trypsin  (Worthington Biochemical)


Bioz Verified Symbol Worthington Biochemical is a verified supplier
Bioz Manufacturer Symbol Worthington Biochemical manufactures this product  
  • Logo
  • About
  • News
  • Press Release
  • Team
  • Advisors
  • Partners
  • Contact
  • Bioz Stars
  • Bioz vStars
  • 91

    Structured Review

    Worthington Biochemical trypsin
    Trypsin, supplied by Worthington Biochemical, used in various techniques. Bioz Stars score: 91/100, based on 33 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/trypsin/product/Worthington Biochemical
    Average 91 stars, based on 33 article reviews
    Price from $9.99 to $1999.99
    trypsin - by Bioz Stars, 2022-10
    91/100 stars

    Images

    Similar Products

  • Logo
  • About
  • News
  • Press Release
  • Team
  • Advisors
  • Partners
  • Contact
  • Bioz Stars
  • Bioz vStars
  • 95
    Worthington Biochemical tosylsulfonyl phenylalanyl chloromethyl keton tpck trypsin
    Rescue of IAV using pPIG2012 and pDP2002 in PK-15/MDCK and HEK293 T/MDCK Co-culture. Co-culture of PK-15/MDCK (5:2)(A, B, C) or HEK293 T/MDCK (3:1)(D, E, F) were transfected with plasmids encoding CA04 (A, D), Ty04 (B, E), or SGML (C, F) PB2, PB1, PA, HA, NP, NA, M and NS in pPig2012 (white circles) or pDP2002 (black circles) vector overnight (14 h) using TransIT transfection reagent. The media was replaced and supplemented with <t>TPCK-trypsin.</t> Cell culture supernatants were collected at 12, 24, 48, 72, and 96 h after addition of <t>TPCK-trypsin</t> for the quantification of virus titers by TCID50 assays using the Reed-Muench method. Plotted data represents means ± standard errors. Multiple t tests with correction for multiple comparisons using Holm-Sidak method was performed to calculate P values. **
    Tosylsulfonyl Phenylalanyl Chloromethyl Keton Tpck Trypsin, supplied by Worthington Biochemical, used in various techniques. Bioz Stars score: 95/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/tosylsulfonyl phenylalanyl chloromethyl keton tpck trypsin/product/Worthington Biochemical
    Average 95 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    tosylsulfonyl phenylalanyl chloromethyl keton tpck trypsin - by Bioz Stars, 2022-10
    95/100 stars
      Buy from Supplier

    93
    Worthington Biochemical soybean trypsin inhibitor sti
    <t>STI</t> and <t>α-chymotrypsin</t> interact to form 1:1 and 1:2 complexes
    Soybean Trypsin Inhibitor Sti, supplied by Worthington Biochemical, used in various techniques. Bioz Stars score: 93/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/soybean trypsin inhibitor sti/product/Worthington Biochemical
    Average 93 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    soybean trypsin inhibitor sti - by Bioz Stars, 2022-10
    93/100 stars
      Buy from Supplier

    95
    Worthington Biochemical tpck treated trypsin
    (A–D) Time courses of in vitro phosphorylation of R-domain peptides with COOH-terminal His tags. WT (A) and mutant R-domain peptides, with Ser768 replaced by alanine (S768A; B), Ser737 replaced by alanine (S737A; C), or Ser737 and Ser768 both replaced by alanine (S737A-S768A; D), were phosphorylated with 10 nM PKA and 5 μM γ 32 P-MgATP for 0.5–60 min as indicated. Samples were subjected to <t>SDS-PAGE</t> and analyzed by autoradiography; the arrowheads indicate relative molecular mass of 28 kD. The major mobility shift (to band 3; Figs. 1 and 2 ) was seen in the WT and S768A peptides, but not in the S737A or S737A-S768A peptides. The kinetics of R-domain phosphorylation, as demonstrated by the mobility shifts, was little altered in the two S768A mutants. (E and F) Two-dimensional tryptic phosphopeptide maps of His-tagged WT and S768A R-domain peptides phosphorylated in vitro as in A and B, but for 0.5 min with 10 nM PKA and 50 μM γ 32 P-MgATP, and then subjected to SDS-PAGE and analyzed by autoradiography. The lower radioactive bands were excised, digested overnight with 50 μg/ml <t>TPCK-trypsin,</t> and the digests separated on thin layer cellulose plates by electrophoresis at pH 3.5 in the first dimension and ascending chromatography in the second dimension. O, 0rigin; left, positive; right, negative. Four spots (arrows) in the WT R domain map are absent from the S768A map, but no similarly striking differences are seen in the pattern or intensity of other spots.
    Tpck Treated Trypsin, supplied by Worthington Biochemical, used in various techniques. Bioz Stars score: 95/100, based on 2 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/tpck treated trypsin/product/Worthington Biochemical
    Average 95 stars, based on 2 article reviews
    Price from $9.99 to $1999.99
    tpck treated trypsin - by Bioz Stars, 2022-10
    95/100 stars
      Buy from Supplier

