tlck treated bovine α chymotrypsin  (Worthington Biochemical)


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    Name:
    Trypsin
    Description:
    Supplied as dialyzed and lyophilized powder
    Catalog Number:
    LS003702
    Price:
    23
    Source:
    Bovine Pancreas
    Size:
    100 mg
    Cas Number:
    9002.07.7
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    Structured Review

    Worthington Biochemical tlck treated bovine α chymotrypsin
    Supplied as dialyzed and lyophilized powder
    https://www.bioz.com/result/tlck treated bovine α chymotrypsin/product/Worthington Biochemical
    Average 99 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    tlck treated bovine α chymotrypsin - by Bioz Stars, 2021-05
    99/100 stars

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    Related Articles

    Purification:

    Article Title: Differential Induction of Type I and Type III Interferons by Swine and Human Origin H1N1 Influenza A Viruses in Porcine Airway Epithelial Cells
    Article Snippet: The swine influenza viruses; A/Sw/Illinois/2008 (H1N1 IL/08), A/Sw/Iowa/2004 (H1N1 IA/04), and A (H3N2) variant virus (H3N2v), and the human pandemic influenza A/California/04/2009 (pH1N1 CA/09) were obtained from the University of Minnesota Veterinary Diagnostic Laboratory (St Paul, MN). .. Viruses were propagated in MDCK cells in DMEM containing 0.5 μg/ml TPCK-trypsin (Worthington Biochemical Corporation, Lakewood, NJ) and purified from the clarified cell culture supernatants by ultracentrifugation through a 30% (w/v) sucrose cushion and stored in aliquots at -80o C. Culture supernatant from un-infected MDCK cells were processed similarly to use for mock infection. .. Isolation of primary pAECs Primary pAECs were isolated from three healthy neonatal pigs as described previously [ ] with slight modifications.

    Article Title: The analysis of macromolecular interactions by sedimentation equilibrium
    Article Snippet: .. Purified α-chymotrypsin (Cat. No. 1475) and soybean trypsin inhibitor (STI) (Cat. No. 3570) were purchased from Worthington Biochemical Corporation. .. Approximately 21 mg of each were dissolved in 0.2M sodium chloride and 0.05M sodium phosphate (pH = 6.7) and further purified by size exclusion chromatography on a HiPrep 16/60 Sephacryl S-200 HR column (Cat. No. 17-1166-01, GE Healthcare) at 0.5 mL/min in the same buffer.

    Cell Culture:

    Article Title: Differential Induction of Type I and Type III Interferons by Swine and Human Origin H1N1 Influenza A Viruses in Porcine Airway Epithelial Cells
    Article Snippet: The swine influenza viruses; A/Sw/Illinois/2008 (H1N1 IL/08), A/Sw/Iowa/2004 (H1N1 IA/04), and A (H3N2) variant virus (H3N2v), and the human pandemic influenza A/California/04/2009 (pH1N1 CA/09) were obtained from the University of Minnesota Veterinary Diagnostic Laboratory (St Paul, MN). .. Viruses were propagated in MDCK cells in DMEM containing 0.5 μg/ml TPCK-trypsin (Worthington Biochemical Corporation, Lakewood, NJ) and purified from the clarified cell culture supernatants by ultracentrifugation through a 30% (w/v) sucrose cushion and stored in aliquots at -80o C. Culture supernatant from un-infected MDCK cells were processed similarly to use for mock infection. .. Isolation of primary pAECs Primary pAECs were isolated from three healthy neonatal pigs as described previously [ ] with slight modifications.

    Infection:

    Article Title: Differential Induction of Type I and Type III Interferons by Swine and Human Origin H1N1 Influenza A Viruses in Porcine Airway Epithelial Cells
    Article Snippet: The swine influenza viruses; A/Sw/Illinois/2008 (H1N1 IL/08), A/Sw/Iowa/2004 (H1N1 IA/04), and A (H3N2) variant virus (H3N2v), and the human pandemic influenza A/California/04/2009 (pH1N1 CA/09) were obtained from the University of Minnesota Veterinary Diagnostic Laboratory (St Paul, MN). .. Viruses were propagated in MDCK cells in DMEM containing 0.5 μg/ml TPCK-trypsin (Worthington Biochemical Corporation, Lakewood, NJ) and purified from the clarified cell culture supernatants by ultracentrifugation through a 30% (w/v) sucrose cushion and stored in aliquots at -80o C. Culture supernatant from un-infected MDCK cells were processed similarly to use for mock infection. .. Isolation of primary pAECs Primary pAECs were isolated from three healthy neonatal pigs as described previously [ ] with slight modifications.

