, equal aliquots of GST and GST-EGFR-T were incubated with 5 ng purified kinase in the presence of 200 μM ATP (Sigma-Aldrich) at room temperature for 60 min before their use in binding assays.
The in vitro binding assays using GST-fusion proteins were carried out as described previously (Ghosh et al., 2008 (link)). In brief, purified GST-fusion proteins (15–20 μg) or GST alone (30 μg) were immobilized on glutathione-Sepharose beads and resuspended in binding buffer supplemented with nucleotides (50 mM Tris-HCl, pH 7.4, 100 mM NaCl, 0.4% [vol/vol], NP-40, 10 mM MgCl2, 5 mM EDTA, 2 mM DTT, and protease inhibitor cocktail supplemented with either 30 μM GDP or 30 μM guanosine diphosphate [GDP], 30 μM AlCl3, and 10 mM NaF) (Ghosh et al., 2008 (link)). Thereafter, [35S]Met (GE Healthcare) -labeled GIV prepared using the TnT Quick Coupled Transcription/Translation System (Promega, Madison, WI) was added to the binding buffer, and binding was carried out overnight at 4°C with constant tumbling. The following day, the beads were washed (4.3 mM Na2HPO4, 1.4 mM KH2PO4, pH 7.4, 137 mM NaCl, 2.7 mM KCl, 0.1% [vol/vol] Tween 20, 10 mM MgCl2, 5 mM EDTA, and 2 mM DTT), and boiled in sample buffer for SDS-polyacrylamide gel electrophoresis. For Gαi3, the wash buffer was supplemented with GDP or GDP, AlCl3 and NaF during binding.
Ghosh P., Beas A.O., Bornheimer S.J., Garcia-Marcos M., Forry E.P., Johannson C., Ear J., Jung B.H., Cabrera B., Carethers J.M, & Farquhar M.G. (2010). A Gαi–GIV Molecular Complex Binds Epidermal Growth Factor Receptor and Determines Whether Cells Migrate or Proliferate. Molecular Biology of the Cell, 21(13), 2338-2354.
Publication 2010
Aluminum Chloride Biological Assay Buffers Cells Edetic Acid EGFR protein, human G-substrate Glutathione Guanosine Diphosphate Immunoprecipitation Ligands Magnesium Chloride Nonidet P-40 Nucleotides Orthovanadate Phosphotransferases Phosphotransferases, ATP Promega Protease Inhibitors Proteins SDS-PAGE Sepharose Sodium Sodium Chloride Transcription, Genetic Tromethamine Tween 20
4
RIP3 Kinase Immunoprecipitation and Assay

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Publication 2009
Antibodies Antibodies, Anti-Idiotypic beta-glycerol phosphate Biological Assay Buffers Cells Complex, Immune Densitometry Edetic Acid Gels Glycerin HEPES Homo sapiens Immunoprecipitation Jurkat Cells Magnesium Chloride manganese chloride myosin phosphatase-Rho interacting protein, human NADH Dehydrogenase Complex 1 Nonidet P-40 Orthovanadate Phosphotransferases Rabbits SDHD protein, human Sepharose Sodium Sodium Chloride Tromethamine
5
SILAC-Based Proteomic Analysis of HeLa Cells

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Publication 2010
Amino Acids Arginine Buffers Cell Culture Techniques Cells Complex, Immune Deoxycholic Acid, Monosodium Salt Edetic Acid Fetal Bovine Serum G-substrate Glutamine HeLa Cells HEPES Immunoglobulins Iodoacetamide Isotopes Light Liquid Chromatography Lysine Orthovanadate Penicillins Peptides Phosphoric Monoester Hydrolases Protease Inhibitors Radioimmunoprecipitation Assay Sodium Sodium Chloride Sterility, Reproductive Streptomycin Tandem Mass Spectrometry Urea

Most recents protocols related to «Orthovanadate»

1
Western Blot Analysis of Protein Signaling
After incubation and pharmacological treatments as indicated, cells were rapidly cooled by washing with ice-cold PBS and then lysed in 2X-Laemmlli Sample buffer (0.5 M Tris pH 6.8, glycerol, 10% SDS) supplemented with 1 mM sodium orthovanadate, 10 mM okadaic acid, and 20 mM of protease inhibitor. Whole-cell lysates were then syringed 5 times with a 27.5-gauge syringe. Lysates were then heated at 65 °C for 15 min under reducing conditions (supplementation of lysis buffer with 10% beta-mercaptoethanol and 5% bromophenol blue), resolved by SDS-PAGE, and transferred to 0.2 m pore PVDF membrane (PALL Life Science). The membrane was blocked with 3% bovine serum albumin (BSA) and then incubated with indicated antibodies in 1% BSA at 1:1000 dilution at 4 °C overnight. The membrane was then subjected to a secondary horseradish peroxidase–conjugated antibody (with 1% BSA) and left to shake for 1 h at RT before imaging. Bands were visualized with Luminata ECL chemiluminescence substrate (Milipore Sigma).
