bovine α chymotrypsin  (Millipore)


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    Name:
    Chymotrypsin
    Description:
    This product is provided as delivered and specified by the issuing Pharmacopoeia All information provided in support of this product including SDS and any product information leaflets have been developed and issued under the Authority of the Issuing Pharmacopoeia For further information and support please go to the website of the issuing Pharmacopoeia
    Catalog Number:
    c2160000
    Price:
    None
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    Structured Review

    Millipore bovine α chymotrypsin
    The 3D model of Atx—yPDI complex. (A) Covalent complex of sulfo-SBED-Atx and yPDI was digested with <t>α-chymotrypsin</t> and 10% of the reaction mixture (whole sample) was chromatographed on a Chrompack C18 (100 × 3.0 mm) HPLC column (red line) equilibrated in 0.1% (v/v) TFA and eluted with a gradient of 0.1% (v/v) TFA containing 90% (v/v) acetonitrile. From the rest of the whole sample biotin-containing peptides were isolated on avidin-beads and analysed on HPLC under identical conditions as the whole sample (blue line). Arrows point at fractions containing the major biotinylated peptides. (B) The major biotinylated peptides were identified by N-terminal sequencing. Their positions in primary structures of yPDI or Atx are marked by different colours. A colour designates yPDI and Atx peptides identified in the same fraction. Such peptides are covalently cross-linked and lie close together in the complex, at the rim of the interaction area between yPDI and Atx. (C) Modelling using rigid-body docking protocol Hex 5.1, HADDOCK procedure and experimentally defined structural restraints resulted in two solutions for Atx binding to yPDI. According to the first, Atx binds to yPDI between domains b and b’ (bb’-model or binding site), while according to the second, it binds at domains a’ and c of yPDI (a’c-model or binding site). Both solutions are displayed on the same molecule of yPDI using the PyMOL program in two views rotated by 180 o . Peptides cross-linked at Atx—yPDI interaction site mapping experiment are indicated by the same colours as in (B). Arrows point towards the active side of yPDI. Experimental details are in Materials and Methods.
    This product is provided as delivered and specified by the issuing Pharmacopoeia All information provided in support of this product including SDS and any product information leaflets have been developed and issued under the Authority of the Issuing Pharmacopoeia For further information and support please go to the website of the issuing Pharmacopoeia
    https://www.bioz.com/result/bovine α chymotrypsin/product/Millipore
    Average 99 stars, based on 26 article reviews
    Price from $9.99 to $1999.99
    bovine α chymotrypsin - by Bioz Stars, 2020-11
    99/100 stars

    Images

    1) Product Images from "On the Role of Protein Disulfide Isomerase in the Retrograde Cell Transport of Secreted Phospholipases A2"

    Article Title: On the Role of Protein Disulfide Isomerase in the Retrograde Cell Transport of Secreted Phospholipases A2

    Journal: PLoS ONE

    doi: 10.1371/journal.pone.0120692

    The 3D model of Atx—yPDI complex. (A) Covalent complex of sulfo-SBED-Atx and yPDI was digested with α-chymotrypsin and 10% of the reaction mixture (whole sample) was chromatographed on a Chrompack C18 (100 × 3.0 mm) HPLC column (red line) equilibrated in 0.1% (v/v) TFA and eluted with a gradient of 0.1% (v/v) TFA containing 90% (v/v) acetonitrile. From the rest of the whole sample biotin-containing peptides were isolated on avidin-beads and analysed on HPLC under identical conditions as the whole sample (blue line). Arrows point at fractions containing the major biotinylated peptides. (B) The major biotinylated peptides were identified by N-terminal sequencing. Their positions in primary structures of yPDI or Atx are marked by different colours. A colour designates yPDI and Atx peptides identified in the same fraction. Such peptides are covalently cross-linked and lie close together in the complex, at the rim of the interaction area between yPDI and Atx. (C) Modelling using rigid-body docking protocol Hex 5.1, HADDOCK procedure and experimentally defined structural restraints resulted in two solutions for Atx binding to yPDI. According to the first, Atx binds to yPDI between domains b and b’ (bb’-model or binding site), while according to the second, it binds at domains a’ and c of yPDI (a’c-model or binding site). Both solutions are displayed on the same molecule of yPDI using the PyMOL program in two views rotated by 180 o . Peptides cross-linked at Atx—yPDI interaction site mapping experiment are indicated by the same colours as in (B). Arrows point towards the active side of yPDI. Experimental details are in Materials and Methods.
    Figure Legend Snippet: The 3D model of Atx—yPDI complex. (A) Covalent complex of sulfo-SBED-Atx and yPDI was digested with α-chymotrypsin and 10% of the reaction mixture (whole sample) was chromatographed on a Chrompack C18 (100 × 3.0 mm) HPLC column (red line) equilibrated in 0.1% (v/v) TFA and eluted with a gradient of 0.1% (v/v) TFA containing 90% (v/v) acetonitrile. From the rest of the whole sample biotin-containing peptides were isolated on avidin-beads and analysed on HPLC under identical conditions as the whole sample (blue line). Arrows point at fractions containing the major biotinylated peptides. (B) The major biotinylated peptides were identified by N-terminal sequencing. Their positions in primary structures of yPDI or Atx are marked by different colours. A colour designates yPDI and Atx peptides identified in the same fraction. Such peptides are covalently cross-linked and lie close together in the complex, at the rim of the interaction area between yPDI and Atx. (C) Modelling using rigid-body docking protocol Hex 5.1, HADDOCK procedure and experimentally defined structural restraints resulted in two solutions for Atx binding to yPDI. According to the first, Atx binds to yPDI between domains b and b’ (bb’-model or binding site), while according to the second, it binds at domains a’ and c of yPDI (a’c-model or binding site). Both solutions are displayed on the same molecule of yPDI using the PyMOL program in two views rotated by 180 o . Peptides cross-linked at Atx—yPDI interaction site mapping experiment are indicated by the same colours as in (B). Arrows point towards the active side of yPDI. Experimental details are in Materials and Methods.

