mini edta free protease inhibitor cocktail roche  (Roche)

 
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    Structured Review

    Roche mini edta free protease inhibitor cocktail roche
    Mini Edta Free Protease Inhibitor Cocktail Roche, supplied by Roche, used in various techniques. Bioz Stars score: 94/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/mini edta free protease inhibitor cocktail roche/product/Roche
    Average 94 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    mini edta free protease inhibitor cocktail roche - by Bioz Stars, 2020-04
    94/100 stars

    Related Products / Commonly Used Together

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    Related Articles

    Colorimetric Assay:

    Article Title: Cereblon versus VHL: Hijacking E3 ligases against each other using PROTACs
    Article Snippet: After the appropriate incubation time, cells were washed with DPBS (Gibco) and lysed using 85 µL RIPA buffer (Sigma-Aldrich) supplemented with cOmplete Mini EDTA-free protease inhibitor cocktail (Roche) and benzonase. .. Lysates were clarified by centrifugation (20000 g , 10 min, 4 °C) and the total protein content of the supernatant was quantified using a Bradford colorimetric assay.

    Centrifugation:

    Article Title: Cereblon versus VHL: Hijacking E3 ligases against each other using PROTACs
    Article Snippet: After the appropriate incubation time, cells were washed with DPBS (Gibco) and lysed using 85 µL RIPA buffer (Sigma-Aldrich) supplemented with cOmplete Mini EDTA-free protease inhibitor cocktail (Roche) and benzonase. .. Lysates were clarified by centrifugation (20000 g , 10 min, 4 °C) and the total protein content of the supernatant was quantified using a Bradford colorimetric assay.

    Protease Inhibitor:

    Article Title: Cereblon versus VHL: Hijacking E3 ligases against each other using PROTACs
    Article Snippet: .. After the appropriate incubation time, cells were washed with DPBS (Gibco) and lysed using 85 µL RIPA buffer (Sigma-Aldrich) supplemented with cOmplete Mini EDTA-free protease inhibitor cocktail (Roche) and benzonase. .. Lysates were clarified by centrifugation (20000 g , 10 min, 4 °C) and the total protein content of the supernatant was quantified using a Bradford colorimetric assay.

    Concentration Assay:

    Article Title: Cereblon versus VHL: Hijacking E3 ligases against each other using PROTACs
    Article Snippet: 4.2.2 Evaluation of cellular activity of PROTACs HeLa (5 × 105 ) and HEK293 (1 × 106 ) cells were seeded in standard 6-well plates (2 mL medium) overnight before treatment with compounds at the desired concentration and a final DMSO concentration of 0.1% v/v. .. After the appropriate incubation time, cells were washed with DPBS (Gibco) and lysed using 85 µL RIPA buffer (Sigma-Aldrich) supplemented with cOmplete Mini EDTA-free protease inhibitor cocktail (Roche) and benzonase.

    Incubation:

    Article Title: Cereblon versus VHL: Hijacking E3 ligases against each other using PROTACs
    Article Snippet: .. After the appropriate incubation time, cells were washed with DPBS (Gibco) and lysed using 85 µL RIPA buffer (Sigma-Aldrich) supplemented with cOmplete Mini EDTA-free protease inhibitor cocktail (Roche) and benzonase. .. Lysates were clarified by centrifugation (20000 g , 10 min, 4 °C) and the total protein content of the supernatant was quantified using a Bradford colorimetric assay.

    Activity Assay:

    Article Title: Cereblon versus VHL: Hijacking E3 ligases against each other using PROTACs
    Article Snippet: Paragraph title: Evaluation of cellular activity of PROTACs ... After the appropriate incubation time, cells were washed with DPBS (Gibco) and lysed using 85 µL RIPA buffer (Sigma-Aldrich) supplemented with cOmplete Mini EDTA-free protease inhibitor cocktail (Roche) and benzonase.

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    Roche complete mini edta free protease inhibitor cocktail
    Apocatalase polypeptide proteolysis is induced in late exponential growth phase E. faecalis cells. A , lysates from strain OG1RF cells grown in heme-free medium until early exponential growth phase ( sample A ) or late exponential growth phase ( sample B ) and lysates from cells grown in heme-supplemented medium until late exponential growth phase ( sample C ) were analyzed individually or as mixtures as indicated. The samples were incubated at 37 °C, and the presence of KatA polypeptide in aliquots removed at the indicated time points was determined by immuno-blot. B , proteolysis of KatA in sample A mixed with sample B in the presence of 1 m m <t>PMSF</t> and/or <t>EDTA</t> or Complete EDTA-free protease inhibitor cocktail. The reference, sample A + B without any additions, is indicated by Ctrl .
    Complete Mini Edta Free Protease Inhibitor Cocktail, supplied by Roche, used in various techniques. Bioz Stars score: 99/100, based on 86 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/complete mini edta free protease inhibitor cocktail/product/Roche
    Average 99 stars, based on 86 article reviews
    Price from $9.99 to $1999.99
    complete mini edta free protease inhibitor cocktail - by Bioz Stars, 2020-04
    99/100 stars
      Buy from Supplier