Rahmani S., Ahmed H., Ibazebo O., Fussner-Dupas E., Wakarchuk W.W, & Antonescu C.N. (2023). O-GlcNAc transferase modulates the cellular endocytosis machinery by controlling the formation of clathrin-coated pits. The Journal of Biological Chemistry, 299(3), 102963.
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Publication 2023
2-Mercaptoethanol Antibodies Bromphenol Blue Buffers Cells Chemiluminescence Common Cold Glycerin Horseradish Peroxidase Immunoglobulins Okadaic Acid Orthovanadate Pharmacotherapy polyvinylidene fluoride Protease Inhibitors SDS-PAGE Serum Albumin, Bovine Sodium Syringes Technique, Dilution Tissue, Membrane Tremor Tromethamine
2
Hypoxia-Induced ERK Signaling Modulation
UFH-001 cells were exposed to normoxic or hypoxic conditions with or without BCP, at the indicated concentrations, for a total of 16 h. A second set of cells were first exposed to normoxic or hypoxic conditions for 15 ½ h, and then treated for an additional 30 min to JWH-015 at 10 μM (a CB2 receptor activator). All cells were then placed on ice, washed with ice-cold PBS (10 mM sodium phosphate salts, 120 mM NaCl, pH 7.4), and lysed in RIPA buffer [1% NP-40, 10 mM phosphate buffer, 0.1% SDS, 150 mM NaCl, 0.5% sodium deoxycholate, 1 mM sodium orthovanadate, 0.5 mM phenylmethyl sulfonyl fluoride (PMSF) and protease inhibitor (Roche Diagnostics), pH, 7.4]. Cell lysates were clarified by centrifugation at 16,000 × g for 15 min at 4°C. Protein concentration of the clarified supernatants was determined using a modification of the Lowry assay [75 (link)]. Equal protein was loaded onto 10% PAGE gels, separated by electrophoresis according to Laemmli et al. [76 (link)], and transferred to nitrocellulose membranes for western blot analysis [77 (link)] using enhanced chemiluminescence (ECL) (GE Healthcare, # RPN2106 or RPN2232). Protein loading was checked by blotting for GAPDH (Cell Signaling, D16H11). Membranes were further probed for total ERK (Calbiochem #442700) or pERK1/2 (Biolabs #9106). Images of the original western blots can be found in the Supplemental material (S1 Raw images).
Frost C.J., Ramirez-Mata A., Khattri R.B., Merritt M.E, & Frost S.C. (2023). Effects of β-caryophyllene and oxygen availability on cholesterol and fatty acids in breast cancer cells. PLOS ONE, 18(3), e0281396.