    Techniques Used: High Performance Liquid Chromatography, Isolation, Avidin-Biotin Assay, Sequencing, Binding Assay

    2) Product Images from "PROSTATE-SPECIFIC ANTIGEN IS A "CHYMOTRYPSIN-LIKE" SERINE PROTEASE WITH UNIQUE P1 SUBSTRATE SPECIFICITY"

    Article Title: PROSTATE-SPECIFIC ANTIGEN IS A "CHYMOTRYPSIN-LIKE" SERINE PROTEASE WITH UNIQUE P1 SUBSTRATE SPECIFICITY

    Journal: Biochemistry

    doi: 10.1021/bi9001858

    Surface representation of the S1 pocket of PSA ( left ) and bovine α-chymotrypsin ( right ). The P1 tyrosine residue is shown as a yellow ball-and-stick model. The polar hydroxyl moiety of the bound residue is depicted in purple. Surface colors represent
    Figure Legend Snippet: Surface representation of the S1 pocket of PSA ( left ) and bovine α-chymotrypsin ( right ). The P1 tyrosine residue is shown as a yellow ball-and-stick model. The polar hydroxyl moiety of the bound residue is depicted in purple. Surface colors represent

    Techniques Used:

    A, Sequence alignment of the 15 human kallikreins and bovine α-chymotrypsin. Only the residues spanning the S1 pocket of serine proteases are presented. The residues highlighted in yellow are critical for the P1 specificities of respective protease.
    Figure Legend Snippet: A, Sequence alignment of the 15 human kallikreins and bovine α-chymotrypsin. Only the residues spanning the S1 pocket of serine proteases are presented. The residues highlighted in yellow are critical for the P1 specificities of respective protease.

    Techniques Used: Sequencing

    Related Articles

    High Performance Liquid Chromatography:

    Article Title: Chemical glycosylation of cytochrome c improves physical and chemical protein stability
    Article Snippet: .. Chemicals Cytochrome c from equine heart (EC 232-700-9), dextran from L. mesenteroides (EC 232–6775, average Mw = 9–11 kD), trypsin from porcine pancreas, α-chymotrypsin type II from bovine pancreas, caspase 3 substrate (DEVD-pNA), caspase 9 substrate (LEHD-pNa), disuccinimidyl suberate linker, protease inhibitor cocktail, 2,2’-azino-bis(3-ethylbenzothiazoline-6-sulphonic acid) (ABTS), ammonium carbonate, dimethyl sulfoxide (DMSO), methylene chloride, acetone, and acetonitrile (HPLC grade) were from Sigma-Aldrich (St. Louis, MO). ..

    Fluorescence:

    Article Title: Pyropia yezoensis Protein Prevents Dexamethasone-Induced Myotube Atrophy in C2C12 Myotubes
    Article Snippet: .. 20S Proteasome Activity Assay The chymotrypsin-like activity of the 20S proteasome was measured by changes in the fluorescence of 7-amino-4-methylcoumarin (AMC) conjugated to the chymotrypsin peptide substrate LLVY, using a 20S proteasome activity assay kit (Chemicon, Temecula, CA, USA). .. In brief, cells were suspended in RIPA lysis buffer (50 mM Tris-HCl, pH 7.5, 150 mM sodium chloride, 0.5% sodium deoxycholate, 1% Triton X-100, 0.1% SDS, and 2 mM EDTA) containing protease inhibitors (1 mg/mL aprotinin, 1 mg/mL leupeptin, 1 mg/mL pepstatin A, 200 mM Na3 VO4 , 500 mM NaF, and 100 mM PMSF) and centrifuged at 16,000× g for 10 min at 4 °C.