    93
    Roche mini edta free protease inhibitor cocktail tablet
    Limited RNaseIII activity in E . histolytica trophozoite lysate. (A) Stem-loop structure of pre-miR122 dsRNA substrate used for RNaseIII activity assay. Mature miR-122/miR-122* duplex shown in red. Structure obtained from http://www.mirbase.org/cgi-bin/mirna_entry.pl?acc=MI0000442 . (B) In vitro cleavage of [α- 32 P]ATP-labeled pre-miR122 by 10μl of whole cell lysate from E . histolytica trophozoites expressing Myc-EhRNaseIII. Reactions contained 3mM MgCl 2 , <t>20mM</t> potassium glutamate, ± 20mM <t>EDTA</t> and were incubated for 40, 80, or 120 minutes at 37°C. EDTA chelates the magnesium and inhibits RNaseIII activity. The dsRNA only sample contained no protein. The buffer only sample contained 10μl of lysate buffer (no protein). dsRNA and buffer only samples were incubated for 120 minutes at 37°C. Positive control reactions contained 1U of E . coli RNaseIII (Ambion). Asterisks indicate specific cleavage products– 50-60nt (*) and 20-21nt (**). The 40-50nt bands are non-specific products of the pre-miR122 cleavage.
    Mini Edta Free Protease Inhibitor Cocktail Tablet, supplied by Roche, used in various techniques. Bioz Stars score: 93/100, based on 11 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/mini edta free protease inhibitor cocktail tablet/product/Roche
    Average 93 stars, based on 11 article reviews
    Price from $9.99 to $1999.99
    mini edta free protease inhibitor cocktail tablet - by Bioz Stars, 2020-04
    93/100 stars
      Buy from Supplier

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    Apocatalase polypeptide proteolysis is induced in late exponential growth phase E. faecalis cells. A , lysates from strain OG1RF cells grown in heme-free medium until early exponential growth phase ( sample A ) or late exponential growth phase ( sample B ) and lysates from cells grown in heme-supplemented medium until late exponential growth phase ( sample C ) were analyzed individually or as mixtures as indicated. The samples were incubated at 37 °C, and the presence of KatA polypeptide in aliquots removed at the indicated time points was determined by immuno-blot. B , proteolysis of KatA in sample A mixed with sample B in the presence of 1 m m PMSF and/or EDTA or Complete EDTA-free protease inhibitor cocktail. The reference, sample A + B without any additions, is indicated by Ctrl .

    Journal: The Journal of Biological Chemistry

    Article Title: In Vitro Assembly of Catalase *

    doi: 10.1074/jbc.M114.596148

    Figure Lengend Snippet: Apocatalase polypeptide proteolysis is induced in late exponential growth phase E. faecalis cells. A , lysates from strain OG1RF cells grown in heme-free medium until early exponential growth phase ( sample A ) or late exponential growth phase ( sample B ) and lysates from cells grown in heme-supplemented medium until late exponential growth phase ( sample C ) were analyzed individually or as mixtures as indicated. The samples were incubated at 37 °C, and the presence of KatA polypeptide in aliquots removed at the indicated time points was determined by immuno-blot. B , proteolysis of KatA in sample A mixed with sample B in the presence of 1 m m PMSF and/or EDTA or Complete EDTA-free protease inhibitor cocktail. The reference, sample A + B without any additions, is indicated by Ctrl .

    Article Snippet: To test protection of KatA by protease inhibitors 1 mm PMSF and/or 1 mm EDTA, or 1× Complete mini EDTA-free protease inhibitor cocktail (Roche Applied Science), were added to lysate from late exponential growth phase cells.

