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Phosstop phosphotase inhibitor

Manufactured by Roche
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PhosSTOP is a phosphatase inhibitor designed for use in biological samples. It functions by inhibiting the activity of phosphatases, enzymes that remove phosphate groups from proteins. This product is intended to preserve the phosphorylation status of proteins during sample preparation and analysis.

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Lab products found in correlation

Complete protease inhibitor, by Roche (3 mentions) Polyvinylidene fluoride membrane, by Thermo Fisher Scientific (2 mentions) Bca assay, by Thermo Fisher Scientific (2 mentions) Nupage bis tris gel, by Thermo Fisher Scientific (2 mentions) Ripa lysis and extraction buffer, by Thermo Fisher Scientific (2 mentions) Hsc70, by Santa Cruz Biotechnology (1 mentions) Primer blast tool, by Merck Group (1 mentions) Phospho p42 44, by Cell Signaling Technology (1 mentions)

Close spelling variants of this product

PhosSTOP phosphotase inhibitor cocktail tablet PhosSTOP inhibitor PhosSTOP

3 protocols using phosstop phosphotase inhibitor

1

Measuring PDGFRB Expression and Signaling

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Pdgfrb−/− MEFs or 10T1/2 fibroblasts were transduced, sorted by FACS analysis for GFP expression, and replated onto standard cell culture plates. Expression of P-WT and P-Ex12 was assessed by qRT-PCR or western blotting, essentially as previously described (Silva et al. 2005 (link)). RT-PCR primers were designed using the National Library of Medicine PRIMER-BLAST tool, and obtained from Sigma-Aldrich. For western blotting, proteins were solubilized in RIPA lysis buffer supplemented with PhosStop Phosphotase inhibitor and Roche Complete Protease inhibitor (Roche). Primary antibodies recognized human and mouse PDGFRB (EMD Millipore, #04-825), phospho-p42/44 (Cell signaling #9102), total MAPK (Cell Signaling, 9102S), and HSC-70 (Santa Cruz SC-729). Secondary antibodies included anti-goat (Jackson ImmunoResearch 705-035-003), anti-rabbit (Jackson ImmunoResearch 111-035-003), and anti-mouse (Jackson ImmunoResearch 715-035-0150, and protein expression was detected by using both CareStream film (Sigma-Aldrich Z3730398) and Bio-Rad Clarity Enhanced Chemiluminescence (Bio-Rad 1705060)
Hassan M., Butler E., Wilson R., Roy A., Zheng Y., Liem P., Rakheja D., Pavlick D., Young L.L., Rosenzweig M., Erlich R., Ali S.M., Leavey P.J., Parsons D.W., Skapek S.X, & Laetsch T.W. (2019). Novel PDGFRB rearrangement in multifocal infantile myofibromatosis is tumorigenic and sensitive to imatinib. Cold Spring Harbor Molecular Case Studies, 5(5), a004440.
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2

Western Blot Analysis of Tumor Samples

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Protein lysates were extracted from unsorted splenic tumor samples using fresh RIPA lysis and extraction buffer (Thermo Fisher Scientific, Waltham, MA) prepared with cOmplete protease inhibitor and PhosSTOP phosphotase inhibitor (Roche Diagnostics, Indianapolis, IN). Protein concentration was quantified by the BCA assay (Thermo Fisher Scientific). Tumor samples were separated by electrophoresis in MOPS buffer on 4–12% Bis-Tris NuPAGE gels (Invitrogen), transferred to polyvinylidene fluoride membranes (Invitrogen), blocked with 5% milk, and probed using a rabbit polyclonal antibody against HA (Y-11, Santa Cruz Biotechnology, Dallas, TX) at a 1/200 dilution. The secondary antibody utilized was a donkey anti-rabbit (GE Healthcare) at a dilution of 1/500 and an antibody to beta actin (C-4, Santa Cruz Biotechnology, Dallas, TX) was used at a dilution of 1/1000 to control for protein loading.
Liu Y., Easton J., Shao Y., Maciaszek J., Wang Z., Wilkinson M.R., McCastlain K., Edmonson M., Pounds S.B., Shi L., Zhou X., Ma X., Sioson E., Li Y., Rusch M., Gupta P., Pei D., Cheng C., Smith M.A., Auvil J.G., Gerhard D.S., Relling M.V., Winick N.J., Carroll A.J., Heerema N.A., Raetz E., Devidas M., Willman C.L., Harvey R.C., Carroll W.L., Dunsmore K.P., Winter S.S., Wood B.L., Sorrentino B.P., Downing J.R., Loh M.L., Hunger S.P., Zhang J, & Mullighan C.G. (2017). THE GENOMIC LANDSCAPE OF PEDIATRIC AND YOUNG ADULT T-LINEAGE ACUTE LYMPHOBLASTIC LEUKEMIA. Nature genetics, 49(8), 1211-1218.
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3

Western Blot Analysis of Tumor Samples

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Protein lysates were extracted from unsorted splenic tumor samples using fresh RIPA lysis and extraction buffer (Thermo Fisher Scientific, Waltham, MA) prepared with cOmplete protease inhibitor and PhosSTOP phosphotase inhibitor (Roche Diagnostics, Indianapolis, IN). Protein concentration was quantified by the BCA assay (Thermo Fisher Scientific). Tumor samples were separated by electrophoresis in MOPS buffer on 4–12% Bis-Tris NuPAGE gels (Invitrogen), transferred to polyvinylidene fluoride membranes (Invitrogen), blocked with 5% milk, and probed using a rabbit polyclonal antibody against HA (Y-11, Santa Cruz Biotechnology, Dallas, TX) at a 1/200 dilution. The secondary antibody utilized was a donkey anti-rabbit (GE Healthcare) at a dilution of 1/500 and an antibody to beta actin (C-4, Santa Cruz Biotechnology, Dallas, TX) was used at a dilution of 1/1000 to control for protein loading.
Liu Y., Easton J., Shao Y., Maciaszek J., Wang Z., Wilkinson M.R., McCastlain K., Edmonson M., Pounds S.B., Shi L., Zhou X., Ma X., Sioson E., Li Y., Rusch M., Gupta P., Pei D., Cheng C., Smith M.A., Auvil J.G., Gerhard D.S., Relling M.V., Winick N.J., Carroll A.J., Heerema N.A., Raetz E., Devidas M., Willman C.L., Harvey R.C., Carroll W.L., Dunsmore K.P., Winter S.S., Wood B.L., Sorrentino B.P., Downing J.R., Loh M.L., Hunger S.P., Zhang J, & Mullighan C.G. (2017). THE GENOMIC LANDSCAPE OF PEDIATRIC AND YOUNG ADULT T-LINEAGE ACUTE LYMPHOBLASTIC LEUKEMIA. Nature genetics, 49(8), 1211-1218.
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