Phosphatase inhibitor cocktail type 1 and 2

Manufactured by Merck Group

Sourced in Germany

Phosphatase inhibitor cocktail type I and II is a laboratory product designed to inhibit the activity of serine/threonine and tyrosine phosphatases. It is a mixture of various chemical compounds that effectively inhibit a broad range of phosphatases, allowing researchers to study protein phosphorylation and dephosphorylation processes in biological samples.

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Lab products found in correlation

Bradford protein assay, by Bio-Rad (4 mentions) Protease inhibitor cocktail, by Roche (4 mentions) Gapdh, by Merck Group (3 mentions) Pvdf membrane, by Thermo Fisher Scientific (2 mentions) Sds page, by Bio-Rad (1 mentions) P erk, by Cell Signaling Technology (1 mentions) Phospho p44 42 mapk, by Cell Signaling Technology (1 mentions) Eaat2, by Santa Cruz Biotechnology (1 mentions) P44 42 mapk, by Cell Signaling Technology (1 mentions) Glial fibrillary acidic protein (gfap), by Cell Signaling Technology (1 mentions) Nupage bis tris gel, by Thermo Fisher Scientific (1 mentions) Pcamkii t286, by Cell Signaling Technology (1 mentions) Pakt s473, by Cell Signaling Technology (1 mentions)

Spelling variants of this product

Phosphatase inhibitor cocktail (1110 citations) Phosphatase inhibitors (852 citations) Phosphatase inhibitor 2 (16 citations) Type II (13 citations) Cocktail II (10 citations) Phosphatases inhibitors (7 citations) Cocktail inhibitor (6 citations) Type I (6 citations) Phosphatase I inhibitor (2 citations) Inhibitor II (2 citations)

4 protocols using phosphatase inhibitor cocktail type 1 and 2

Western Blot Analysis of Cystathionine Gamma-Lyase

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Mouse tissues were homogenized in a solution containing 50 mM Tris buffer (pH 7.4), 2 mM EDTA, 5 mM EGTA, 0.1% SDS, a protease inhibitor cocktail (Roche, Indianapolis, IN), and phosphatase inhibitor cocktail type I and II (Sigma, Saint Louis, MO). Homogenates were centrifuged at 500×g for 15 min and supernatants were collected. Protein concentrations were analyzed using the Bradford protein assay (BioRad, Hercules, CA). Proteins were separated using 10% SDS-PAGE (Bio-Rad, Hercules, CA) and transferred onto PVDF membranes, and incubated with antibodies against CSE catalogue # 12217-1-AP (Fisher Scientific), eNOS catalogue #9572, phospho-eNOS catalogue #9750, and α/β-Tubulin catalogue #2148 (Cell Signaling). Chemiluminescent bands were detected and quantified using NIH Image J software.

Kolluru G.K., Glawe J.D., Pardue S., Kasabali A., Alam S., Rajendran S., Cannon A.L., Abdullah C.S., Traylor J.G., Shackelford R.E., Woolard M.D., Orr A.W., Goeders N.E., Dominic P., Bhuiyan M.S, & Kevil C.G. (2022). Methamphetamine causes cardiovascular dysfunction via cystathionine gamma lyase and hydrogen sulfide depletion. Redox Biology, 57, 102480.

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Western Blot Analysis of NAc Proteins

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NAc tissues were homogenized in a solution containing 50 mM Tris buffer (pH 7.4), 2 mM EDTA, 5 mM EGTA, 0.1% SDS, protease inhibitor cocktail (Roche, Indianapolis, IN), and phosphatase inhibitor cocktail type I and II (Sigma). Homogenates were centrifuged at 500 g for 15 min and supernatants were collected. Proteins were analyzed using Bradford protein assay (BioRad, Hercules, CA). Proteins were separated by 4–12% NuPAGE Bis Tris gels at 130 V for 2 h, transferred onto PVDF membranes at 30 V for 1 h (Thermo Fisher Scientific, Waltham, MA), and incubated with antibodies against EAAT2 (Santa Cruz, Dallas, TX; SC-365634; 1:500), CAP1 (Santa Cruz, Dallas, TX; SC-376286; 1:500), RTN4 (Santa Cruz, Dallas, TX; SC-271878; 1:500), pERK; phospho-p44/42MAPK (Cell Signaling, Danvers, MA; 9106; 1:500), ERK; p44/42MAPK (Cell Signaling, Danvers; 9102; 1:500), and GAPDH (Millipore, Burlington, MA; MAB374; 1:2000). Chemiluminescent bands were detected on an Image Station and quantified using NIH Image J software.