    Techniques: Incubation, Protease Inhibitor

    Association of EhRab7A with EhVps26, EhVps29, and EhVps35. (A) SDS-PAGE profiles of EhRab7A-binding proteins isolated from the E. histolytica lysate. GST-EhRab7A- or GST-EhRab5-immobilized columns were loaded with GTPγS or GDP and then incubated with the amoeba lysate. Bound proteins were eluted and analyzed by SDS-PAGE, followed by silver staining. Molecular-weight standards are indicated on the left of the gel (kDa). EhVps35 and EhVps26, identified by liquid chromatography and tandem mass spectrometry, as well as costripped GST-EhRab5 and GST-EhRab7, are also indicated. (B) A multiple alignment (top, only the carboxyl half is shown) and a schematic diagram (bottom) of Vps26 from E. histolytica , human, and yeast. The alignment was created by the Neighbor-Joining method using CLUSTAL W version 1.81 with the Blosum matrix. Identical residues are marked with asterisks and conserved amino acid substitutions are marked with either dots or colons. A unique carboxyl-terminal extension present in EhVps26 is overlined (top) or shown as an open box (bottom). (C and D) In vitro binding of recombinant EhRab7A with EhVps26 and EhVps29 (C), and of recombinant EhRab7A with EhVps26FL and EhVps26ΔC (D). The GST-EhRab7A-immobilized column was loaded with GTPγS and incubated with histidine-tagged EhVps26, EhVps29, or both (C), or histidine-tagged EhVps26FL or EhVps26ΔC (D). A fraction eluted from the resin with EDTA and an unbound fraction were analyzed by immunoblotting with anti-EhVps26 (C and D) and EhVps29 (C) antibodies.

    Journal: Molecular Biology of the Cell

    Article Title: A Retromerlike Complex Is a Novel Rab7 Effector That Is Involved in the Transport of the Virulence Factor Cysteine Protease in the Enteric Protozoan Parasite Entamoeba histolytica

    doi: 10.1091/mbc.E05-04-0283

    Figure Lengend Snippet: Association of EhRab7A with EhVps26, EhVps29, and EhVps35. (A) SDS-PAGE profiles of EhRab7A-binding proteins isolated from the E. histolytica lysate. GST-EhRab7A- or GST-EhRab5-immobilized columns were loaded with GTPγS or GDP and then incubated with the amoeba lysate. Bound proteins were eluted and analyzed by SDS-PAGE, followed by silver staining. Molecular-weight standards are indicated on the left of the gel (kDa). EhVps35 and EhVps26, identified by liquid chromatography and tandem mass spectrometry, as well as costripped GST-EhRab5 and GST-EhRab7, are also indicated. (B) A multiple alignment (top, only the carboxyl half is shown) and a schematic diagram (bottom) of Vps26 from E. histolytica , human, and yeast. The alignment was created by the Neighbor-Joining method using CLUSTAL W version 1.81 with the Blosum matrix. Identical residues are marked with asterisks and conserved amino acid substitutions are marked with either dots or colons. A unique carboxyl-terminal extension present in EhVps26 is overlined (top) or shown as an open box (bottom). (C and D) In vitro binding of recombinant EhRab7A with EhVps26 and EhVps29 (C), and of recombinant EhRab7A with EhVps26FL and EhVps26ΔC (D). The GST-EhRab7A-immobilized column was loaded with GTPγS and incubated with histidine-tagged EhVps26, EhVps29, or both (C), or histidine-tagged EhVps26FL or EhVps26ΔC (D). A fraction eluted from the resin with EDTA and an unbound fraction were analyzed by immunoblotting with anti-EhVps26 (C and D) and EhVps29 (C) antibodies.

    Article Snippet: GST-EhRab5 or GST-EhRab7A were expressed in E. coli and immobilized onto glutathione-Sepharose 4B by incubation of the E. coli lysate with the resin for 1 h at 4°C, in PBS, pH 7.4, containing 200 μM GDP, 5 mM MgCl2 , 5 mM 2-mercaptoethanol, Complete Mini EDTA free protease inhibitor cocktail (Roche, Basel, Switzerland), and 10 μg/ml transepoxysuccinyl- l -leucylamido-(4-guanidino)butane (E-64), and 0.1% Triton X-100, followed by extensive washing.

    Techniques: SDS Page, Binding Assay, Isolation, Incubation, Silver Staining, Molecular Weight, Liquid Chromatography, Mass Spectrometry, In Vitro, Recombinant

    Extensive proteolytic processing in human platelets during storage. Platelets were stored under blood-banking conditions for 9 days with or without EDTA-free cOmplete protease inhibitor cocktail, and the platelet proteome from different days was characterized

    Journal: Blood

    Article Title: TAILS N-terminomics of human platelets reveals pervasive metalloproteinase-dependent proteolytic processing in storage

    doi: 10.1182/blood-2014-04-569640

    Figure Lengend Snippet: Extensive proteolytic processing in human platelets during storage. Platelets were stored under blood-banking conditions for 9 days with or without EDTA-free cOmplete protease inhibitor cocktail, and the platelet proteome from different days was characterized

    Article Snippet: For broad protease inhibition, cOmplete mini EDTA-free protease inhibitor cocktail tablets (1 tablet/10 mL) (Roche) were used.

