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Enzyme Trypsin Serine Lysine Protease Arginine Protease Recombinant Trypsin

Enzyme Trypsin Serine Lysine Protease Arginine Protease Recombinant Trypsin

    • Enzyme Trypsin Serine   Lysine Protease   Arginine Protease   Recombinant Trypsin
    • Enzyme Trypsin Serine   Lysine Protease   Arginine Protease   Recombinant Trypsin
    • Enzyme Trypsin Serine   Lysine Protease   Arginine Protease   Recombinant Trypsin
    • Enzyme Trypsin Serine   Lysine Protease   Arginine Protease   Recombinant Trypsin
    • Enzyme Trypsin Serine   Lysine Protease   Arginine Protease   Recombinant Trypsin
  • Enzyme Trypsin Serine   Lysine Protease   Arginine Protease   Recombinant Trypsin

    Product Details:

    Place of Origin: China
    Brand Name: YaxinBio
    Certification: ISO 9001 2015
    Model Number: RPT0201

    Payment & Shipping Terms:

    Minimum Order Quantity: 10mg
    Price: 65$/10mg
    Packaging Details: ice packaging
    Payment Terms: T/T
    Supply Ability: 1000g per week
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    Detailed Product Description
    Product: Recombinant Porcine Trypsin Cat. No.: RPT0201
    Specific Activity: ≥3800 USP U/mg Pro Purity: > 99%
    Related Product: Recombinant Lipase A

    Enzyme Trypsin Serine   Lysine Protease   Arginine Protease   Recombinant Trypsin

     

     

     

    Description

     

    Trypsin can autocatalytically activate more trypsinogen to trypsin. Trypsin consists of a single chain polypeptide of 223 amino acid residues. This native form of trypsin is refered to as β-trypsin. Autolysis

    of β-trypsin (which is cleaved at Lys- Ser in the bovine sequence) results in α-trypsin which is held together by disulfide bridges. Trypsin is a member of the serine protease S1 family. The active site amino acid residues of trypsin include His and Ser Trypsin is a member of the serine protease family. Trypsin cleaves peptides on the C-terminal end of lysine and arginine amino acid residues. The optimum pH of trypsin is pH 7 - 10. The enzyme is inhibited by serine protease inhibitors, e.g. PMSF and by metal chelating agents,e.g.EDTA.

     

    Advantages

    (1)Animal origin free: recombinant trypsin is no exogenous virus contamination,and any animal origin material is not used in the production process.

    (2)Stable quality: Mass production can ensure stable and continuous batch production.It is no difference between the batch and the product quality is stable.

    (3)High purity: Higher specific activity.Host protein residues is less than the limits of biological products.

    (4)Lyophilized powder: The product is lyophilized powder and is easy to store and transport.

    (5)Compliance with regulatory requirements: Production equipment and production environment comply with relevant regulatory requirements, and the production process is in full compliance with NSF ISO 9001: 2015 quality system and GMP guidelines.

    (6) Complete quality documents: we can provide relevant regular support files in according to customers’ requirement.

     

    Main Features

     

    Source

    E. Coli

    Purified by

    HPLC

    Format

    White lyophilized

    Purity(RP-HPLC)

    NLT 70% β-trysin, NMT 20% α-trypsin

    Contaminant activity

    No chymotrypsin, carboxypeptidase A, and other protease contaminant.

     

     

     

     

     

     

     

     

    Unit Definition

     

    One USP unit of trypsin activity will produce a Delta A253 of 0.003 per minute in a reaction volume of 3.0ml at pH7.6 and 25℃, with BAEE as a substrate (1cm light path).

     

    Recommend Usage

     

    Prepare 1-10mg/ml recombinant trypsin with 1mM HCl.The ratio to aimed protein is 1:50 to 1:1000 (w/w).The optimum pH is pH7-10.

     

     

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    Enzyme Trypsin Serine   Lysine Protease   Arginine Protease   Recombinant Trypsin

     

    Contact Details
    Shanghai Yaxin Biotechnology Co.,Ltd.

    Contact Person: Miss Eland

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