    Image Search Results


    Rescue of IAV using pPIG2012 and pDP2002 in PK-15/MDCK and HEK293 T/MDCK Co-culture. Co-culture of PK-15/MDCK (5:2)(A, B, C) or HEK293 T/MDCK (3:1)(D, E, F) were transfected with plasmids encoding CA04 (A, D), Ty04 (B, E), or SGML (C, F) PB2, PB1, PA, HA, NP, NA, M and NS in pPig2012 (white circles) or pDP2002 (black circles) vector overnight (14 h) using TransIT transfection reagent. The media was replaced and supplemented with TPCK-trypsin. Cell culture supernatants were collected at 12, 24, 48, 72, and 96 h after addition of TPCK-trypsin for the quantification of virus titers by TCID50 assays using the Reed-Muench method. Plotted data represents means ± standard errors. Multiple t tests with correction for multiple comparisons using Holm-Sidak method was performed to calculate P values. **

    Journal: Journal of virological methods

    Article Title: Development of a swine RNA polymerase I driven Influenza reverse genetics system for the rescue of type A and B Influenza viruses

    doi: 10.1016/j.jviromet.2020.114011

    Figure Lengend Snippet: Rescue of IAV using pPIG2012 and pDP2002 in PK-15/MDCK and HEK293 T/MDCK Co-culture. Co-culture of PK-15/MDCK (5:2)(A, B, C) or HEK293 T/MDCK (3:1)(D, E, F) were transfected with plasmids encoding CA04 (A, D), Ty04 (B, E), or SGML (C, F) PB2, PB1, PA, HA, NP, NA, M and NS in pPig2012 (white circles) or pDP2002 (black circles) vector overnight (14 h) using TransIT transfection reagent. The media was replaced and supplemented with TPCK-trypsin. Cell culture supernatants were collected at 12, 24, 48, 72, and 96 h after addition of TPCK-trypsin for the quantification of virus titers by TCID50 assays using the Reed-Muench method. Plotted data represents means ± standard errors. Multiple t tests with correction for multiple comparisons using Holm-Sidak method was performed to calculate P values. **

    Article Snippet: Subsequently, the media was replaced with 2 mL of Opti-MEM/AB containing 1 μg/mL tosylsulfonyl phenylalanyl chloromethyl keton (TPCK)-trypsin (Worthington Biochemicals, Lakewood, NJ).

    Techniques: Co-Culture Assay, Transfection, Plasmid Preparation, Cell Culture, Endpoint Dilution Assay

    STI and α-chymotrypsin interact to form 1:1 and 1:2 complexes

    Journal: Methods (San Diego, Calif.)

    Article Title: The analysis of macromolecular interactions by sedimentation equilibrium

    doi: 10.1016/j.ymeth.2010.12.005

    Figure Lengend Snippet: STI and α-chymotrypsin interact to form 1:1 and 1:2 complexes

    Article Snippet: Purified α-chymotrypsin (Cat. No. 1475) and soybean trypsin inhibitor (STI) (Cat. No. 3570) were purchased from Worthington Biochemical Corporation.

    Techniques:

    STI and α-chymotrypsin are monomers

    Journal: Methods (San Diego, Calif.)

    Article Title: The analysis of macromolecular interactions by sedimentation equilibrium

    doi: 10.1016/j.ymeth.2010.12.005

    Figure Lengend Snippet: STI and α-chymotrypsin are monomers

    Article Snippet: Purified α-chymotrypsin (Cat. No. 1475) and soybean trypsin inhibitor (STI) (Cat. No. 3570) were purchased from Worthington Biochemical Corporation.