Germany C.E., Reker A.N., Hinton D.J., Oliveros A., Shen X., Andres-Beck L.G., Wininger K.M., Trutchul M., Cvek U., Choi D.S, & Nam H.W. (2018). Pharmacoproteomics Profile in Response to Acamprosate Treatment of an Alcoholism Animal Model. Proteomics, 18(7), e1700417.

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Protein Analysis in Rodent Brain Regions

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Mice were anesthetized with carbon dioxide and rapidly decapitated. Brains were quickly removed and dissected to isolate the CPu and NAc. Briefly, tissues were homogenized in a solution containing 50 mmol/L Tris buffer (pH 7.4), 2 mmol/L EDTA, 5 mmol/L EGTA, 0.1% SDS, protease inhibitor cocktail (Roche, Germany), and phosphatase inhibitor cocktail type I and II (Sigma-Aldrich, St. Louis, MO). Homogenates were centrifuged at 500 g at 4°C for 15 min and supernatants were collected. Proteins were analyzed using Bradford protein assay (BioRad, Hercules, CA). Proteins were separated by 4–12% NuPAGE™ Bis Tris gels at 130 V for 2 h, transferred onto PVDF membranes at 30 V for 1 h (Invitrogen, Carlsbad, CA), and analyzed using antibodies against GFAP (1:1000; Cell Signaling, Danvers, MA) and GAPDH (1:1000; Millipore, Billerica, MA). Blots were developed using chemiluminescent detection reagents (Pierce, Rockford, IL). Chemiluminescent bands were detected on a Kodak Image Station 4000R scanner (New Haven, CT) and quantified using NIH Image J software.

Hinton D.J., Lee M.R., Jang J.S, & Choi D.S. (2014). Type 1 equilibrative nucleoside transporter regulates astrocyte-specific glial fibrillary acidic protein expression in the striatum. Brain and Behavior, 4(6), 903-914.

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Quantitative Western Blot Analysis of Signaling Molecules

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NAc tissues were homogenized in a solution containing 50 mM Tris buffer (pH 7.4), 2 mM EDTA, 5 mM EGTA, 0.1% SDS, protease inhibitor cocktail (Roche, Indianapolis, IN), and phosphatase inhibitor cocktail type I and II (Sigma). Homogenates were centrifuged at 500 g for 15 min and supernatants were collected. Proteins were analyzed using Bradford protein assay (BioRad, Hercules, CA). Proteins were separated by PROTEAN TGX gels at 100 V for 1 h, transferred onto PVDF membranes at 30 V for 1 h (BioRad, Hercules, CA), and incubated with antibodies against pCaMKII (T286) (Cell Signaling, Danvers; 9102; 1:500), CaMKII (Cell Signaling, Danvers; 9102; 1:500), pNR2B (S1303) (Cell Signaling, Danvers; 9102; 1:500), pGluR1(S831) (Cell Signaling, Danvers; 9102; 1:500), pPKCγ(T514) (Cell Signaling, Danvers; 9102; 1:500), PKCγ; (Cell Signaling, Danvers; 9102; 1:500), pNR1(S896) (Cell Signaling, Danvers; 9102; 1:500), Ng (Cell Signaling, Danvers; 9102; 1:500), pAKT(S473) (Cell Signaling, Danvers; 9102; 1:500), AKT (Cell Signaling, Danvers; 9102; 1:500), mGluR5 (Cell Signaling, Danvers; 9102; 1:500) and GAPDH (Millipore, Burlington, MA; MAB374; 1:2000). Chemiluminescent bands were detected on an Image Station and quantified using NIH Image J software.

Nam H.W., Grant C., Jorgensen A., Heppelmann C.J., Trutschl M, & Cvek U. (2019). Neurogranin Regulates Alcohol Sensitivity Through AKT Pathway in the Nucleus Accumbens. Proteomics, 20(1), e1900266.

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