trypsin tpck  (Worthington Biochemical)


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  • 99
    Name:
    Trypsin TPCK Treated
    Description:
    A chromatographically purified diafiltered lyophilized powder that has been treated with L tosylamido 2 phenyl ethyl chloromethyl ketone TPCK to inhibit contaminating chymotryptic activity Kostka and Carpenter J Biol Chem 239 1799 1964
    Catalog Number:
    LS003740
    Price:
    86
    Source:
    Bovine Pancreas
    Size:
    100 mg
    Cas Number:
    9002.07.7
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    Structured Review

    Worthington Biochemical trypsin tpck
    The R377W and F488L mutations do not affect protein stability. (A). Thermal denaturation study of the WT and R377W and F488L mutant C-termini. Shown are thermal denaturation curves for the WT and mutant C-termini obtained at 220 nm from 20°C to 80°C (GST, black; WT, blue; R377W, green; and F488L, red). Denaturation curves are in units of molar ellipticity vs. temperature. The transition temperature was at ∼ 59°C for GST and was at ∼ 68°C for the C-terminal fusion proteins. The unfolding temperature at the R377W and F488L mutants was not different from that in the WT. (B). Limited tryptic digestion of the WT and R377W and F488L mutant CNGA3. The membranes prepared from cells that had been <t>transfected</t> with cDNAs encoding the WT and R377W and F488L mutants were incubated with <t>trypsin-TPCK</t> (30 μg/ml) at 30°C for 2, 5, and 10 min. The digested products were resolved on 10% SDS-PAGE, followed by Western blotting using the polyclonal anti-CNGA3 antibody. Shown are representative images showing limited proteolysis of the WT and mutant CNGA3 subunits. The cleavage rates of the mutants to trypsin were about the same as the WT.
    A chromatographically purified diafiltered lyophilized powder that has been treated with L tosylamido 2 phenyl ethyl chloromethyl ketone TPCK to inhibit contaminating chymotryptic activity Kostka and Carpenter J Biol Chem 239 1799 1964
    https://www.bioz.com/result/trypsin tpck/product/Worthington Biochemical
    Average 99 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    trypsin tpck - by Bioz Stars, 2021-10
    99/100 stars

    Images

    1) Product Images from "The Disease-Causing Mutations in the Carboxyl-Terminus of Cone Cyclic Nucleotide-Gated Channel CNGA3 Subunit Alter the Local Secondary Structure and Interfere with the Channel Active Conformational Change"

    Article Title: The Disease-Causing Mutations in the Carboxyl-Terminus of Cone Cyclic Nucleotide-Gated Channel CNGA3 Subunit Alter the Local Secondary Structure and Interfere with the Channel Active Conformational Change

    Journal: Biochemistry

    doi: 10.1021/bi901960u

    The R377W and F488L mutations do not affect protein stability. (A). Thermal denaturation study of the WT and R377W and F488L mutant C-termini. Shown are thermal denaturation curves for the WT and mutant C-termini obtained at 220 nm from 20°C to 80°C (GST, black; WT, blue; R377W, green; and F488L, red). Denaturation curves are in units of molar ellipticity vs. temperature. The transition temperature was at ∼ 59°C for GST and was at ∼ 68°C for the C-terminal fusion proteins. The unfolding temperature at the R377W and F488L mutants was not different from that in the WT. (B). Limited tryptic digestion of the WT and R377W and F488L mutant CNGA3. The membranes prepared from cells that had been transfected with cDNAs encoding the WT and R377W and F488L mutants were incubated with trypsin-TPCK (30 μg/ml) at 30°C for 2, 5, and 10 min. The digested products were resolved on 10% SDS-PAGE, followed by Western blotting using the polyclonal anti-CNGA3 antibody. Shown are representative images showing limited proteolysis of the WT and mutant CNGA3 subunits. The cleavage rates of the mutants to trypsin were about the same as the WT.
    Figure Legend Snippet: The R377W and F488L mutations do not affect protein stability. (A). Thermal denaturation study of the WT and R377W and F488L mutant C-termini. Shown are thermal denaturation curves for the WT and mutant C-termini obtained at 220 nm from 20°C to 80°C (GST, black; WT, blue; R377W, green; and F488L, red). Denaturation curves are in units of molar ellipticity vs. temperature. The transition temperature was at ∼ 59°C for GST and was at ∼ 68°C for the C-terminal fusion proteins. The unfolding temperature at the R377W and F488L mutants was not different from that in the WT. (B). Limited tryptic digestion of the WT and R377W and F488L mutant CNGA3. The membranes prepared from cells that had been transfected with cDNAs encoding the WT and R377W and F488L mutants were incubated with trypsin-TPCK (30 μg/ml) at 30°C for 2, 5, and 10 min. The digested products were resolved on 10% SDS-PAGE, followed by Western blotting using the polyclonal anti-CNGA3 antibody. Shown are representative images showing limited proteolysis of the WT and mutant CNGA3 subunits. The cleavage rates of the mutants to trypsin were about the same as the WT.

