Protease and phosphatase inhibitor

Name: Protease and phosphatase inhibitor
Brand: Thermo Fisher Scientific
SKU: pyLhCZIBPBHhf-iFeM4p
Availability: InStock

Manufactured by Thermo Fisher Scientific

1 915 citations

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About the product

Protease and phosphatase inhibitors are laboratory reagents used to prevent the degradation of proteins and phosphorylated molecules during sample preparation and analysis. They inhibit the activity of enzymes that break down these biomolecules, helping to maintain their integrity and structure for further experimentation and study.

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Thermo Fisher Scientific's protease and phosphatase inhibitors are actively commercialized and available through authorized distributors. For example, the Halt™ Protease and Phosphatase Inhibitor Cocktail (100X) is listed on the manufacturer's website. Prices for these products vary depending on the specific formulation and quantity.

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1 915 protocols using «protease and phosphatase inhibitor»

Western Blotting and EGFR Dimerization Analysis

2025

After treatment, the cells were washed with PBS and lysed in RIPA buffer (Beyotime Biotechnology, Shanghai, China) supplemented with protease and phosphatase inhibitors (Thermo Fisher Scientific, Waltham, MA, US). Western blot analysis was performed as previously described [26 (link)]. Briefly, protein lysates were separated on 8%–12% SDS polyacrylamide gels and then transferred to polyvinylidene difluoride (PVDF) membranes. After blocking with bovine serum albumin (BSA), the membranes were incubated with anti-REG3A (#ab192224, Abcam, Cambridge, UK), anti-tubulin (#2128, Cell Signaling Technology, Danvers, MA, US), anti-phosphorylated STAT3 (#9131, Cell Signaling Technology), anti-STAT3 (#4904, Cell Signaling Technology), anti-phosphorylated tyrosine (#9411, Cell Signaling Technology), anti-phosphorylated EGFR (Y1068, #3777, Cell Signaling Technology), anti-EGFR (#4405, Cell Signaling Technology), anti-phosphorylated ERK (#4370, Cell Signaling Technology), or anti-ERK (#4695, Cell Signaling Technology) antibodies. The secondary antibody was HRP-conjugated anti-rabbit IgG (#111-035-003, Jackson ImmunoResearch Labs, West Grove, PA, US). For the phospho-kinase array, a commercial MAPK pathway phosphorylation array (#AAH-MAPK-1-4, RayBiotech, Norcross, GA, US) was used following the manufacturer’s protocol. Unless otherwise specified, all protein phosphorylation detection were performed in cells under serum-starved conditions for 24 h. Image J software (National Institutes of Health, Bethesda, MD, US) was used to measure the integrated optical density (IOD) of each dot. All blots were repeated at least 3 times for the statistical analysis.
To detect EGFR dimerization, PANC-1 cells were starved in serum-free medium for 24 h, washed with PBS, and then cold PBS containing 10 ng/mL recombinant human EGF (SinoBiological, Beijing, China) or 1 μg/mL recombinant human REG3A (rhREG3A, SinoBiological) was added to the plates, which were then incubated for 30 min at 4 °C. The cells were again washed with cold PBS and then incubated with 0.5 mM bis(sulfosuccinimidyl)suberate cross-linker (BS3, Thermo Fisher Scientific) in PBS for 2 h at 4 °C on ice. After washing again, the cross-linking reaction was stopped by incubating in 50 mM Tris buffer (pH 7.5) for 15 min. The cells were then lysed, and the dimerization of EGFR was analyzed by western blotting.

Ren X., Teng Y., Xie K., He X., Chen G., Zhang K., Liao Q., Zhang J., Zhou X., Zhu Y., Song W., Lin Y., Zhang Y., Xu Z., Maeshige N., Liang X., Su D., Sun P, & Ding Y. (2025). REG3A secreted by peritumoral acinar cells enhances pancreatic ductal adenocarcinoma progression via activation of EGFR signaling. Cell Communication and Signaling : CCS, 23, 96.