    Protease Inhibitor:

    Article Title: Chemical glycosylation of cytochrome c improves physical and chemical protein stability
    Article Snippet: .. Chemicals Cytochrome c from equine heart (EC 232-700-9), dextran from L. mesenteroides (EC 232–6775, average Mw = 9–11 kD), trypsin from porcine pancreas, α-chymotrypsin type II from bovine pancreas, caspase 3 substrate (DEVD-pNA), caspase 9 substrate (LEHD-pNa), disuccinimidyl suberate linker, protease inhibitor cocktail, 2,2’-azino-bis(3-ethylbenzothiazoline-6-sulphonic acid) (ABTS), ammonium carbonate, dimethyl sulfoxide (DMSO), methylene chloride, acetone, and acetonitrile (HPLC grade) were from Sigma-Aldrich (St. Louis, MO). ..

    Purification:

    Article Title: Changes in solvent exposure reveal the kinetics and equilibria of adsorbed protein unfolding in hydrophobic interaction chromatography
    Article Snippet: .. Bovine α-lactalbumin, bovine β-lactoglobulin B, and bovine α-chymotrypsinogen A were obtained from Sigma (St. Louis, MO, USA) and used without further purification. .. The HIC media used in this study were Phenyl Sepharose™ 6 Fast Flow (low substitution), Phenyl Sepharose™ 6 Fast Flow (high substitution) and Butyl Sepharose™ 4 Fast Flow bulk resins purchased from GE Healthcare (Piscataway, NJ, USA).

    other:

    Article Title: Prion Protein Paralog Doppel Protein Interacts with Alpha-2-Macroglobulin: A Plausible Mechanism for Doppel-Mediated Neurodegeneration
    Article Snippet: Proteins Apo-transferrin, mouse albumin, aprotinin and alpha-chymotrypsin were purchased from Sigma-Aldrich (St. Louis, MO, USA).

    Activity Assay:

    Article Title: Pyropia yezoensis Protein Prevents Dexamethasone-Induced Myotube Atrophy in C2C12 Myotubes
    Article Snippet: .. 20S Proteasome Activity Assay The chymotrypsin-like activity of the 20S proteasome was measured by changes in the fluorescence of 7-amino-4-methylcoumarin (AMC) conjugated to the chymotrypsin peptide substrate LLVY, using a 20S proteasome activity assay kit (Chemicon, Temecula, CA, USA). .. In brief, cells were suspended in RIPA lysis buffer (50 mM Tris-HCl, pH 7.5, 150 mM sodium chloride, 0.5% sodium deoxycholate, 1% Triton X-100, 0.1% SDS, and 2 mM EDTA) containing protease inhibitors (1 mg/mL aprotinin, 1 mg/mL leupeptin, 1 mg/mL pepstatin A, 200 mM Na3 VO4 , 500 mM NaF, and 100 mM PMSF) and centrifuged at 16,000× g for 10 min at 4 °C.

    Article Title: New Difluoro Knoevenagel Condensates of Curcumin, Their Schiff Bases and Copper Complexes as Proteasome Inhibitors and Apoptosis Inducers in Cancer Cells
    Article Snippet: .. Purified rabbit 20S proteasome and fluorogenic substrate Suc-LLVY-AMC for the proteasomal chymotrypsin-like (CT-like) activity were obtained from Calbiochem Inc. (San Diego, CA). ..

    Activated Clotting Time Assay:

    Article Title: EC-QCL mid-IR transmission spectroscopy for monitoring dynamic changes of protein secondary structure in aqueous solution on the example of β-aggregation in alcohol-denaturated α-chymotrypsin
    Article Snippet: .. Reagents and samples Sodium phosphate monobasic dihydrate p.a. (NaH2 PO4 •2H2 O) was purchased from Fluka (Buchs, Switzerland), sodium phosphate dibasic dihydrate (Na2 HPO4 •2H2 O) BioUltra, for molecular biology, sodium hydroxide solution 50 % in water (NaOH), hydrochloric acid 37 % (HCl) ACS reagent and 2,2,2-trifluoroethanol ReagentPlus ≥99 % (TFE), were obtained from Sigma-Aldrich (Steinheim, Germany). α-Chymotrypsin from bovine pancreas (≥85 %) (aCT) was obtained by Sigma-Aldrich (Steinheim, Germany) and used as purchased. .. Ultrapure water (18 MΩ cm) used for preparation of all solutions was obtained with a Milli-Q water purification system from Millipore (Bedford, USA).

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  • 99
    Millipore bovine α chymotrypsin
    Bovine α Chymotrypsin, supplied by Millipore, used in various techniques. Bioz Stars score: 99/100, based on 26 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/bovine α chymotrypsin/product/Millipore
    Average 99 stars, based on 26 article reviews
    Price from $9.99 to $1999.99
    bovine α chymotrypsin - by Bioz Stars, 2020-11
    99/100 stars
      Buy from Supplier

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