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Sodium Vanadate

Sodium Vanadate: A chemical compound consisting of sodium and vanadium, with the formula Na3VO4.
It is used in various industrial and research applications, including as a catalyst, an additive in glass and ceramics, and a potential treatment for certain medical conditions.
Sodium Vanadate has been studied for its effects on glucose and lipid metabolism, as well as its potential neuroprotective and antioxidant properties.
Researchers can leverge PubComapre.ai's AI-powered platform to easily locate and compare protocols from scientific literature, preprints, and patents, helping to identify the best methods and products for their Sodium Vanadate research and accelerate their discoveries.

Most cited protocols related to «Sodium Vanadate»

1
Fractionation of Breast Epithelial Cell Proteome
Human breast epithelial cells (MCF10A) were transfected with a pQCXIH vector and were cultured in DMEM/F12 (Invitrogen, Carlsbad, CA) supplemented with 5% horse serum (Invitrogen), 20 ng/mL EGF, 0.5 μg/mL hydro-cortisone, 100 ng/mL cholera toxin, 10 μg/mL insulin, and 50 μg/mL penicillin/streptomycin until 70–80% confluence was reached. The cells were then lysed in a buffer containing 8 M urea, 2.5 mM sodium pyrophosphate, 1 mM β-glycerophosphate, 50 mM ammonium bicarbonate, one-third tablet of protease inhibitor, and 2 mM sodium ortho-vanadate. Proteins were denatured, reduced, and alkylated after which tryptic digestions were performed at an enzyme/substrate ratio of 1:50. For method comparison between SCX and RP, digested peptides were cleaned by flowing through a 1 mL solid-phase extraction C18 column (Discovery DSC-18, SUPELCO, Bellefonte, PA). Samples were concentrated using a Speed-Vac SC 250 Express (Thermo Savant, Holbrook, NY) and stored at −80°C until time for analysis. A 300.0 μg desalted peptide sample was used for each SCX, low-pH RPLC, and high-pH RPLC fractionation. A 300.0 μg nondesalted protein digest was used to evaluate the potential of high-pH approach for desalting.
Wang Y., Yang F., Gritsenko M.A., Wang Y., Clauss T., Liu T., Shen Y., Monroe M.E., Lopez-Ferrer D., Reno T., Moore R.J., Klemke R.L., Camp DG I.I, & Smith R.D. (2011). Reversed-phase chromatography with multiple fraction concatenation strategy for proteome profiling of human MCF10A cells. Proteomics, 11(10), 2019-2026.
Publication 2011
ammonium bicarbonate beta-glycerol phosphate Breast Buffers Cells Cholera Toxin Cloning Vectors Cortisone Digestion Enzymes Epithelial Cells Equus caballus Fractionation, Chemical Homo sapiens Insulin Penicillins Peptides Protease Inhibitors Proteins Serum sodium pyrophosphate Sodium Vanadate Solid Phase Extraction Streptomycin Tablet Trypsin Urea
2
Histological and Immunological Analysis of Placental Samples
Samples were fixed, paraffin embedded, sectioned, and stained with hematoxylin/eosin for histological evaluation as described [57 (link)]. Tissue sections were subject to immunological staining with avidin:biotinylated enzyme complex as described [18 (link),58 (link)]. Proteins were extracted from TS cells using M-PER reagent (PIERCE) with the addition of protease inhibitor cocktail (Sigma-Aldrich), 1 mM sodium molybdate, 1 mM sodium vanadate, and 10 mM N-ethylmaleimide, or SDS lysis buffer (2% SDS, 10% glycerol, and 50 mM Tris, pH 6.8). Protein extracts were subject to immunoblotting as described [54 (link)]. Bound primary antibodies were detected with horseradish peroxidase-conjugated secondary antibodies (Vector Lab), followed by ECL-mediated visualization (GE HealthCare) and autoradiography. Mouse monoclonal antibodies anti-actin (Thermo Fisher; 1:1,000), anti-BrdU (Thermo Fisher; 1:300), anti-Cdx2 (BioGenex; 1:1), anti-MDM2 (Santa Cruz; 1:100), and anti-SUMO-1 (Zymed; 1:2,000); rabbit polyclonal antibodies anti-calnexin (Stressgene; 1:2,000), anti-cyclin D1 (Neomarker; 1:100), anti-Ki67 (Neomarker; 1:400), anti-laminin (Sigma-Aldrich; 1:25), anti-Myc tag (CalBioChem; 1:400), anti-Oct4 (Santa Cruz; 1:200), anti-p53 (Santa Cruz; 1:50), and anti-p450scc (Chemicon; 1:200); and goat polyclonal antibody anti-lamin B (Santa Cruz; 1:100) were used as primary antibodies. BrdU incorporation analysis was performed by intraperitoneal injection of BrdU (250 μg/g of body weight) into pregnant females for 1 h. Placentas were recovered, fixed, embedded, sectioned, and subject to immunostaining as described [18 (link),57 (link)].