    Techniques:

    (A–D) Time courses of in vitro phosphorylation of R-domain peptides with COOH-terminal His tags. WT (A) and mutant R-domain peptides, with Ser768 replaced by alanine (S768A; B), Ser737 replaced by alanine (S737A; C), or Ser737 and Ser768 both replaced by alanine (S737A-S768A; D), were phosphorylated with 10 nM PKA and 5 μM γ 32 P-MgATP for 0.5–60 min as indicated. Samples were subjected to SDS-PAGE and analyzed by autoradiography; the arrowheads indicate relative molecular mass of 28 kD. The major mobility shift (to band 3; Figs. 1 and 2 ) was seen in the WT and S768A peptides, but not in the S737A or S737A-S768A peptides. The kinetics of R-domain phosphorylation, as demonstrated by the mobility shifts, was little altered in the two S768A mutants. (E and F) Two-dimensional tryptic phosphopeptide maps of His-tagged WT and S768A R-domain peptides phosphorylated in vitro as in A and B, but for 0.5 min with 10 nM PKA and 50 μM γ 32 P-MgATP, and then subjected to SDS-PAGE and analyzed by autoradiography. The lower radioactive bands were excised, digested overnight with 50 μg/ml TPCK-trypsin, and the digests separated on thin layer cellulose plates by electrophoresis at pH 3.5 in the first dimension and ascending chromatography in the second dimension. O, 0rigin; left, positive; right, negative. Four spots (arrows) in the WT R domain map are absent from the S768A map, but no similarly striking differences are seen in the pattern or intensity of other spots.

    Journal: The Journal of General Physiology

    Article Title: Preferential Phosphorylation of R-domain Serine 768 Dampens Activation of CFTR Channels by PKA

    doi: 10.1085/jgp.200409076

    Figure Lengend Snippet: (A–D) Time courses of in vitro phosphorylation of R-domain peptides with COOH-terminal His tags. WT (A) and mutant R-domain peptides, with Ser768 replaced by alanine (S768A; B), Ser737 replaced by alanine (S737A; C), or Ser737 and Ser768 both replaced by alanine (S737A-S768A; D), were phosphorylated with 10 nM PKA and 5 μM γ 32 P-MgATP for 0.5–60 min as indicated. Samples were subjected to SDS-PAGE and analyzed by autoradiography; the arrowheads indicate relative molecular mass of 28 kD. The major mobility shift (to band 3; Figs. 1 and 2 ) was seen in the WT and S768A peptides, but not in the S737A or S737A-S768A peptides. The kinetics of R-domain phosphorylation, as demonstrated by the mobility shifts, was little altered in the two S768A mutants. (E and F) Two-dimensional tryptic phosphopeptide maps of His-tagged WT and S768A R-domain peptides phosphorylated in vitro as in A and B, but for 0.5 min with 10 nM PKA and 50 μM γ 32 P-MgATP, and then subjected to SDS-PAGE and analyzed by autoradiography. The lower radioactive bands were excised, digested overnight with 50 μg/ml TPCK-trypsin, and the digests separated on thin layer cellulose plates by electrophoresis at pH 3.5 in the first dimension and ascending chromatography in the second dimension. O, 0rigin; left, positive; right, negative. Four spots (arrows) in the WT R domain map are absent from the S768A map, but no similarly striking differences are seen in the pattern or intensity of other spots.

    Article Snippet: Gel pieces containing 32 P-labeled R-domain protein were excised from the dried SDS-polyacrylamide gel, and subjected to digestion with TPCK-treated trypsin (50 μg/ml; Worthington) as previously described ( ).

    Techniques: In Vitro, Mutagenesis, SDS Page, Autoradiography, Mobility Shift, Electrophoresis, Chromatography

    The S2 glycoprotein of mutant MHV-A59 virus S A59 H716D undergoes a conformational change and becomes susceptible to a unique trypsin cleavage event after incubation at 37°C with soluble murine CEACAM1a[1-4] at pH 6.5 or at pH 8.0 in the absence of receptor. Gradient purified S A59 H716D virions were incubated at 4 or 37°C for 30 min at pH 6.5 with soluble murine CEACAM1a[1-4] or without receptor proteins at pH 6.5 or 8.0. The samples were incubated at 4°C for 20 min with trypsin-TPCK at 10 μg/ml, subjected to SDS-PAGE, and immunoblotted with anti-S2 MAb 5B19.5. Untreated virions contained a novel subunit of S with an apparent molecular mass of 120 kDa. Incubation of the S A59 H716D virions with soluble murine CEACAM1a[1-4] at 37°C made the 180-kDa spike glycoprotein susceptible to cleavage by trypsin-TPCK at this novel site. To a lesser degree, incubation of virions at pH 8.0 and 37°C also increased the susceptibility of the S A59 H716D spike to trypsin cleavage.