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Quantifying Cytoskeletal Protein Regulation

2025

Proteins from drug-treated B35 and C6 cells were extracted using the CelLytic™ M cell lysis reagent (Sigma-Aldrich, St. Louis, MO, USA) with protease and phosphatase inhibitors (Thermo Scientific) to prevent degradation. Protein samples (10–50 μg) were separated using SDS-PAGE (8%, 10%, or 12.5%) and transferred to PVDF membranes. Membranes were blocked and probed with primary antibodies specific to target proteins, followed by HRP-conjugated secondary antibodies. β-actin was used as an internal control. Protein bands were visualized using the Western Lightning^® Plus-ECL kit (PerkinElmer, Inc., Waltham, MA, USA). Primary antibodies used included those for beta-actin (GTX26276, GeneTex Inc., Irvine, CA, USA), RhoGDI1 (#2564, Cell Signaling Technology, Danvers, MA, USA), phosphorylated RhoGDI1 (phospho S174, ab74142, Abcam, Cambridge, UK), RhoA (#2117, Cell Signaling Technology), anti-CDC42 (#2462, Cell Signaling Technology), CDC42 (#2462, Cell Signaling Technology), Rac1 (GTX100761, GeneTex Inc.), phosphorylated RhoA Ser188 (sc-32954, Santa Cruz Biotechnology, Santa Cruz, CA, USA), phosphorylated CDC42 (ab74142, Abcam, Cambridge, UK), phosphorylated Rac1 (phospho S71) (PAB7743, Abnova Corporation, Taipei, Taiwan), ROCK1 (ab45171, Abcam), myosin light chain 2 (#3672, Cell Signaling Technology), phosphorylated MLC2 (Ser-18) (TA309976, OriGene Technologies, Rockville, MD, USA), cofilin-1(H00001072-M04, Abnova Corporation, Taipei, Taiwan), and profilin-1(#3237, Cell Signaling Technology).

Shih P.C., Tzeng I.S., Chen Y.C, & Chen M.L. (2025). Gastrodin Mitigates Ketamine-Induced Inhibition of F-Actin Remodeling and Cell Migration by Regulating the Rho Signaling Pathway. Biomedicines, 13(3), 649.

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Quantifying CD44 and MMP2 Protein Expression

2025

Protein expression levels of CD44 and MMP2 were assessed by Western blotting. Cells were lysed using RIPA buffer (Thermo Fisher Scientific, Cat. No. 89900) supplemented with protease and phosphatase inhibitors (Thermo Fisher Scientific, Cat. No. 78442). Lysates were separated by SDS-PAGE and transferred to PVDF membranes (Millipore, Cat. No. IPVH00010). Membranes were probed with primary antibodies against CD44 (Cell Signaling Technology, Cat. No. 3570) and MMP2 (Abcam, Cat. No. ab37150), followed by secondary antibodies conjugated to HRP (Thermo Fisher Scientific, Cat. No. 31460). Bands were visualized using the ECL Western Blotting Substrate (Thermo Fisher Scientific, Cat. No. 32106) and imaged using a ChemiDoc Imaging System (Bio-Rad, Cat. No. 17001402).

Jiang F., Ahmad S., kanwal S., Hameed Y, & Tang Q. (2025). Key wound healing genes as diagnostic biomarkers and therapeutic targets in uterine corpus endometrial carcinoma: an integrated in silico and in vitro study. Hereditas, 162, 5.