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Publication 2023
Biological Assay Buffers Cells Centrifugation Chemiluminescence Cold Temperature Deoxycholic Acid, Monosodium Salt Diagnosis Electrophoresis GAPDH protein, human Gels Hartnup Disease Hypoxia JWH 015 Nitrocellulose Nonidet P-40 Orthovanadate Phosphates Protease Inhibitors Proteins Radioimmunoprecipitation Assay Receptor, Cannabinoid, CB2 Salts Sodium Sodium Chloride sodium phosphate sulfuryl fluoride Tissue, Membrane Western Blot
3
Western Blot Analysis of Inflammasome Proteins
Cells were lysed in RIPA lysis buffer with 2 mM phenylmethylsulfonyl fluoride, 1 mM sodium orthovanadate and protease inhibitor cocktail (Santa Cruz Biotech, Dallas, TX, sc-24948) for 30 min at 4 °C and then centrifuged at 16,000 g for 15 min. Samples (25–50 μg of protein/lane) were resolved by sodium dodecyl sulfate–polyacrylamide gel electrophoresis and transferred to nitrocellulose membranes (Bio-Rad, Hercules, CA, 1704271). Blots were probed with rabbit monoclonal anti-caspase 1 (1:1000; Abcam, Cambridge, UK, ab179515), rabbit polyclonal anti-IL-1beta/IL-1F2 (1:1000; Novus Biologicals, Abingdon, UK, NB600-633), rabbit polyclonal anti-NLRP1/NALP1 (1:1000; Cell Signaling, Danvers, MA, 4990S), rabbit polyclonal anti-NLRP3/NALP3 (1:2500; Novus Biologicals, NBP2-12446), and mouse monoclonal anti-ACTB/actin (1:30,000; Sigma-Aldrich, A3853). After overnight incubation at 4 °C, bound antibodies were visualized using horseradish peroxidase-coupled secondary antibodies and the Clarity™ Western ECL Substrate (Bio-Rad, 1705061) or Clarity™ Max ECL western blotting substrate (Bio-Rad, 1705062) for low protein concentrations.
de Dios C., Abadin X., Roca-Agujetas V., Jimenez-Martinez M., Morales A., Trullas R., Mari M, & Colell A. (2023). Inflammasome activation under high cholesterol load triggers a protective microglial phenotype while promoting neuronal pyroptosis. Translational Neurodegeneration, 12, 10.
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Publication 2023
Actins Antibodies Biological Factors Buffers Caspase 1 Cells Diet, Protein-Restricted Horseradish Peroxidase Interleukin-1 beta Mus Nitrocellulose Novus Orthovanadate Phenylmethylsulfonyl Fluoride Protease Inhibitors Proteins Rabbits Radioimmunoprecipitation Assay SDS-PAGE Sodium Tissue, Membrane
4
Western Blot Analysis of Inflammasome Proteins
Cells were lysed in RIPA lysis buffer with 2 mM phenylmethylsulfonyl fluoride, 1 mM sodium orthovanadate and protease inhibitor cocktail (Santa Cruz Biotech, Dallas, TX, sc-24948) for 30 min at 4 °C and then centrifuged at 16,000 g for 15 min. Samples (25–50 μg of protein/lane) were resolved by sodium dodecyl sulfate–polyacrylamide gel electrophoresis and transferred to nitrocellulose membranes (Bio-Rad, Hercules, CA, 1704271). Blots were probed with rabbit monoclonal anti-caspase 1 (1:1000; Abcam, Cambridge, UK, ab179515), rabbit polyclonal anti-IL-1beta/IL-1F2 (1:1000; Novus Biologicals, Abingdon, UK, NB600-633), rabbit polyclonal anti-NLRP1/NALP1 (1:1000; Cell Signaling, Danvers, MA, 4990S), rabbit polyclonal anti-NLRP3/NALP3 (1:2500; Novus Biologicals, NBP2-12446), and mouse monoclonal anti-ACTB/actin (1:30,000; Sigma-Aldrich, A3853). After overnight incubation at 4 °C, bound antibodies were visualized using horseradish peroxidase-coupled secondary antibodies and the Clarity™ Western ECL Substrate (Bio-Rad, 1705061) or Clarity™ Max ECL western blotting substrate (Bio-Rad, 1705062) for low protein concentrations.
de Dios C., Abadin X., Roca-Agujetas V., Jimenez-Martinez M., Morales A., Trullas R., Mari M, & Colell A. (2023). Inflammasome activation under high cholesterol load triggers a protective microglial phenotype while promoting neuronal pyroptosis. Translational Neurodegeneration, 12, 10.