    Journal: Journal of Virology

    Article Title: Conformational Changes in the Spike Glycoprotein of Murine Coronavirus Are Induced at 37?C either by Soluble Murine CEACAM1 Receptors or by pH 8

    doi: 10.1128/JVI.77.2.830-840.2003

    Figure Lengend Snippet: The S2 glycoprotein of mutant MHV-A59 virus S A59 H716D undergoes a conformational change and becomes susceptible to a unique trypsin cleavage event after incubation at 37°C with soluble murine CEACAM1a[1-4] at pH 6.5 or at pH 8.0 in the absence of receptor. Gradient purified S A59 H716D virions were incubated at 4 or 37°C for 30 min at pH 6.5 with soluble murine CEACAM1a[1-4] or without receptor proteins at pH 6.5 or 8.0. The samples were incubated at 4°C for 20 min with trypsin-TPCK at 10 μg/ml, subjected to SDS-PAGE, and immunoblotted with anti-S2 MAb 5B19.5. Untreated virions contained a novel subunit of S with an apparent molecular mass of 120 kDa. Incubation of the S A59 H716D virions with soluble murine CEACAM1a[1-4] at 37°C made the 180-kDa spike glycoprotein susceptible to cleavage by trypsin-TPCK at this novel site. To a lesser degree, incubation of virions at pH 8.0 and 37°C also increased the susceptibility of the S A59 H716D spike to trypsin cleavage.

    Article Snippet: Incubation of MHV-A59 virions with smCEACAM1a[1-4] receptor glycoprotein at 4°C did not make the S2 protein susceptible to degradation by trypsin-TPCK at 4°C (Fig. ).

    Techniques: Mutagenesis, Incubation, Purification, SDS Page

    Conformational changes in the S2 domain of MHV-A59 spike glycoprotein induced at 37°C by CEACAM1a at pH 6.5 or by the presence of pH 8.0 without receptor. A trypsin sensitivity assay was used to demonstrate conformational changes in the viral spike protein. Gradient-purified MHV-A59 virions were incubated at 4 or 37°C for 30 min at pH 6.5 with either soluble murine CEACAM1a[1-4] or CEACAM2[1,4] or without receptor proteins at pH 6.5 or 8.0. The samples were then incubated at 4°C for 20 min with trypsin-TPCK, subjected to SDS-PAGE, and immunoblotted with MAbs specific for the receptor binding S1 domain of the spike (MAb A1.9) or for the carboxyl-terminal S2 domain of the spike (MAb 5B93.7) which has been associated with membrane fusion.

    Journal: Journal of Virology

    Article Title: Conformational Changes in the Spike Glycoprotein of Murine Coronavirus Are Induced at 37?C either by Soluble Murine CEACAM1 Receptors or by pH 8

    doi: 10.1128/JVI.77.2.830-840.2003

    Figure Lengend Snippet: Conformational changes in the S2 domain of MHV-A59 spike glycoprotein induced at 37°C by CEACAM1a at pH 6.5 or by the presence of pH 8.0 without receptor. A trypsin sensitivity assay was used to demonstrate conformational changes in the viral spike protein. Gradient-purified MHV-A59 virions were incubated at 4 or 37°C for 30 min at pH 6.5 with either soluble murine CEACAM1a[1-4] or CEACAM2[1,4] or without receptor proteins at pH 6.5 or 8.0. The samples were then incubated at 4°C for 20 min with trypsin-TPCK, subjected to SDS-PAGE, and immunoblotted with MAbs specific for the receptor binding S1 domain of the spike (MAb A1.9) or for the carboxyl-terminal S2 domain of the spike (MAb 5B93.7) which has been associated with membrane fusion.

    Article Snippet: Incubation of MHV-A59 virions with smCEACAM1a[1-4] receptor glycoprotein at 4°C did not make the S2 protein susceptible to degradation by trypsin-TPCK at 4°C (Fig. ).

    Techniques: Sensitive Assay, Purification, Incubation, SDS Page, Binding Assay