Chiu S.Y., Asai N., Costantini F, & Hsu W. (2008). SUMO-Specific Protease 2 Is Essential for Modulating p53-Mdm2 in Development of Trophoblast Stem Cell Niches and Lineages. PLoS Biology, 6(12), e310.
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Publication 2008
Actins Antibodies Autoradiography Avidin Body Weight Bromodeoxyuridine Buffers Calnexin Cloning Vectors Cyclin D1 Eosin Ethylmaleimide Glycerin Goat Horseradish Peroxidase immunoglobulin B Immunoglobulins Injections, Intraperitoneal Laminin Lamins Lamin Type B MDM2 protein, human Monoclonal Antibodies Multienzyme Complexes Mus Paraffin Placenta POU5F1 protein, human Pregnant Women Protease Inhibitors Proteins Rabbits sodium molybdate(VI) Sodium Vanadate SUMO1 protein, human Tissues Tromethamine
3
Western Blot Analysis of GABAergic Signaling Proteins
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 GABAAR 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 GABAAR 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
4
Murine Tissue Fractionation and Proteomic Analysis
Five murine brains
and livers were harvested from CO2 asphyxiated 3-week-old
male Swiss-Webster mice (Jackson Lab, Bar Harbor, ME). Saccharomyces
cerevisiae cells were grown to an OD of 1.0, washed with
ice cold PBS and snap frozen in liquid N2 until further
use. Brain/liver tissues and yeast cells were mechanically lysed with
a homogenizer in SDS lysis buffer [2.0% SDS w/v, 250 mM NaCl, PhosSTOP
(Roche, Madison, WI) phosphatase inhibitors, 2 mM sodium vanadate,
EDTA free protease inhibitor cocktail (Promega, Madison, WI), and
50 mM HEPES, pH 8.5]. Lysates were reduced with 5 mM DTT and cysteine
residues alkylated with iodoacetamide (14 mM) in the dark (30 min).
Protein was extracted by methanol–chloroform precipitation
and subsequent ice cold acetone washes. Pellets were dried and resuspended
in 8 M urea containing 50 mM HEPES (pH 8.5). Protein concentrations
were measured by BCA assay (Thermo Scientific, Rockford, IL) prior
to protease digestion. Protein lysates were diluted to 4 M urea and
digested with LysC (Wako, Japan) in a 1/200 enzyme/protein ratio overnight.
Protein extracts were diluted further to a 1.5 M urea concentration,
and trypsin (Promega, Madison, WI) was added to a final 1/250 enzyme/protein
ratio for 6 h at 37 °C. Digests were acidified with 200 μL
of 20% formic acid (FA) to a pH ∼2 and subjected to C18 solid-phase
extraction (SPE) (Sep-Pak, Waters, Milford, MA).
Erickson B.K., Jedrychowski M.P., McAlister G.C., Everley R.A., Kunz R, & Gygi S.P. (2014). Evaluating Multiplexed Quantitative Phosphopeptide Analysis on a Hybrid Quadrupole Mass Filter/Linear Ion Trap/Orbitrap Mass Spectrometer. Analytical Chemistry, 87(2), 1241-1249.