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Publication 2023
Actins Antibodies Biological Factors Buffers Caspase 1 Cells Diet, Protein-Restricted Horseradish Peroxidase Interleukin-1 beta Mus Nitrocellulose Novus Orthovanadate Phenylmethylsulfonyl Fluoride Protease Inhibitors Proteins Rabbits Radioimmunoprecipitation Assay SDS-PAGE Sodium Tissue, Membrane
5
Western Blot Analysis of Protein Extracts
After incubation, the cells were harvested and lysed in ice-cold 1% NP-40 lysis buffer containing 150 mM NaCl, 10 mM HEPES (pH 7.45), 5 mM sodium pyrophosphate, 5 mM sodium fluoride, 2 mM sodium orthovanadate, and a protease inhibitor cocktail (Roche Applied Science). Whole cell extracts were obtained from the supernatants after centrifugation of the cell lysate at 13,000 × g for 15 min at 4°C. Protein concentration was quantitated using the Bradford assay. Proteins (50 µg) were separated via SDS-polyacrylamide gel electrophoresis (PAGE; 8–13%) and transferred onto 0.45 µM nitrocellulose membranes (Amersham; Cytiva). The membranes were blocked for 60 min at room temperature using 5% (w/v) BD Difco skim milk powder (Thermo Fisher Scientific, Inc.) and immunoblotted with primary antibodies at 4°C overnight at optimal dilution (Table I). After washing three with Tris-buffered saline with 0.1% Tween 20 buffer, the membranes were incubated with horseradish peroxidase-conjugated secondary antibodies at a dilution of 1:2,000 for 1 h at room temperature. Immunoreactivity was detected using ECL Plus (Amersham; Cytiva) and digitalized using Image Quant LAS 4000 (GE Healthcare).
Yang E.S., Do Y., Cheon S.Y., Kim B., Ling J., Cho M.K., Kim T., Bae S.J, & Ha K.T. (2023). Andrographolide suppresses aerobic glycolysis and induces apoptotic cell death by inhibiting pyruvate dehydrogenase kinase 1 expression. Oncology Reports, 49(4), 72.
Publication 2023
Antibodies Biological Assay Buffers Cell Extracts Cells Centrifugation Cold Temperature HEPES Horseradish Peroxidase Milk, Cow's Nitrocellulose Nonidet P-40 Orthovanadate Powder Protease Inhibitors Proteins Saline Solution SDS-PAGE Sodium Sodium Chloride Sodium Fluoride sodium pyrophosphate Technique, Dilution Tissue, Membrane Tween 20

Top products related to «Orthovanadate»

1
Protease inhibitor cocktail by Merck Group
Sourced in United States, Germany, China, United Kingdom, Italy, Japan, Sao Tome and Principe, France, Canada, Macao, Switzerland, Spain, Australia, Israel, Hungary, Ireland, Denmark, Brazil, Poland, India, Mexico, Senegal, Netherlands, Singapore
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.
2
Sodium orthovanadate by Merck Group
Sourced in United States, Germany, France, United Kingdom, Italy, Switzerland, Japan
Sodium orthovanadate is a laboratory chemical compound commonly used as a protein tyrosine phosphatase inhibitor in various biochemical and cell-based assays. It is a white crystalline solid that is soluble in water and other polar solvents. Sodium orthovanadate is often utilized in research applications to investigate cellular signaling pathways and protein phosphorylation dynamics.
3
Protease inhibitor cocktail by Roche
Sourced in United States, Switzerland, Germany, China, United Kingdom, France, Canada, Japan, Italy, Australia, Austria, Sweden, Spain, Cameroon, India, Macao, Belgium, Israel
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.