    Techniques Used: Mutagenesis, Transfection, Incubation, SDS Page, Western Blot

    Related Articles

    Modification:

    Article Title: Single-cell transcriptome of bronchoalveolar lavage fluid reveals sequential change of macrophages during SARS-CoV-2 infection in ferrets
    Article Snippet: .. SARS-CoV-2 strain NMC-nCoV02 was propagated in Vero cells in Dulbecco’s Modified Eagle Medium (DMEM; GIBCO, NY, US, 11-995-040) supplemented with 1% penicillin/streptomycin (GIBCO, 15140-122) and TPCK-treated trypsin (0.5 μg/mL; Worthington Biochemical, NJ, US, TRSEQZ) in a 37 °C incubator with 5% CO2 for 72 h. The propagated virus was then stored at −80 °C, and used as the working stock for animal studies. ..

    Infection:

    Article Title: Prevalence of Neutralising Antibodies to HCoV-NL63 in Healthy Adults in Australia
    Article Snippet: .. HCoV-NL63 (Amsterdam-1 strain) was used to infect LLC-MK2 (ATCC, CCL-7) cells at a multiplicity of infection of 0.1 in OptiMEM/2% fetal calf serum/1% antibiotic–antimycotic (Thermo Fisher Scientific, Scoresby, VIC, Australia) supplemented with 1 µg/mL tosyl phenylalanyl chloromethyl ketone (TPCK)-treated trypsin (Worthington Biochemical, Lakewood, NJ, USA). ..

    Article Title: Mutation E48K in PB1 Polymerase Subunit Improves Stability of a Candidate Live Attenuated Influenza B Virus Vaccine
    Article Snippet: .. MDCK cells at approximately 90% confluency in 24-well plates were infected at a multiplicity of infection (MOI) of 0.01 of each virus in Opti-MEM (Thermo Fisher Scientific, Waltham, MA, USA) containing 1 μg/mL TPCK-trypsin (Worthington Biochemicals, Lakewood, NJ, USA) and 1% antibiotic/antimycotic solution (Sigma-Aldrich St. Louis, MO, USA). ..

    Article Title: Reprogrammed CRISPR-Cas13b suppresses SARS-CoV-2 replication and circumvents its mutational escape through mismatch tolerance
    Article Snippet: .. VERO cells expressing pspCas14b-BFP and various crRNAs were then infected in a level 3 containment laboratory with 200 μL of the ancestral, D614G, or the B.1.1.7 (known as the UK variant) SARS-CoV-2 virus isolate, a kind gift from Dr. Julian Druce (Victoria Infectious Disease Reference Lab, VIDRL) at MOI of 0.1 or 0.01 in DMEM containing Penicillin/Streptomycin, L-Glutamine and 1 μg/mL TPCK-treated trypsin (LS003740, Worthington) to facilitate Spike cleavage and cell entry of the virus. ..

    Article Title: Reprogrammed CRISPR-Cas13b suppresses SARS-CoV-2 replication and circumvents its mutational escape through mismatch tolerance
    Article Snippet: .. Calu-3 cells expressing pspCas13b-BFP and various crRNAs were infected with 200 μL of the ancestral virus isolate with 104 TCID50/mL in DMEM containing 1% FBS, Penicillin/Streptomycin, L-Glutamine and 1 μg/mL TPCK-treated trypsin. ..

    Expressing:

    Article Title: Structure-Based Optimization of ML300-Derived, Noncovalent Inhibitors Targeting the Severe Acute Respiratory Syndrome Coronavirus 3CL Protease (SARS-CoV-2 3CLpro)
    Article Snippet: .. The virus was propagated in Vero E6 cells expressing the ACE2 receptor (a gift from Y. Choi, Cleveland Clinic Lerner Research Institute) in DMEM supplemented with 1× penicillin-streptomycin (Gibco) and 0.5 μg/mL TPCK-treated trypsin (Worthington Biochemical) at 37 °C in a humidified incubator with 5% CO2. ..

    Article Title: Reprogrammed CRISPR-Cas13b suppresses SARS-CoV-2 replication and circumvents its mutational escape through mismatch tolerance
    Article Snippet: .. VERO cells expressing pspCas14b-BFP and various crRNAs were then infected in a level 3 containment laboratory with 200 μL of the ancestral, D614G, or the B.1.1.7 (known as the UK variant) SARS-CoV-2 virus isolate, a kind gift from Dr. Julian Druce (Victoria Infectious Disease Reference Lab, VIDRL) at MOI of 0.1 or 0.01 in DMEM containing Penicillin/Streptomycin, L-Glutamine and 1 μg/mL TPCK-treated trypsin (LS003740, Worthington) to facilitate Spike cleavage and cell entry of the virus. ..