Publication 2014
Acetone Biological Assay Brain Buffers Cells Chloroform Cold Temperature Digestion Edetic Acid Enzymes formic acid Freezing HEPES inhibitors Iodoacetamide Liver Methanol Mouse, Swiss Mus Pellets, Drug Peptide Hydrolases Phosphoric Monoester Hydrolases Promega Protease Inhibitors Proteins Sodium Chloride Sodium Vanadate Staphylococcal Protein A Tissues Trypsin Urea Yeast, Dried
5
Cell Lysis and Immunoprecipitation Protocol
HEK293T cells were transiently transfected using polyethylenimine. Sixteen hours after transfection HEK293T cells were incubated with or without MG132 for 3 h before collection. NHFs, NIH3T3, RPE and U2OS cells were subjected to experimental conditions (serum-starvation before re-addition of serum or siRNA) for various times before collection. Cell lysis was carried out with lysis buffer (50 mM Tris, at pH 8.0, 150 mM NaCl, glycerol 10%, 1 mM EDTA, 50 mM NaF and NP-40 0.1%) supplemented with protease and phosphatase inhibitors. For denaturating conditions, cells were lysed in lysis buffer containing 1% SDS, 5 mM dithiothreitol, 1 mM sodium vanadate and 50 mM Tris at pH 7.4 and boiled for 10 min before immunoprecipitation. Immunoprecipitation and immunoblotting were performed as previously described49 (link),50 (link).
Kuchay S., Duan S., Schenkein E., Peschiaroli A., Saraf A., Florens L., Washburn M.P, & Pagano M. (2013). FBXL2- and PTPL1-mediated degradation of p110-free p85β regulatory subunit controls the PI(3)K signalling cascade. Nature cell biology, 15(5), 10.1038/ncb2731.
Publication 2013
Buffers Cells Dithiothreitol Edetic Acid Glycerin Immunoprecipitation inhibitors MG 132 NIH 3T3 Cells Nonidet P-40 Peptide Hydrolases Phosphoric Monoester Hydrolases Polyethyleneimine RNA, Small Interfering Serum Sodium Chloride Sodium Vanadate Transfection Tromethamine

Most recents protocols related to «Sodium Vanadate»

1
Quantification of KCC2 expression in spinal cord
To detect the expression of KCC2 in the spinal cord, tissues were collected at P8 and frozen after removing the dorsal and ventral roots. Samples were prepared in an ice-cold lysis buffer containing 1% Igepal CA-630 (Sigma-Aldrich, Merck KGaA, Germany), 0.1% sodium dodecyl sulfate, 10 mM sodium vanadate, 10 mM sodium fluoride, 10 mM sodium pyrophosphate, and 1.8 mg/mL iodoacetamide supplemented with a cocktail of protease inhibitors (Complete-mini, Roche Life Science). After centrifugation at 18,000×g for 30 min at 4 °C, the supernatant was collected, and protein concentrations were determined using the DC protein assay (BioRad). Proteins of equivalent amounts (30 µg) were separated from the samples by performing electrophoresis using SDS-PAGE (4–15% Criterion™ TGX Stain-Free™ Precast Gels, BioRad). These were transferred to a nitrocellulose membrane and incubated overnight at 4 °C with the affinity-purified rabbit anti-KCC2 polyclonal antibody (diluted 1:1000; Merck-Millipore). The blot was then incubated after 1 h at 24 °C with an ImmunoPure goat horseradish peroxidase-conjugated rabbit-specific antibody (1:80,000, Thermo Scientific, in blocking solution of Tris-buffered saline containing 5% fat-free milk powder). Bands were visualized using chemiluminescence (Merck-Millipore). Signal intensities were measured using ImageQuant LAS 4000 and ImageQuant LAS 4000 Control Software (GE HealthCare). Equal amounts of protein samples were loaded, and total protein normalization was performed using stain-free imaging (BioRad), which makes the proteins fluorescent directly in the gel, followed by their transfer. The total density for each lane was measured from the blot and used to calculate the normalizing factors. After normalization to the total protein signal intensity for KCC2, we normalized the data by dividing each sample by the mean value of the control samples60 (link).
Tsuji M., Mukai T., Sato Y., Azuma Y., Yamamoto S., Cayetanot F., Bodineau L., Onoda A., Nagamura-Inoue T, & Coq J.O. (2023). Umbilical cord-derived mesenchymal stromal cell therapy to prevent the development of neurodevelopmental disorders related to low birth weight. Scientific Reports, 13, 3841.