    Article Title: Unique Type I Interferon Responses Determine the Functional Fate of Migratory Lung Dendritic Cells during Influenza Virus Infection
    Article Snippet: Supporting Information Migratory DCs can transfer infectious virus to uninfected cells in the absence of TPCK-trypsin. .. A. MLN-DCs (gate V, ) from PR8 or WSN infected mice (day 3) were co-cultured with MDCK cells in the presence or absence of TPCK-trypsin for 2 days. .. Virus replication was assessed by HRP-based immunostaining of MDCK cells with a chicken polyclonal antibody to influenza virus.

    other:

    Article Title: Exploring protein interfaces with a general photochemical reagent
    Article Snippet: Complete enzymatic digestion of these carbamidomethylated samples with TPCK trypsin was achieved in NH4 CO3 H (0.1 M at pH 8.0), after 12–24 h at 37°C using a 2% (w/w) enzyme:substrate ratio.

    Article Title: Unique Type I Interferon Responses Determine the Functional Fate of Migratory Lung Dendritic Cells during Influenza Virus Infection
    Article Snippet: Supporting Information Migratory DCs can transfer infectious virus to uninfected cells in the absence of TPCK-trypsin.

    Incubation:

    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
    Article Snippet: Incubation of MHV-A59 virions at pH 6.5 and 37°C with soluble murine receptor glycoproteins CEACAM1a[1-4] (Fig. ) or the corresponding two-domain isoform smCEACAM1a[1,4] (data not shown) followed by trypsin-TPCK digestion at 4°C resulted in degradation of the S2 protein but not of the S1 protein. .. 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. ). ..

    Mouse Assay:

    Article Title: Unique Type I Interferon Responses Determine the Functional Fate of Migratory Lung Dendritic Cells during Influenza Virus Infection
    Article Snippet: Supporting Information Migratory DCs can transfer infectious virus to uninfected cells in the absence of TPCK-trypsin. .. A. MLN-DCs (gate V, ) from PR8 or WSN infected mice (day 3) were co-cultured with MDCK cells in the presence or absence of TPCK-trypsin for 2 days. .. Virus replication was assessed by HRP-based immunostaining of MDCK cells with a chicken polyclonal antibody to influenza virus.

    Article Title: Unique Type I Interferon Responses Determine the Functional Fate of Migratory Lung Dendritic Cells during Influenza Virus Infection
    Article Snippet: Control wells were stained with chicken normal serum followed by HRP-based immunostaining. .. B. Sorted CD103+ DCs and CD11bhigh DCs from PR8 or WSN-infected mice were co-cultured with MDCK cells in the presence or absence of TPCK-trypsin and the culture supernatants were assayed for infectious virus particles at day 2 by hemmaglutination of RBCs. (PDF) Click here for additional data file. .. Sorting strategy to isolate LN-resident CD8α+ DCs during influenza virus infection.

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  • 93
    Worthington Biochemical α chymotrypsin
    STI and <t>α-chymotrypsin</t> interact to form 1:1 and 1:2 complexes
    α Chymotrypsin, 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/α chymotrypsin/product/Worthington Biochemical
    Average 93 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    α chymotrypsin - by Bioz Stars, 2021-05
    93/100 stars
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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:

    L1793P and E1883K mutant myosin filaments show altered stability compared with wild-type. ( A ) SDS-PAGE separation of wild-type and mutant filaments subjected to α-chymotrypsin proteolysis with samples collected at various time points during the reaction. Proteolysis of full-length (FL) myosin filaments yields ∼130 kD sized rod fragments and ∼90 kD S1 head fragments within 5–10 min. After 30-60 min of digestion, additional cleaved products originating from the rod fragments are apparent. Wild-type and R1845W myosins show one truncated rod fragment while the L1793P and E1883K myosins show three, indicative of reduced stability. Extended proteolysis of 120 min does not yield any new truncated products for wild-type or R1845W myosins. ( B ) Un-Scan-It peak profiles of protein bands detected in the electrophoresed gels at baseline (0 min), 60 and 120 min after proteolysis. Peak analyses of digested wild-type and R1845W mutant myosin filaments corroborated presence of one truncated rod peak, while those of the L1793P and E1883K mutants confirmed the presence of three truncated fragments in addition to the intact rod fragment (designated by arrows in the right panel).

    Journal: Human Molecular Genetics

    Article Title: Myosin storage myopathy mutations yield defective myosin filament assembly in vitro and disrupted myofibrillar structure and function in vivo

    doi: 10.1093/hmg/ddx359

    Figure Lengend Snippet: L1793P and E1883K mutant myosin filaments show altered stability compared with wild-type. ( A ) SDS-PAGE separation of wild-type and mutant filaments subjected to α-chymotrypsin proteolysis with samples collected at various time points during the reaction. Proteolysis of full-length (FL) myosin filaments yields ∼130 kD sized rod fragments and ∼90 kD S1 head fragments within 5–10 min. After 30-60 min of digestion, additional cleaved products originating from the rod fragments are apparent. Wild-type and R1845W myosins show one truncated rod fragment while the L1793P and E1883K myosins show three, indicative of reduced stability. Extended proteolysis of 120 min does not yield any new truncated products for wild-type or R1845W myosins. ( B ) Un-Scan-It peak profiles of protein bands detected in the electrophoresed gels at baseline (0 min), 60 and 120 min after proteolysis. Peak analyses of digested wild-type and R1845W mutant myosin filaments corroborated presence of one truncated rod peak, while those of the L1793P and E1883K mutants confirmed the presence of three truncated fragments in addition to the intact rod fragment (designated by arrows in the right panel).

