Cocktail inhibitor

Manufactured by Merck Group

The Cocktail inhibitor is a laboratory equipment product designed to inhibit the activity of various enzymes or proteins. It is a mixture of different inhibitors that can target multiple biological processes simultaneously. The Cocktail inhibitor is a tool used in research laboratories to study the effects of enzyme or protein inhibition on cellular functions.

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Lab products found in correlation

Close spelling variants of this product

Cocktails of protease inhibitors and phosphatase inhibitors Proteases and phosphatases inhibitors cocktails Protease inhibitors and phosphatase inhibitors cocktails Protease inhibitor cocktails and phosphatase inhibitors Cocktails of Protease inhibitors Cocktails of protease and phosphatase inhibitors Phosphatase inhibitors (cocktails 2 and 3, Protease inhibitor and phosphatase inhibitor (2,3) cocktails Protease inhibitor and phosphatase inhibitor cocktails I and II Protease inhibitor cocktails set III

6 protocols using cocktail inhibitor

Extraction and Separation of Cytoskeletal and Fibrin Proteins

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Frozen tissues were homogenized in 10 volumes (mg : μl) of T-PER tissue protein extraction reagent (Thermo#78510) containing cocktail inhibitor (Sigma#P8340) and PMSF. After centrifugation at 10,000 g for 10 min, supernatant was collected for β actin detection. Pellet was homogenized in 3 M urea and vortexed for 2 hrs at 37°C. After centrifugation at 14,000 g for 15 min, pellet was suspended in Immunoblot sample buffer (reducing) and vortexed at 65°C for 30 min and ready for fibrin detection.

Wu C., Lu W., Zhang Y., Zhang G., Shi X., Hisada Y., Grover S.P., Zhang X., Li L., Xiang B., Shi J., Li X.A., Daugherty A., Smyth S.S., Kirchhofer D., Shiroishi T., Shao F., Mackman N., Wei Y, & Li Z. (2019). Inflammasome activation triggers blood clotting and host death through pyroptosis. Immunity, 50(6), 1401-1411.e4.

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Protein Expression Analysis of Stem Cell Markers

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Cells (5 × 10⁵) were collected at various time points and then washed with ice-cold PBS twice before adding lysis buffer (M-PER Mammalian Protein Extraction reagent, Thermo Scientific, Cat No. 78501) and cocktail inhibitor (Sigma, 5 μg/ml, Cat No. P8340). Equal amounts of protein were loaded into each well and separated by NuPAGE 4–12% Bis-Tris gel, followed by transfer onto PVDF-membranes (Bio-Rad, Cat No. 162-0177). Membranes were blocked with 5% non-fat milk in PBS-T for 1 h at room temperature. The blots were then incubated with antibodies against GRPR, Caspase-3, p-AKT1, AKT1, p-AKT2, AKT2, p-mTOR, mTOR, p-MAPK, MAPK, p-RPS6, RPS6, p-p38 MAPK, p38 MAPK CD133, Sox2, and ALDH for 1 h at 4°C. Goat anti-rabbit IgG secondary (1:5000; Santa Cruz Biotechnology, Cat No. sc-2004) was then incubated for 45 min at room temperature. Immunoblots were developed by using the chemiluminescence detection system (PerkinElmer, Cat No. NEL105) and autoradiography was performed. β-actin was used as a loading control.

Kim K.W., Kim J.Y., Qiao J., Clark R.A., Powers C.M., Correa H, & Chung D.H. (2019). Dual-Targeting AKT2 and ERK in cancer stem-like cells in neuroblastoma. Oncotarget, 10(54), 5645-5659.

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Western Blot Analysis of LC3 I/II

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Cells (5X10⁵) were collected at various time points, and then washed with ice-cold PBS twice before adding lysis buffer (M-PER Mammalian Protein Extraction reagent, Thermo Scientific, 78501) and cocktail inhibitor (5 µg/ml, Sigma, P8340). Equal amounts of protein were loaded into each well and separated by NuPAGE 4-12% Bis-Tris gel, followed by transfer onto PVDF-membranes (Bio-Rad, 162-0177). Membranes were blocked with 5% non-fat milk in PBS-T for 1 h at room temperature (RT). The blots were then incubated with antibodies against LC3 I &II. for 1 h at 4°C. Goat anti-rabbit IgG secondary antibody (1:5000; Santa Cruz Biotechnology, sc-2004) was then incubated for 45 min at RT. Immunoblots were developed by using the chemiluminescence detection system (PerkinElmer, NEL105) and autoradiography was performed. β-actin was used as a loading control.