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Publication 2023
Antibodies, Anti-Idiotypic Biological Assay Buffers Cardiac Arrest Centrifugation Chemiluminescence Cold Temperature Electrophoresis Freezing Goat Horseradish Peroxidase Igepal CA-630 Immunoglobulins Iodoacetamide Milk, Cow's Nitrocellulose Powder Protease Inhibitors Proteins Rabbits Saline Solution SDS-PAGE Sodium Fluoride sodium pyrophosphate Sodium Vanadate Spinal Cord Stains Sulfate, Sodium Dodecyl Tissue, Membrane Tissues Ventral Roots
2
Quantification of RANKL Protein Levels
This factor in MSCs (6 BCPs and 5 HVs) was analyzed by Western Blot. Briefly, cells were lysed in RIPA buffer [Tris (pH=7.5) 25 mM, NaCl 360 mM, nonidet P-40 2.5%, sodium deoxycholate 1%, SDS 0.25%, sodium vanadate 5 mM], supplemented with proteases and phosphatases inhibitor cocktail (P8340, Sigma) at 4°C for 30 min. After centrifugation for 30 min at 16,000 g at 4°C, pellets were frozen and conserved at -80°C until use. SDS-PAGE electrophoresis was performed using 20 µg of denatured protein, later transferred onto a nitrocellulose membrane (RPN3032D, Amersham). The membrane was stained with 0.2% Ponceau S in 0.5% acetic acid to verify the integrity of the transferred proteins. After blocking with 5% skim milk in T20-TBS, the membranes were incubated with primary Abs against human RANKL (1:200, mouse IgG2b, MAB626, Clone: 70525, R&D Systems) and β-Actin (1:2000, mouse IgG1, ab6276, Clone: AC-15, Abcam). Goat anti mouse Ig conjugated to horseradish peroxidase was used as secondary Ab (goat IgG, HAF007, R&D Systems). Hybridizing bands were visualized using ECL™ Prime Western Blotting System (GERPN2232, Sigma) and were digitalized using the image analysis system (G Box Chemi XT16, Syngene, USA). Relative RANKL quantification was performed by normalization with β-Actin signal and expressed as mean relative density using ImageJ analysis software (NIH).
Fernández Vallone V., Borzone F.R., Martinez L.M., Giorello M.B., Choi H., Dimase F., Feldman L., Bordenave R.H., Chudzinski-Tavassi A.M., Batagelj E, & Chasseing N.A. (2023). Spontaneous Osteoclastogenesis, a risk factor for bone metastasis in advanced luminal A-type breast cancer patients. Frontiers in Oncology, 13, 1073793.
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Publication 2023
Acetic Acid Actins Buffers Cells Centrifugation Clone Cells Deoxycholic Acid, Monosodium Salt Electrophoresis Endopeptidases Freezing Goat Homo sapiens Horseradish Peroxidase IgG1 IgG2B Milk, Cow's Mus Nitrocellulose Nonidet P-40 Pellets, Drug Phosphoric Monoester Hydrolases ponceau S Proteins Radioimmunoprecipitation Assay SDS-PAGE Sodium Chloride Sodium Vanadate Tissue, Membrane TNFSF11 protein, human Tromethamine Western Blot
3
Western Blotting of eIF6 in HCT116 Cells
HCT116 cells (human colorectal carcinoma line) (ATCC) were cultured as described previously (37 (link),57 (link)). HCT116 cells were maintained in McCoy's 5A medium supplemented with 10% fetal bovine serum (FBS), and 100 units/ml penicillin and 100 μg/ml streptomycin (Gibco). Cells are routinely ensured to be negative for mycoplasma contamination using the mycoplasma detection kit (ATCC). For western blotting, the cells were washed twice in PBS and lysed in mammalian cell lysis buffer (MCLB) (50 mM Tris–Cl pH 8.0, 5 mM EDTA, 0.5% Igepal, 150 mM NaCl) that was supplemented with the following inhibitors just before lysis: 1 mM phenylmethylsufonyl fluoride (PMSF), 1 mM sodium fluoride, 10 mM β-glycerophosphate, 1 mM sodium vanadate, 2 mM DTT, 1× protease inhibitor cocktail (Sigma–Aldrich), 1× phosphatase inhibitor cocktail (Santa Cruz Biotechnology). Lysates were rocked for 15 min at 4°C followed by centrifugation at 14 000 rpm for 10 min at 4°C. Blots were probed with anti-eIF6 antibody (Santa Cruz Biotechnology, sc-390441) (1:1000, overnight) or anti-βTubulin antibody (Cell Signaling, 2128) (1:1000, overnight) diluted in TBS-T buffer.