    Article Snippet: Myosin filament samples were digested with α-chymotrypsin (0.05 mg/ml; Worthington Biochemical) for 0 to 120 min. A 5 µl sample volume of the digestion mixture was taken out at specific time points, diluted in 5X SB buffer and denatured at 95 °C for 5 min.

    Techniques: Mutagenesis, SDS Page

    Dependence of the natural logarithm of the association equilibrium constant of soybean trypsin inhibitor with α-chymotrypsin as a function of TMAO concentration (top row), urea concentration (middle row), and TMAO concentration in the presence of 1 M urea (bottom row). Dotted lines indicate the best-fit of a straight line to each set of data. The error bars represent one standard deviation.

    Journal: The journal of physical chemistry. B

    Article Title: Compensating Effects of Urea and Trimethylamine-N-Oxide on the Heteroassociation of α-Chymotrypsin and Soybean Trypsin Inhibitor

    doi: 10.1021/jp4006923

    Figure Lengend Snippet: Dependence of the natural logarithm of the association equilibrium constant of soybean trypsin inhibitor with α-chymotrypsin as a function of TMAO concentration (top row), urea concentration (middle row), and TMAO concentration in the presence of 1 M urea (bottom row). Dotted lines indicate the best-fit of a straight line to each set of data. The error bars represent one standard deviation.

    Article Snippet: α-Chymotrypsin (MW 25K), soybean trypsin inhibitor (MW 21.5K), and ovalbumin (MW 45K) were obtained from Worthington Biochemical Corporation ( , , and , respectively).

    Techniques: Concentration Assay, Standard Deviation

    Characterization of a 2:1  α -chymotrypsin/soybean trypsin inhibitor interaction at neutral pH as a function of temperature. Data are presented as  r avg  versus mole fraction of 0–1, with the mole fraction being the total molar concentration

    Journal: Biophysical Journal

    Article Title: Free-Solution, Label-Free Protein-Protein Interactions Characterized by Dynamic Light Scattering

    doi: 10.1016/j.bpj.2009.09.061

    Figure Lengend Snippet: Characterization of a 2:1 α -chymotrypsin/soybean trypsin inhibitor interaction at neutral pH as a function of temperature. Data are presented as r avg versus mole fraction of 0–1, with the mole fraction being the total molar concentration

    Article Snippet: We chose to work with proteins that were inexpensive and commercially available. α -chymotrypsin (25.5 kDa) and soybean trypsin inhibitor (Kunitz type, rather than Bowman-Birk type) (21.5 kDa) were obtained from Worthington Biochemical (Lakewood, NJ).

    Techniques: Concentration Assay

    Characterization of α -chymotrypsin dimerization as a function of acidic buffer salinity. ( a ) Average hydrodynamic radius as a function of α -chymotrypsin concentration. Symbols represent measured data, fits are shown as solid lines, and

    Journal: Biophysical Journal

    Article Title: Free-Solution, Label-Free Protein-Protein Interactions Characterized by Dynamic Light Scattering

    doi: 10.1016/j.bpj.2009.09.061

    Figure Lengend Snippet: Characterization of α -chymotrypsin dimerization as a function of acidic buffer salinity. ( a ) Average hydrodynamic radius as a function of α -chymotrypsin concentration. Symbols represent measured data, fits are shown as solid lines, and

    Article Snippet: We chose to work with proteins that were inexpensive and commercially available. α -chymotrypsin (25.5 kDa) and soybean trypsin inhibitor (Kunitz type, rather than Bowman-Birk type) (21.5 kDa) were obtained from Worthington Biochemical (Lakewood, NJ).

    Techniques: Concentration Assay

    Characterization of a 1:1  α -chymotrypsin/bovine pancreatic trypsin inhibitor interaction at neutral pH at two temperatures. The profile expected for no association is shown by the dotted line. Fits are shown as solid lines. ( Inset ) Negative control

    Journal: Biophysical Journal

    Article Title: Free-Solution, Label-Free Protein-Protein Interactions Characterized by Dynamic Light Scattering

    doi: 10.1016/j.bpj.2009.09.061

    Figure Lengend Snippet: Characterization of a 1:1 α -chymotrypsin/bovine pancreatic trypsin inhibitor interaction at neutral pH at two temperatures. The profile expected for no association is shown by the dotted line. Fits are shown as solid lines. ( Inset ) Negative control

    Article Snippet: We chose to work with proteins that were inexpensive and commercially available. α -chymotrypsin (25.5 kDa) and soybean trypsin inhibitor (Kunitz type, rather than Bowman-Birk type) (21.5 kDa) were obtained from Worthington Biochemical (Lakewood, NJ).

    Techniques: Negative Control