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    • TRYPSIN TPCK TREATED FROM BOVINE PANCREA

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    Documents SDS COO/COA Specification Sheet
    T1426
    Sigma-Aldrich

    TRYPSIN TPCK TREATED FROM BOVINE PANCREA

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    Nacres: NA.54
    Mdl No: MFCD00082094
    Grouped product items
    SKU Pack Size Availability Price Quantity
    T1426-100MG - Available to ship on January 21, 2024
    IDR 6,951.00
    T1426-100G - Available to ship on January 06, 2024
    IDR 527,702,000.00
    T1426-1G - Available to ship on January 06, 2024
    IDR 9,298,000.00
    T1426-250MG - Available to ship on January 06, 2024
    IDR 3,074,000.00
    T1426-500MG - Available to ship on January 06, 2024
    IDR 5,397,000.00
    T1426-5G - Available to ship on January 06, 2024
    IDR 37,116,000.00
    T1426-50MG - Available to ship on January 21, 2024
    IDR 2,830.00
    Request a Bulk Order Check Availability
    Documents SDS COO/COA Specification Sheet

    Properties

    Properties
    applications diagnostic assay manufacturing
    biological source bovine pancreas
    components Trypsin consists of a single chain polypeptide of 223 amino acid residues, produced by the removal of the N-terminal hexapeptide from trypsinogen which is cleaved at the Lys - lle peptide bond. The sequence of amino acids is cross-linked by 6 disulfide bridges. This is the native form of trypsin, beta-trypsin. BETA-trypsin can be autolyzed, cleaving at the Lys - Ser residue, to produce alpha-trypsin. Trypsin is a member of the serine protease family.
    Description TRYPSIN TPCK TREATED FROM BOVINE PANCREA
    foreign activity Chymotrypsin ≤
    form 0.1 BTEE units/mg protein
    format essentially salt-free lyophilized powder
    MDM Code T1426-100MG
    Material Number T1426
    Business Unit 760
    Shipping Mode AIR
    MRP Type PD
    Local HS Code 35079000
    Legacy SIGMA
    Shelf Life 61
    Plant 6311
    Sales Org 6304

    Description

    Application

    For trypsin digestion of peptides, use a ratio of about 1:100 to 1:20 for trypsin:peptide. The typical use for this product is in removing adherent cells from a culture surface. The concentration of trypsin necessary to dislodge cells from their substrate is dependent primarily on the cell type and the age of the culture. Trypsins have also been used for the re-suspension of cells during cell culture, in proteomics research for digestion of proteins and in various in-gel digestions. Additional applications include assessing crystallization by membrane-based techniques and in a study to determine that protein folding rates and yields can be limited by the presence of kinetic traps.

    Biochem/physiol Actions

    Trypsin cleaves peptides on the C-terminal side of lysine and arginine residues. The rate of hydrolysis of this reaction is slowed if an acidic residue is on either side of the cleavage site and hydrolysis is stopped if a proline residue is on the carboxyl side of the cleavage site. The optimal pH for trypsin activity is 7-9. Trypsin can also act to cleave ester and amide linkages of synthetic derivatives of amino acids. EDTA is added to trypsin solutions as a chelating agent that neutralizes calcium and magnesium ions that obscure the peptide bonds on which trypsin acts. Removing these ions increases the enzymatic activity.

    Serine protease inhibitors, including DFP, TLCK, APMSF, AEBSEF, and aprotinin, amongst others, will inhibit Trypsin.

    Caution

    Solutions in 1 mM HCl are stable for 1 year in aliquots and stored at -20°C. The presence of Ca2+ will also diminish the self-autolysis of trypsin and maintain its stability in solution. Trypsin will also retain most of its activity in 2.0 M urea, 2.0 M guanidine HCl, or 0.1% (w/v) SDS.

    Preparation Note

    Soluble in 1 mM HCl at 1 mg/mL.
    It is also TPCK-treated and dialyzed. Treatment with L-1-Tosylamide-2-phenylethyl chloromethyl ketone (TPCK) reduces the chymotrypsin activity which is usually present in trypsin.

    Unit Definition

    One BAEE unit will produce a A253 of 0.001 per minute at pH 7.6 at 25°C using BAEE as a substrate.

    SAFETY INFORMATION

    GHS07,GHS08

    Signal Word

    Danger

    H315 - H319 - H334 - H335

    P261 - P264 - P271 - P280 - P302 + P352 - P305 + P351 + P338

    RIDADRRIDADR

    WGK Germany

    WGK 1

    Flash Point (F)

    Flash Point (C)

    Target Organs

    Respiratory system

    Risk Statement

    Supplemental Hazard Statements

    DOCUMENTATION

    Certificate of Analysis View Sample COA
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    Certificate of Origin
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