Elliff J., Biswas A., Roshan P., Kuppa S., Patterson A., Mattice J., Chinnaraj M., Burd R., Walker S.E., Pozzi N., Antony E., Bothner B, & Origanti S. (2023). Dynamic states of eIF6 and SDS variants modulate interactions with uL14 of the 60S ribosomal subunit. Nucleic Acids Research, 51(4), 1803-1822.
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Publication 2023
Antibodies, Anti-Idiotypic beta-glycerol phosphate Buffers Cells Centrifugation Colorectal Carcinoma Edetic Acid EIF6 protein, human Fetal Bovine Serum Fluorides HCT116 Cells Homo sapiens inhibitors Mammals McCoy's 5A medium Mycoplasma Penicillins Phosphoric Monoester Hydrolases Protease Inhibitors Sodium Chloride Sodium Fluoride Sodium Vanadate Streptomycin Tromethamine
4
Western Blot Analysis of Smad and AKT
Sectioned muscles were lysed with ice-cold RIPA buffer (20 mM Tris-HCl, pH 7.4; 2 mM EDTA; 2 mM ethylene glycol tetraacetic acid; 1 mM DTT; 50 mM β-glycerol phosphate; 0.1 mM sodium vanadate; 1.6 mM pervanadate; 1% Triton X-100; 10% glycerol; 10 μg/mL aprotinin; 10 μg/mL pepstatin; 1 μM benzamide; and 2 μM PMSF). After homogenization, the protein lysates were centrifuged at 12,000 rpm for 5 min at 4 °C, and only the supernatants were used. To quantify the total proteins in the tissue lysates, a Bradford assay was conducted. A total of 20 μg/μL of protein was loaded onto each 10% polyacrylamide gel. Those gels were electrophoresed at 100 V for 2 h. The proteins were sorted by size and transferred to a PVDF membrane overnight. That membrane was probed with the following primary antibodies overnight at 4 °C: anti-Smad2/3 (CST #8685), anti-p-Smad2 s245/250/255 (CST #3104), anti-p-Smad2 s465/467/Smad3 (CST #8828), anti-AKT (CST #9272), anti-p-AKT Ser473 (CST #4058), and anti-GAPDH (Santa Cruz #SC166545). The membrane was washed 3 times with Tris-buffered saline with Tween 20 and then incubated with secondary antibodies conjugated with horseradish peroxidase in BSA for 2 h. Chemiluminescence was detected with a ChemiDoc imaging system (Luminograph III, ATTO, NY, USA), and band intensity was measured and quantified with ImageJ software.
Oh J., Park S.H., Kim D.S., Choi W., Jang J., Rahmawati L., Jang W.Y., Lim H.K., Hwang J.Y., Gu G.R., Geum J.H., Choi S.Y., Kim J.H, & Cho J.Y. (2023). The Preventive Effect of Specific Collagen Peptides against Dexamethasone-Induced Muscle Atrophy in Mice. Molecules, 28(4), 1950.