Kim K.W., Qiao J., Kim J.Y., Park K, & Chung D.H. (2020). Overexpression of microRNA-145 inhibits tumorigenesis through autophagy in chemotherapy and radiation resistant neuroblastoma cells. Oncoscience, 7(1-2), 1-9.

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Protein Extraction and Fibrin Detection

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Frozen tissues were homogenized in 20 volumes (mg: μL) of T-PER tissue protein extraction reagent (Thermo scientific, Cat#78510) containing cocktail inhibitor (Sigma, Cat#P8340). After centrifugation at 10,000 g for 10 minutes, supernatant was collected for β-actin detection. Pellets were then homogenized in 3 M urea and vortexed for 2 hours at 37 °C. After centrifugation at 14,000 g for 15 minutes, pellets were suspended in LDS sample buffer and vortexed at 65 °C for 30 minutes and ready for fibrin detection.

Cui J., Li H., Zhang G., Zhang Y., Yang L., Sim M.M., Wood J.P., Wei Y., Li Z, & Wu C. (2023). Inhibiting NINJ1-dependent plasma membrane rupture protects against inflammasome-induced blood coagulation and inflammation. bioRxiv.

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Western Blot Analysis of Apoptosis Markers

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Frozen kidney tissues or cells were lysed in PLC lysis buffer containing cocktail inhibitor (Merck Millipore, GER) for 30 minutes on ice. Samples were boiled in SDS loading buffer and then separated on SDS-PAGE gels following standard protocol. Transfer membranes were immunoblotted with primary antibodies against cleaved caspase-3 (^#9664S, Cell Signaling Technology, UK), caspase-12 (^#2202P, Cell Signaling Technology, UK), CHOP (^#2895P, Cell Signaling Technology, UK), GRP78 (^#3177S, Cell Signaling Technology, UK), Phospho-Akt (Ser473) (^#4060S, Cell Signaling Technology, UK), Akt (^#4691S, Cell Signaling Technology, UK), Phospho-p70S6 kinase (^#9204S, Cell Signaling Technology, UK), p70S6 kinase (^#9202S, Cell Signaling Technology, UK) and GAPDH (^#2118S, Cell Signaling Technology, UK) overnight at 4°C. After extensive washing in TBST buffer, the membranes were incubated with secondary antibody for 1h at room temperature. The protein bands on the western blots were then visualized using an ECL Plus (Amersham, IL) according to the manufacturer's instructions.

Long Y., Zhen X., Zhu F., Hu Z., Lei W., Li S., Zha Y, & Nie J. (2017). Hyperhomocysteinemia Exacerbates Cisplatin-induced Acute Kidney Injury. International Journal of Biological Sciences, 13(2), 219-231.

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Protein Extraction and Western Blot Analysis

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The proteins were extracted from NRK-52E cells using PLC lysis buffer containing a cocktail inhibitor (Merck Millipore, GER). The cell lysate was subjected to western blot as described previously [30 (link)]. The primary antibodies used are as follows: anti-EZH2 (5246 s; Cell Signaling Technology), anti-Bcl-2 (3498 s; Cell Signaling Technology), anti-cleaved caspase 3 (9664 s; Cell Signaling Technology), anti-Akt (4685 s; Cell Signaling Technology), anti-p ~ Akt (4060 s; Cell Signaling Technology), anti-S6K (2708 s; Cell Signaling Technology), anti-p ~ S6K (9234 s; Cell Signaling Technology), anti-HuR (ab200342; Abcam), anti-Deptor (11816 s; Cell Signaling Technology), anti-H3K27me3 (9733 s; Cell Signaling Technology), H3 (4499 s; Cell Signaling Technology), and anti-GAPDH (5174 s; Cell Signaling Technology).

Chen S.Q., Li J.Q., Wang X.Q., Lei W.J., Li H., Wan J., Hu Z., Zou Y.W., Wu X.Y, & Niu H.X. (2020). EZH2-inhibitor DZNep enhances apoptosis of renal tubular epithelial cells in presence and absence of cisplatin. Cell Division, 15, 8.

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