trypsin  (Worthington Biochemical)


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    Structured Review

    Worthington Biochemical trypsin
    Trypsin, supplied by Worthington Biochemical, used in various techniques. Bioz Stars score: 92/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/trypsin/product/Worthington Biochemical
    Average 92 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    trypsin - by Bioz Stars, 2021-09
    92/100 stars

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    other:

    Article Title: Uterine Selection of Human Embryos at Implantation
    Article Snippet: Trypsin (TRLS, Cat# LS003734) and soybean trypsin inhibitor (SI, Cat# LS003570) were purchased from Worthington Biochemical Corp., Lakewood, NJ, USA).

    Article Title: Cell-specific ablation of Hsp47 defines the collagen-producing cells in the injured heart
    Article Snippet: The ventricles were then enzymatically digested using 84 U/ml collagenase type I (Worthington, LS005273) and trypsin (Worthington, LS003736).

    Mouse Assay:

    Article Title: Quantitative Profiling of Peptides from RNAs classified as non-coding
    Article Snippet: .. Mouse cortical cultures Cortices of the mice embryos (C57BL/6, Charles River) at stage E16.5 were dissected and dissociated in 1× Hank’s Balanced Salt Solution (HBSS) (14175-046, Life Technologies), 100 mM MgCl2, 10 mM Kynurenic acid, 100 mM HEPES, 20 mg/ml trypsin (LS003736, Worthington Biochemicals) and 0.32 mg/ml L-cysteine (C7352, Sigma) for 10 min. Trypsin treatment to dissociate cells was terminated with three 2 min washes in 1× HBSS with 10 mg/ml trypsin inhibitor (T6522, Sigma). ..

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    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: 97/100, 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 97 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    soybean trypsin inhibitor sti - by Bioz Stars, 2021-09
    97/100 stars
      Buy from Supplier

    99
    Worthington Biochemical trypsin tpck
    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 <t>4°C</t> for 20 min with <t>trypsin-TPCK</t> 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.
    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, 2021-09
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    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:

    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

    (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

    Migratory CD103 + DCs are the major cell type carrying infectious virus particles to the MLNs. A–C. Isolation of different MLN cell populations from influenza infected mice by cell sorting. A. Live gate for total MLN leukocytes shown as CD45 + DAPI - cells (gate II). B. Sorting strategy to obtain total migratory DCs (gate V), individual CD103 + DCs (gate VI), or CD11b high DCs (gate VII), and non-DC MLN cells by pooling gates i, ii, and iii during collection. All these cell populations were selected from the total CD45 + live cell gate I. C. Alternative sorting strategy starting with gate II, to obtain B220 + cells (gate B), Gr1 + cells (gate G), and pDCs (gate P2). D. Total migratory DCs (gate V) comprised of CD103 + DCs and CD11b high DCs, or MLN non-DC cells (gates I, ii, and iii pooled) sorted at 3 dpi, were layered over MDCK cells in a 1∶2 serial dilution, starting with 14,000 and 500,000 cells respectively, and were co-cultured in the presence of TPCK-trypsin for 3 days. Supernatants were assayed for infectious virus particles by hemagglutination of RBCs. D'. Supernatants from MLN-DC/MDCK co-cultures were assayed for infectious virus by plaque immunostaining on MDCK cells. E. Immunofluorescence of intracellular viral NP of sorted CD103 + DCs and CD11b high DCs from infected mice at 3 dpi. F. Individual cell populations, isolated by sorting at day 3 and 4 post-infection, as described above, were injected into 10-day old embryonated eggs, and 2 days later, allantoic fluid was assayed for infectious virus particles by hemagglutination of RBCs. Each cell type at each time point was assayed in triplicate. F’. Allantoic fluid from eggs injected with CD103 + DCs was assayed for infectious virus particles by a plaque immunostaining assay on MDCK cells.

    Journal: PLoS Pathogens

    Article Title: Unique Type I Interferon Responses Determine the Functional Fate of Migratory Lung Dendritic Cells during Influenza Virus Infection

    doi: 10.1371/journal.ppat.1002345

    Figure Lengend Snippet: Migratory CD103 + DCs are the major cell type carrying infectious virus particles to the MLNs. A–C. Isolation of different MLN cell populations from influenza infected mice by cell sorting. A. Live gate for total MLN leukocytes shown as CD45 + DAPI - cells (gate II). B. Sorting strategy to obtain total migratory DCs (gate V), individual CD103 + DCs (gate VI), or CD11b high DCs (gate VII), and non-DC MLN cells by pooling gates i, ii, and iii during collection. All these cell populations were selected from the total CD45 + live cell gate I. C. Alternative sorting strategy starting with gate II, to obtain B220 + cells (gate B), Gr1 + cells (gate G), and pDCs (gate P2). D. Total migratory DCs (gate V) comprised of CD103 + DCs and CD11b high DCs, or MLN non-DC cells (gates I, ii, and iii pooled) sorted at 3 dpi, were layered over MDCK cells in a 1∶2 serial dilution, starting with 14,000 and 500,000 cells respectively, and were co-cultured in the presence of TPCK-trypsin for 3 days. Supernatants were assayed for infectious virus particles by hemagglutination of RBCs. D'. Supernatants from MLN-DC/MDCK co-cultures were assayed for infectious virus by plaque immunostaining on MDCK cells. E. Immunofluorescence of intracellular viral NP of sorted CD103 + DCs and CD11b high DCs from infected mice at 3 dpi. F. Individual cell populations, isolated by sorting at day 3 and 4 post-infection, as described above, were injected into 10-day old embryonated eggs, and 2 days later, allantoic fluid was assayed for infectious virus particles by hemagglutination of RBCs. Each cell type at each time point was assayed in triplicate. F’. Allantoic fluid from eggs injected with CD103 + DCs was assayed for infectious virus particles by a plaque immunostaining assay on MDCK cells.

    Article Snippet: Supporting Information Migratory DCs can transfer infectious virus to uninfected cells in the absence of TPCK-trypsin.

    Techniques: Isolation, Infection, Mouse Assay, FACS, Serial Dilution, Cell Culture, Immunostaining, Immunofluorescence, Injection