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Western Blot Analysis of XRN1 and PKR

2025

Cells were rinsed with PBS, then lysed in RIPA buffer in the presence of protease and phosphatase inhibitors (Thermo Fisher) and kept on ice. Following addition of SDS-page loading buffer (Invitrogen), lysates were incubated at 95 °C for 20 min. 20–40 μg of protein was run on a precast tris-acetate gel (Invitrogen) and transferred to PVDF via iBlot (Invitrogen). For XRN1 western blots, gels were incubated in 5% ethanol/water for 5 min before transfer. Membranes were blocked with Odyssey blocking buffer before incubation with primary and secondary antibodies and imaging on an Odyssey CLx. Antibodies used were as follows: XRN1 (Cell Signaling Technology (CST) 70205; 1:1000), β-Actin (CST 3700; 1:2000), total PKR (R&D systems MAB1980; 1:500), phospho-Thr451 PKR (Abcam ab81303; 1:500), IRDye 800CW Goat anti-Rabbit (Li-Cor 926-32211; 1:20,000), and IRDye 680RD Goat anti-Mouse (Licor 926-68070; 1:20,000).

Lockbaum G.J., Lynes M.M., Shen S.A., Liu J., Holt N., Nayak S.P., Knockenhauer K.E., Yao S., Sickmier E.A., Raman A., Wu J., Case A., Shehaj L., Buker S.M., Grigoriu S., Ribich S., Blakemore S.J., Sparling B.A., Duncan K.W., Copeland R.A., Silver S.J, & Boriack-Sjodin P.A. (2025). Characterization of exoribonuclease XRN1 as a cancer target and identification of adenosine-3’,5’-bisphosphate as a potent enzyme inhibitor. Communications Biology, 8, 589.

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Western Blot Analysis of Cell Signaling Proteins

2025

Cells were lysed with RIPA buffer (Thermo, USA, Cat# 89900) containing protease and phosphatase inhibitors (Thermo, USA, Cat# 78440), then centrifuged at 14,000 rpm for 10 min at 4 °C to collect the protein-containing supernatant. The protein concentration was measured using a BCA Protein Assay Kit (Cat# 23227, Thermo, USA). Equal amounts of protein (30 µg) were separated by SDS-PAGE on ReadyGel Precast Gels (Bio-Rad, USA, Cat# 161–1104) and transferred to PVDF membranes (Millipore, USA, Cat# IPVH00010) using a semi-dry transfer system (Bio-Rad, USA, Cat# 170–3930). Membranes were blocked with 5% Non-Fat Dry Milk in TBST (Thermo, USA, Cat# 37570), then incubated overnight at 4 °C with primary antibodies: ANAPC10 (Proteintech, China, Cat# 18893-1-AP) at 1:1000, AKT (CST, USA, Cat# 4691) at 1:1000, p-AKT (Ser473) (CST, USA, Cat# 4060) at 1:1000, PI3K (CST, USA, Cat# 4255) at 1:1000, p-PI3K (Tyr458) (CST, USA, Cat# 4249) at 1:1000, mTOR (CST, USA, Cat# 2983) at 1:1000, p-mTOR (Ser2448) (CST, USA, Cat# 5536) at 1:1000, and GAPDH (CST, USA, Cat# 5174) at 1:5000. After washing with TBST, the membranes were incubated with secondary antibodies (anti-rabbit IgG HRP Conjugated (CST, USA, Cat# 7074) and anti-mouse IgG HRP Conjugated (CST, USA, Cat# 7076)) at 1:2000 for 1 h at room temperature. Protein bands were visualized using ECL Western Blotting Substrate (Thermo Fisher, USA, Cat# 34095) and imaged with a Chemiluminescence system (Bio-Rad ChemiDoc).

Fang J., Duan Y., Qiu Y., Liu S., Bai X., Cai H., Zhang M, & Liu W. (2025). ANAPC10 expression predicts poor prognosis in oral squamous cell carcinoma and promotes tumor growth via the PI3K/AKT/mTOR pathway. Discover Oncology, 16, 423.