    Techniques: Protease Inhibitor

    Examples of proteolytic processing identified by TAILS in stored platelets. Platelets were stored under blood-banking conditions for 9 days with or without EDTA-free cOmplete protease inhibitor cocktail, and the platelet proteome from different days was

    Journal: Blood

    Article Title: TAILS N-terminomics of human platelets reveals pervasive metalloproteinase-dependent proteolytic processing in storage

    doi: 10.1182/blood-2014-04-569640

    Figure Lengend Snippet: Examples of proteolytic processing identified by TAILS in stored platelets. Platelets were stored under blood-banking conditions for 9 days with or without EDTA-free cOmplete protease inhibitor cocktail, and the platelet proteome from different days was

    Article Snippet: For broad protease inhibition, cOmplete mini EDTA-free protease inhibitor cocktail tablets (1 tablet/10 mL) (Roche) were used.

    Techniques: Protease Inhibitor

    Limited RNaseIII activity in E . histolytica trophozoite lysate. (A) Stem-loop structure of pre-miR122 dsRNA substrate used for RNaseIII activity assay. Mature miR-122/miR-122* duplex shown in red. Structure obtained from http://www.mirbase.org/cgi-bin/mirna_entry.pl?acc=MI0000442 . (B) In vitro cleavage of [α- 32 P]ATP-labeled pre-miR122 by 10μl of whole cell lysate from E . histolytica trophozoites expressing Myc-EhRNaseIII. Reactions contained 3mM MgCl 2 , 20mM potassium glutamate, ± 20mM EDTA and were incubated for 40, 80, or 120 minutes at 37°C. EDTA chelates the magnesium and inhibits RNaseIII activity. The dsRNA only sample contained no protein. The buffer only sample contained 10μl of lysate buffer (no protein). dsRNA and buffer only samples were incubated for 120 minutes at 37°C. Positive control reactions contained 1U of E . coli RNaseIII (Ambion). Asterisks indicate specific cleavage products– 50-60nt (*) and 20-21nt (**). The 40-50nt bands are non-specific products of the pre-miR122 cleavage.

    Journal: PLoS ONE

    Article Title: A Single RNaseIII Domain Protein from Entamoeba histolytica Has dsRNA Cleavage Activity and Can Help Mediate RNAi Gene Silencing in a Heterologous System

    doi: 10.1371/journal.pone.0133740

    Figure Lengend Snippet: Limited RNaseIII activity in E . histolytica trophozoite lysate. (A) Stem-loop structure of pre-miR122 dsRNA substrate used for RNaseIII activity assay. Mature miR-122/miR-122* duplex shown in red. Structure obtained from http://www.mirbase.org/cgi-bin/mirna_entry.pl?acc=MI0000442 . (B) In vitro cleavage of [α- 32 P]ATP-labeled pre-miR122 by 10μl of whole cell lysate from E . histolytica trophozoites expressing Myc-EhRNaseIII. Reactions contained 3mM MgCl 2 , 20mM potassium glutamate, ± 20mM EDTA and were incubated for 40, 80, or 120 minutes at 37°C. EDTA chelates the magnesium and inhibits RNaseIII activity. The dsRNA only sample contained no protein. The buffer only sample contained 10μl of lysate buffer (no protein). dsRNA and buffer only samples were incubated for 120 minutes at 37°C. Positive control reactions contained 1U of E . coli RNaseIII (Ambion). Asterisks indicate specific cleavage products– 50-60nt (*) and 20-21nt (**). The 40-50nt bands are non-specific products of the pre-miR122 cleavage.

    Article Snippet: Dicing assays were conducted in 20μl volumes where 10μl of whole cell extract was incubated with 10,000 cpm of radiolabeled dsRNA (~2 ng/μl final concentration) in reaction buffer (150mM sucrose, 20mM potassium L-glutamate (Sigma), 20mM HEPES-KOH, pH 7.9, 3mM MgCl2 , 10 μg/ml leupeptin, 1 Complete Mini EDTA-free protease inhibitor cocktail tablet (Roche Diagnostics) for every 3ml of buffer) [ ] supplemented with 30U Protector RNase Inhibitor (Roche Diagnostics) and 1U/μl SUPERNase·IN RNase Inhibitor (Ambion) with or without 20mM EDTA for 2 hours at 37°C unless otherwise indicated.

    Techniques: Activity Assay, In Vitro, Labeling, Expressing, Incubation, Positive Control