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Publication 2023
Antibodies Aprotinin benzamide Biological Assay Buffers Chemiluminescence Cold Temperature Edetic Acid Egtazic Acid GAPDH protein, human Gels Glycerin Glycerophosphates Horseradish Peroxidase Muscle Tissue pepstatin pervanadate polyacrylamide gels polyvinylidene fluoride Proteins Radioimmunoprecipitation Assay Saline Solution SMAD2 protein, human SMAD3 protein, human Sodium Vanadate Staphylococcal Protein A Tissue, Membrane Tissues Triton X-100 Tween 20
5
Cytosolic and Nuclear Protein Extraction
Cells were harvested after the respective treatment and washed twice with 1X PBS and resuspended in Extraction Buffer A (10 mM HEPES, 1 mM EDTA, 1 mM EGTA, 10 mM KCl, 1 mM DTT, 5 mM NaF, 1 mM Sodium vanadate, 10 mM Sodium molybdate, 0.5 mM PMSF and 1X Protease inhibitor cocktail) and was incubated on ice for 15 min. 0.3 µl of 10% NP-40 was added to it and vortexed for 30 sec at 4° C. The lysate was centrifuged at 10000xg for 1 min at 4° C. The supernatant was collected as the cytosolic fraction. The pellet was resuspended in Extraction Buffer B (20 mM HEPES, 1 mM EDTA, 1 mM EGTA, 400 mM NaCl, 1 mM DTT, 5 mM NaF, 1 mM Sodium vanadate, 10 mM Sodium molybdate, 0.5 mM PMSF and 1X Protease inhibitor cocktail). It was incubated for 30 min on a shaker at 4° C and then centrifuged at 20,000xg for 5 min. The supernatant was collected as nuclear fractions.
Singh U., Bindra D., Samaiya A, & Mishra R.K. (2023). Overexpressed Nup88 stabilized through interaction with Nup62 promotes NF-κB dependent pathways in cancer. Frontiers in Oncology, 13, 1095046.
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Publication 2023
Buffers Cells Cytosol Edetic Acid Egtazic Acid HEPES Nonidet P-40 NP 10 Protease Inhibitors Sodium Chloride sodium molybdate(VI) Sodium Vanadate

Top products related to «Sodium Vanadate»

1
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.
2
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.
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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.
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Pvdf membrane by Merck Group
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5
Sodium vanadate by Merck Group
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Sodium vanadate is a chemical compound that is used as a laboratory reagent. It has the chemical formula Na3VO4 and is a white or yellow crystalline solid. Sodium vanadate is soluble in water and is commonly used in various analytical and research applications in the field of chemistry and biology.
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Pierce bca protein assay kit by Thermo Fisher Scientific
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The Pierce BCA Protein Assay Kit is a colorimetric-based method for the quantification of total protein in a sample. It utilizes the bicinchoninic acid (BCA) reaction, where proteins reduce Cu2+ to Cu+ in an alkaline environment, and the resulting purple-colored reaction is measured spectrophotometrically.
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Dc protein assay kit by Bio-Rad
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The DC protein assay kit is a colorimetric-based protein quantification method developed by Bio-Rad. It allows for the determination of protein concentration in aqueous solutions.
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Complete protease inhibitor cocktail by Roche
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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.
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Complete protease inhibitor by Roche
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Complete protease inhibitor is a laboratory product that functions to inhibit a broad range of proteases. It is designed to prevent the degradation of proteins during sample preparation and analysis.
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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.

More about "Sodium Vanadate"

Sodium Vanadate, also known as sodium orthovanadate or vanadium (V) sodium salt, is a chemical compound composed of sodium and vanadium, with the chemical formula Na3VO4.
This compound has a variety of industrial and research applications, including use as a catalyst, an additive in glass and ceramics, and a potential treatment for certain medical conditions.
In the field of biochemistry and cell biology, Sodium Vanadate is often studied for its effects on glucose and lipid metabolism, as well as its potential neuroprotective and antioxidant properties.
Researchers may also utilize Sodium Vanadate in conjunction with other compounds, such as Protease inhibitor cocktails, Polyvinylidene difluoride (PVDF) membranes, and the Pierce BCA Protein Assay Kit or DC Protein Assay Kit, to investigate cellular processes and signaling pathways.
Leveraging the power of PubComapre.ai's AI-powered platform, researchers can easily locate and compare protocols from scientific literature, preprints, and patents, helping them identify the best methods and products for their Sodium Vanadate research.
This streamlined approach can accelerate their discoveries and drive their work forward more efficiently.
Whether you're studying the metabolic effects of Sodium Vanadate, exploring its potential therapeutic applications, or investigating its role in cellular processes, PubComapre.ai's AI-driven analysis can be a valuable tool in your research workflow.
By optimizing your Sodium Vanadate research, you can unlock new insights and advance your scientific understanding in this important field.