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Top 5 most cited protocols using «protease and phosphatase inhibitor»

Tissue and Serum Protein Profiling

Cited 4 times

Sample preparation, printing, scanning, and data analysis were performed as described later in detail (Gyorgy et al., 2010 (link)). Flash-frozen tissues were briefly pulverized in liquid nitrogen; 200 mg of the frozen powder was transferred into 1 ml of T-per lysis buffer (Thermo Fisher, Waltham, MA, USA) with protease and phosphatase inhibitors (Thermo Fisher) and then sonicated. Samples were centrifuged for 15 min at 4°C; the supernatants were aliquoted and stored at −80°C. Protein concentrations were measured by using a BCA assay (Thermo Fisher). Blood samples were promptly centrifuged after removal at 10,000×g for 15 min at 4°C; the supernatants were aliquoted, flash-frozen, and stored at −80°C. Tissue samples were diluted in print buffer (10% glycerol, 0.05% SDS, 50 mM DTT in 1× TBS) to a final protein concentration of 1 mg/ml, while serum samples were diluted 1:10. Samples were then subjected to an 11-point serial 1:2 dilution and transferred into Genetix 384-well plates (X7022, Fisher Scientific, Pittsburgh, PA, USA) as described (Gyorgy et al., 2010 (link)). Plates were transferred into an Aushon 2470 Arrayer (Aushon Biosystems, Billerica, MA, USA) and samples were printed on ONCYTE Avid (tissue samples) or ONCYTE Nova (serum samples) single-pad nitrocellulose coated glass slides (Grace Bio-Labs, Bend, OR, USA).

Kwon S.K., Kovesdi E., Gyorgy A.B., Wingo D., Kamnaksh A., Walker J., Long J.B, & Agoston D.V. (2011). Stress and Traumatic Brain Injury: A Behavioral, Proteomics, and Histological Study. Frontiers in Neurology, 2, 12.

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Corresponding organizations : Uniformed Services University of the Health Sciences, Walter Reed Army Institute of Research

Protein quantification and western blotting

Cited 4 times

The hippocampal and piriform cortex tissues were dissected immediately after euthanasia and snap frozen in liquid nitrogen. The tissues were homogenized and lysed in RIPA buffer containing 1% protease and phosphatase inhibitors (Thermo-Scientific, USA). We used the kit and the standard protocol from Thermo Scientific. The samples were then centrifuged at 16,000 × g for 10 min and the supernatant was collected. The protein concentration from the supernatant was determined using the Bradford assay kit (Biorad, USA). Equal amounts of protein (30–60 ug) were loaded in the wells of SDS-PAGE gels (8–10%) along with a molecular weight marker. The gels were run at 110V for 1–2h at 4° C. The proteins were transferred onto a nitrocellulose membrane and the transfer sandwich was placed into a mini transfer blot unit (Biorad, USA) at 4°C overnight at 25V for 14–16h according to the manufacturer’s instructions. Next day, the membrane was washed with PBS for few minutes and incubated with Fluorescent Western Blot blocking buffer (Rockland Immunochemicals, PA, USA) for an hour RT. After the blocking, the membranes were incubated overnight at 4°C with the primary antibodies. The following day, the membranes were washed with a mixture of PBS and 0.1% Tween® 20 (PBS-T) and then incubated with IR-680 or IR-800 dyes followed by further washes with PBS-T as described earlier. β-actin was used as a loading control and a molecular weight marker was used to determine appropriate band for the protein of our interest. Fluorescent Western Blot blocking buffer was used as a diluent for both primary and secondary antibodies. The bands were visualized on the Odyssey IR imaging system based on the molecular weight. The Region of Interest was determined by creating a rectangle frame around the largest bands of the row of the protein of interest using Image J software. The intensity of each band was quantified and analyzed by normalizing with the β-actin using Image J software.

Putra M., Sharma S., Gage M., Gasser G., Hinojo-Perez A., Olson A., Gregory-Flores A., Puttachary S., Wang C., Anantharam V, & Thippeswamy T. (2019). Inducible Nitric Oxide Synthase Inhibitor, 1400W, Mitigates DFP-induced Long-term Neurotoxicity in the Rat Model. Neurobiology of disease, 133, 104443.