    Article Title: Reprogrammed CRISPR-Cas13b suppresses SARS-CoV-2 replication and circumvents its mutational escape through mismatch tolerance
    Article Snippet: .. Calu-3 cells expressing pspCas13b-BFP and various crRNAs were infected with 200 μL of the ancestral virus isolate with 104 TCID50/mL in DMEM containing 1% FBS, Penicillin/Streptomycin, L-Glutamine and 1 μg/mL TPCK-treated trypsin. ..

    Concentration Assay:

    Article Title: Quantitative Tyrosine Phosphoproteome Profiling of AXL Receptor Tyrosine Kinase Signaling Network
    Article Snippet: .. Briefly, the protein lysates were reduced with 5 mM dithiothreitol at 37 °C for 1 h and alkylated with 10 mM iodoacetamide at RT in the dark for 30 min. After reduction and alkylation, the protein lysates were diluted in 20 mM HEPES pH 8.0 to a final concentration < 2 M urea and were subjected to in-solution protease digestion using TPCK-treated trypsin (Worthington Biochemical Corp. Lakewood, NJ, USA) on an orbital shaker overnight at room temperature. ..

    Variant Assay:

    Article Title: Reprogrammed CRISPR-Cas13b suppresses SARS-CoV-2 replication and circumvents its mutational escape through mismatch tolerance
    Article Snippet: .. VERO cells expressing pspCas14b-BFP and various crRNAs were then infected in a level 3 containment laboratory with 200 μL of the ancestral, D614G, or the B.1.1.7 (known as the UK variant) SARS-CoV-2 virus isolate, a kind gift from Dr. Julian Druce (Victoria Infectious Disease Reference Lab, VIDRL) at MOI of 0.1 or 0.01 in DMEM containing Penicillin/Streptomycin, L-Glutamine and 1 μg/mL TPCK-treated trypsin (LS003740, Worthington) to facilitate Spike cleavage and cell entry of the virus. ..

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  • 99
    Worthington Biochemical trypsin tpck
    The R377W and F488L mutations do not affect protein stability. (A). Thermal denaturation study of the WT and R377W and F488L mutant C-termini. Shown are thermal denaturation curves for the WT and mutant C-termini obtained at 220 nm from 20°C to 80°C (GST, black; WT, blue; R377W, green; and F488L, red). Denaturation curves are in units of molar ellipticity vs. temperature. The transition temperature was at ∼ 59°C for GST and was at ∼ 68°C for the C-terminal fusion proteins. The unfolding temperature at the R377W and F488L mutants was not different from that in the WT. (B). Limited tryptic digestion of the WT and R377W and F488L mutant CNGA3. The membranes prepared from cells that had been <t>transfected</t> with cDNAs encoding the WT and R377W and F488L mutants were incubated with <t>trypsin-TPCK</t> (30 μg/ml) at 30°C for 2, 5, and 10 min. The digested products were resolved on 10% SDS-PAGE, followed by Western blotting using the polyclonal anti-CNGA3 antibody. Shown are representative images showing limited proteolysis of the WT and mutant CNGA3 subunits. The cleavage rates of the mutants to trypsin were about the same as the WT.
    Trypsin Tpck, supplied by Worthington Biochemical, used in various techniques. Bioz Stars score: 99/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/trypsin tpck/product/Worthington Biochemical
    Average 99 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    trypsin tpck - by Bioz Stars, 2021-10
    99/100 stars
      Buy from Supplier