4
Pvdf membrane by Merck Group
Sourced in United States, Germany, China, United Kingdom, Morocco, Ireland, France, Italy, Japan, Canada, Spain, Switzerland, New Zealand, India, Hong Kong, Sao Tome and Principe, Sweden, Netherlands, Australia, Belgium, Austria
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.
5
Complete protease inhibitor cocktail by Roche
Sourced in United States, Germany, Switzerland, United Kingdom, China, France, Japan, Canada, Spain, Belgium, Australia, Sweden, Italy, Ireland, Macao
The Complete Protease Inhibitor Cocktail is a laboratory product designed to inhibit a broad spectrum of proteases. It is a concentrated solution containing a mixture of protease inhibitors effective against a variety of protease classes. This product is intended to be used in research applications to preserve the integrity of target proteins by preventing their degradation by proteolytic enzymes.
6
Aprotinin by Merck Group
Sourced in United States, Germany, United Kingdom, Italy, China, Canada, Japan, Spain, France, Israel, Belgium, Austria, Switzerland, Finland, India, Australia, Macao, Hungary, Sweden, Sao Tome and Principe
Aprotinin is a protease inhibitor derived from bovine lung tissue. It is used as a laboratory reagent to inhibit protease activity in various experimental procedures.
7
Leupeptin by Merck Group
Sourced in United States, Germany, Italy, China, Japan, France, Israel, Switzerland, Canada, Sao Tome and Principe, United Kingdom, Australia, Ireland
Leupeptin is a protease inhibitor that can be used in laboratory settings to inhibit the activity of certain proteases. It is a tripeptide compound that binds to and inhibits the catalytic sites of proteases.
8
Bca protein assay kit by Thermo Fisher Scientific
Sourced in United States, China, Germany, United Kingdom, Japan, Belgium, France, Switzerland, Italy, Canada, Australia, Sweden, Spain, Israel, Lithuania, Netherlands, Denmark, Finland, India, Singapore
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.
9
β actin by Merck Group
Sourced in United States, United Kingdom, Germany, China, Canada, Japan, Macao, Italy, Sao Tome and Principe, Israel, Spain, Denmark, France, Finland, Australia, Morocco, Ireland, Czechia, Sweden, Uruguay, Switzerland, Netherlands, Senegal
β-actin is a protein that is found in all eukaryotic cells and is involved in the structure and function of the cytoskeleton. It is a key component of the actin filaments that make up the cytoskeleton and plays a critical role in cell motility, cell division, and other cellular processes.
10
Bradford assay by Bio-Rad
Sourced in United States, Germany, United Kingdom, Italy, Canada, China, France, Switzerland, Austria, Spain, Japan, Australia, Brazil, Ireland, Sweden
The Bradford assay is a colorimetric protein assay used to measure the concentration of protein in a solution. It is based on the color change of the Coomassie Brilliant Blue G-250 dye in response to various concentrations of protein.

More about "Orthovanadate"

Orthovanadate, also known as vanadium(V) oxide or vanadate, is a versatile chemical compound with the formula VO4³⁻.
It serves as the conjugate base of orthovanadic acid and is widely used in various scientific disciplines, including biochemistry, materials science, and catalysis.
One of the key applications of orthovanadate is in the study of protein tyrosine phosphatases (PTPs), a class of enzymes that play a crucial role in cellular signaling pathways.
Orthovanadate acts as a potent and specific inhibitor of PTPs, making it an invaluable tool for researchers investigating these important enzymes.
Orthovanadate is also an important precursor in the synthesis of vanadium-based materials, which have numerous applications in areas such as catalysis, energy storage, and electronics.
These materials can be used in a variety of devices, including batteries, fuel cells, and sensors.
In addition to its use in biochemical and materials science research, orthovanadate is often employed in combination with other reagents, such as protease inhibitor cocktails, PVDF membranes, and protein assay kits.
These complementary tools help researchers analyze and quantify the effects of orthovanadate on various biological systems.
Overall, orthovanadate is a versatile and widely-used compound that continues to be of great interest across multiple scientific disciplines.
Its unique properties and diverse applications make it an essential tool for researchers and innovators working at the forefront of their respective fields.