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Corresponding organizations : Iowa State University, Oregon State University

Comprehensive Proteomic Analysis of Tissue Samples

Cited 4 times

Samples were minced and lysed in lysis buffer (8 M Urea, 100 mM Tris Hydrochloride, pH 8.0) containing protease and phosphatase Inhibitors (Thermo Scientific) followed by 1 min of sonication (3 s on and 3 s off, amplitude 25%). The lysate was centrifuged at 14,000×g for 10 min and the supernatant was collected as whole tissue extract. Protein concentration was determined by Bradford protein assay. Extracts from each sample (100 μg protein) was reduced with 10 mM dithiothreitol at 56 °C for 30 min and alkylated with 10 mM iodoacetamide at room temperature in the dark for additional 30 min. Samples were then digested using the FASP method^{54 (link)} with trypsin; tryptic peptides were separated in a home-made reverse-phase C18 column in a pipet tip. Peptides were eluted and separated into nine fractions using a stepwise gradient of increasing acetonitrile (6%, 9%, 12%, 15%, 18%, 21%, 25%, 30%, and 35%) at pH 10. The nine fractions were combined to six fractions, dried in a vacuum concentrator (Thermo Scientific), and then analyzed by liquid chromatography tandem mass spectrometry (LC-MS/MS).

Ge S., Xia X., Ding C., Zhen B., Zhou Q., Feng J., Yuan J., Chen R., Li Y., Ge Z., Ji J., Zhang L., Wang J., Li Z., Lai Y., Hu Y., Li Y., Li Y., Gao J., Chen L., Xu J., Zhang C., Jung S.Y., Choi J.M., Jain A., Liu M., Song L., Liu W., Guo G., Gong T., Huang Y., Qiu Y., Huang W., Shi T., Zhu W., Wang Y., He F., Shen L, & Qin J. (2018). A proteomic landscape of diffuse-type gastric cancer. Nature Communications, 9, 1012.

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Corresponding organizations : Peking University Cancer Hospital, Peking University, Beijing Proteome Research Center, Baylor College of Medicine, Chinese People's Liberation Army, Academy of Military Medical Sciences, East China Normal University, Fudan University, Zhongshan Hospital

Reverse Phase Protein Microarray Analysis

Cited 4 times

Sample preparation, printing, scanning, and data analysis of serum and brain regions were performed using Reverse Phase Protein Microarray (RPPM) as described earlier (Kovesdi et al., 2011 (link); Kwon et al., 2011 (link)). Briefly, frozen brain tissues were pulverized in liquid nitrogen, the powder was transferred into a lysis buffer (Thermo Fisher, Waltham, MA, USA) with protease and phosphatase inhibitors (Thermo Fisher), sonicated, centrifuged, and the supernatants aliquoted and stored at −80°C. Protein concentrations were measured by BCA assay (Thermo Fisher). Blood samples were centrifuged at 10,000 × g for 15 min at 4°C; supernatants were aliquoted, flash-frozen, and stored at −80°C.
Tissue samples were diluted in print buffer and then subjected to an 11-point serial 1:2 dilution and transferred into Genetix 384-well plates (X7022, Fisher Scientific, Pittsburg, PA, USA) using a JANUS Varispan Integrator and Expanded Platform Workstation (PerkinElmer, Waltham, MA, USA). Plates were transferred into an Aushon 2470 Arrayer (Aushon Biosystem, Billerica, MA, USA) to be printed on ONCYTE Avid (brain samples) or ONCYTE Nova (serum samples) single-pad nitrocellulose coated glass slides (Grace Bio-Labs, Bend, OR, USA; Gyorgy et al., 2010 (link)).
Primary antibodies (Table A2 in Appendix) were diluted to 10× the optimal Western analysis concentration in antibody incubation buffer as described earlier (Gyorgy et al., 2010 (link)). The primary antibody solution was incubated overnight at 4°C with a cover slip. The following day slides were washed and then incubated with an Alexa Fluor^® 635 goat anti-mouse (Cat# A-31574), goat anti-rabbit (Cat# A-31576), or rabbit anti-goat IgG (H + L; Cat# A-21086) secondary antibodies from Invitrogen at 1:6000 dilution in antibody incubation buffer for 1 h at room temperature. After washing and drying, fluorescent signals were measured by a Scan Array Express HT microarray scanner (Perkin Elmer, Waltham, MA, USA) using a 633 nm wavelength laser and a 647 nm filter.
Data from the scanned images were imported into a Microsoft Excel-based bioinformatics program developed in-house for analysis (Gyorgy et al., 2010 (link)). The linear regression of the log–log data was calculated after the removal of flagged data, which include signal to noise ratios of less than 2, spot intensities in the saturation range or noise range, or high variability between duplicate spots (>10–15%). The total amount of antigen is determined by the y-axis intercept (Y-cept; Gyorgy et al., 2010 (link)). Data is reported as the mean Y-cept ±SEM.