    98
    Worthington Biochemical deoxyribonuclease i
    The R377W and F488L mutations do not affect protein stability. (A). Thermal denaturation study of the WT and R377W and F488L mutant C-termini. Shown are thermal denaturation curves for the WT and mutant C-termini obtained at 220 nm from 20°C to 80°C (GST, black; WT, blue; R377W, green; and F488L, red). Denaturation curves are in units of molar ellipticity vs. temperature. The transition temperature was at ∼ 59°C for GST and was at ∼ 68°C for the C-terminal fusion proteins. The unfolding temperature at the R377W and F488L mutants was not different from that in the WT. (B). Limited tryptic digestion of the WT and R377W and F488L mutant CNGA3. The membranes prepared from cells that had been <t>transfected</t> with cDNAs encoding the WT and R377W and F488L mutants were incubated with <t>trypsin-TPCK</t> (30 μg/ml) at 30°C for 2, 5, and 10 min. The digested products were resolved on 10% SDS-PAGE, followed by Western blotting using the polyclonal anti-CNGA3 antibody. Shown are representative images showing limited proteolysis of the WT and mutant CNGA3 subunits. The cleavage rates of the mutants to trypsin were about the same as the WT.
    Deoxyribonuclease I, supplied by Worthington Biochemical, used in various techniques. Bioz Stars score: 98/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/deoxyribonuclease i/product/Worthington Biochemical
    Average 98 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    deoxyribonuclease i - by Bioz Stars, 2021-10
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    94
    Worthington Biochemical mg ml 1 collagenase
    The R377W and F488L mutations do not affect protein stability. (A). Thermal denaturation study of the WT and R377W and F488L mutant C-termini. Shown are thermal denaturation curves for the WT and mutant C-termini obtained at 220 nm from 20°C to 80°C (GST, black; WT, blue; R377W, green; and F488L, red). Denaturation curves are in units of molar ellipticity vs. temperature. The transition temperature was at ∼ 59°C for GST and was at ∼ 68°C for the C-terminal fusion proteins. The unfolding temperature at the R377W and F488L mutants was not different from that in the WT. (B). Limited tryptic digestion of the WT and R377W and F488L mutant CNGA3. The membranes prepared from cells that had been <t>transfected</t> with cDNAs encoding the WT and R377W and F488L mutants were incubated with <t>trypsin-TPCK</t> (30 μg/ml) at 30°C for 2, 5, and 10 min. The digested products were resolved on 10% SDS-PAGE, followed by Western blotting using the polyclonal anti-CNGA3 antibody. Shown are representative images showing limited proteolysis of the WT and mutant CNGA3 subunits. The cleavage rates of the mutants to trypsin were about the same as the WT.
    Mg Ml 1 Collagenase, supplied by Worthington Biochemical, 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/mg ml 1 collagenase/product/Worthington Biochemical
    Average 94 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    mg ml 1 collagenase - by Bioz Stars, 2021-10
    94/100 stars
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    Image Search Results


    The R377W and F488L mutations do not affect protein stability. (A). Thermal denaturation study of the WT and R377W and F488L mutant C-termini. Shown are thermal denaturation curves for the WT and mutant C-termini obtained at 220 nm from 20°C to 80°C (GST, black; WT, blue; R377W, green; and F488L, red). Denaturation curves are in units of molar ellipticity vs. temperature. The transition temperature was at ∼ 59°C for GST and was at ∼ 68°C for the C-terminal fusion proteins. The unfolding temperature at the R377W and F488L mutants was not different from that in the WT. (B). Limited tryptic digestion of the WT and R377W and F488L mutant CNGA3. The membranes prepared from cells that had been transfected with cDNAs encoding the WT and R377W and F488L mutants were incubated with trypsin-TPCK (30 μg/ml) at 30°C for 2, 5, and 10 min. The digested products were resolved on 10% SDS-PAGE, followed by Western blotting using the polyclonal anti-CNGA3 antibody. Shown are representative images showing limited proteolysis of the WT and mutant CNGA3 subunits. The cleavage rates of the mutants to trypsin were about the same as the WT.

    Journal: Biochemistry

    Article Title: The Disease-Causing Mutations in the Carboxyl-Terminus of Cone Cyclic Nucleotide-Gated Channel CNGA3 Subunit Alter the Local Secondary Structure and Interfere with the Channel Active Conformational Change

    doi: 10.1021/bi901960u

    Figure Lengend Snippet: The R377W and F488L mutations do not affect protein stability. (A). Thermal denaturation study of the WT and R377W and F488L mutant C-termini. Shown are thermal denaturation curves for the WT and mutant C-termini obtained at 220 nm from 20°C to 80°C (GST, black; WT, blue; R377W, green; and F488L, red). Denaturation curves are in units of molar ellipticity vs. temperature. The transition temperature was at ∼ 59°C for GST and was at ∼ 68°C for the C-terminal fusion proteins. The unfolding temperature at the R377W and F488L mutants was not different from that in the WT. (B). Limited tryptic digestion of the WT and R377W and F488L mutant CNGA3. The membranes prepared from cells that had been transfected with cDNAs encoding the WT and R377W and F488L mutants were incubated with trypsin-TPCK (30 μg/ml) at 30°C for 2, 5, and 10 min. The digested products were resolved on 10% SDS-PAGE, followed by Western blotting using the polyclonal anti-CNGA3 antibody. Shown are representative images showing limited proteolysis of the WT and mutant CNGA3 subunits. The cleavage rates of the mutants to trypsin were about the same as the WT.

    Article Snippet: The membranes prepared from cells that had been transfected with cDNAs for the WT and mutants were incubated with trypsin-TPCK (30 μg/ml) at 30°C for 2, 5, and 10 min.

    Techniques: Mutagenesis, Transfection, Incubation, SDS Page, Western Blot