Kovesdi E., Kamnaksh A., Wingo D., Ahmed F., Grunberg N.E., Long J.B., Kasper C.E, & Agoston D.V. (2012). Acute Minocycline Treatment Mitigates the Symptoms of Mild Blast-Induced Traumatic Brain Injury. Frontiers in Neurology, 3, 111.

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Corresponding organizations : United States Department of Veterans Affairs, Uniformed Services University of the Health Sciences, Center for Neuroscience and Regenerative Medicine

Cell Signaling Pathway Assays for Receptor Activation

Cited 3 times

For cell stimulations for western blot, HEK293 and β-arrestin 1 KO cells transfected with siRNAs and Rasless MEFs and Gnas f/f cells treated for 72 h with Adeno-iCre or Adeno-GFP control were left untreated or treated with 10 μM Isoproterenol (Iso) for indicated time points. Additional 3 min stimulations with Forskolin (FSK) (5 mg/ml) or EGF (10 ng/mL) were also performed when indicated. For the experiments done with pharmacological inhibitors, confluent cells were first treated with the vehicle control (DMSO), LY294002 (25 μM) for 1 h, AG1478 (10 μM) for 1 h, U0126 (10 μM) for 90 min, PP1 (10 μM) for 1 h, SU6656 (10 μM) for 1 h, H89 (10 μM) for 1 h, CE3F4 (10 μM) for 1 h, cAMPS-RP (100 μM) for 30 min, SB-590885 (10 μM) for 4 h, GDC-0879 (10 μM) for 4 h or PTX (50 ng/mL) for 16 h before Iso stimulation. For V2R stimulations, 100 nM of AVP was used at the indicated time points. Cells were lysed in RIPA buffer (Sigma) containing a mixture of protease and phosphatase inhibitors (Thermo Scientific) and clarified by centrifugation. Lysates were resolved on SDS-PAGE gels, transferred onto PVDF membranes (Millipore) and probed with appropriate antibodies. Westerns to detect active RAS-GTP were performed using glutathione–Sepharose beads (GE Healthcare) immobilized with the RAS-interactive binding domain of c-Raf-1 fused to glutathione-S-transferase (GST) as previously described (44 (link)). For pERK1/2 ELISA (Sandwich ELISA kit #7177, Cell Signaling Technology), cells were cultured in a 12-well plate, stimulated with indicated concentrations of ligands and lysed in 150 μl of provided lysis buffer supplemented with protease and phosphatase inhibitors (Thermo Scientific). ELISA was performed according to manufacturer's instructions and absorbance readings were measured on a BioTek Synergy Neo plate reader.

O'Hayre M., Eichel K., Avino S., Zhao X., Steffen D.J., Feng X., Kawakami K., Aoki J., Messer K., Sunahara R., Inoue A., von Zastrow M, & Gutkind J.S. (2017). Genetic evidence that β-arrestins are dispensable for the initiation of β2-adrenergic receptor signaling to ERK. Science signaling, 10(484), eaal3395.

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Corresponding organizations : National Institute of Dental and Craniofacial Research, National Institutes of Health, University of California, San Francisco, University of Calabria, University of California, San Diego, Sichuan University, Tohoku University, Japan Agency for Medical Research and Development, Japan Science and Technology Agency

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