Trypsin from porcine pancreas

CAS:      9002-07-7

Artikel Nr: P6403

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Properties

Synonyms:

trypure;u-4858;parenzyme;parenzymol;pseudotrypsin;PORCINE TRYPSIN;EC 3.4.21.4;CHYMOTRYPSIN PANCREAS, HUMAN

CAS:      9002-07-7

MF:        C35H47N7O10

MW:      725.78858

EINECS:               232-650-8

Product Categories:        sequence Carboxypeptidase B; ProteasesAnalytical Enzymes; Trypsin for General Research ApplicationsCell Culture;USP Chemicals and ReagentsEnzyme Class Index; Cell DissociationApplication Index;Reagents and Supplements; Hydrolases;Specialty Enzymes;Diagnostic reagents;enzyme;enzyme for insulin production;Porcine trypsin;White or White-like lyophilized powder; Recombinant Protease;Cell Dissociation (Cell Culture Tested)Stem Cell Biology;Cell Dissociation and Cell Lysis; DissociationNeural Stem Cell Biology; DissociationReagents and Supplements; EnzymesAnalytical Enzymes;Neural Stem Cell Isolation/Expansion; Trypsin Solutions for Cell Dissociation; Application Index; Cell Dissociation; Stem Cell Isolation; Trypsin; Neural Stem Cell Biology; Trypsin for General Research ApplicationsEnzyme Class Index; 3.4.x.x Peptidases; 3.x.x.x Hydrolases; Proteases&Protein Sequencing;ProteasesEnzyme Class Index;Proteolytic EnzymesProteolytic Enzymes and Substrates; TrypsinAnalytical Enzymes; ProteasesEnzymes, Inhibitors, and Substrates; Proteolytic Enzymes and Substrates; Selective Proteolytic Enzymes; DissociationAnalytical Enzymes; Enzymes, Inhibitors, and Substrates

Mol File:              9002-07-7.mol

Melting point:   115°C

storage temp.: -20°C

solubility:           Reconstitute in aqueous buffer

pka:       pK1:6.25 (25°C, μ=0.1)

form:    lyophilized powder

color:    White powder

Odor:    Odorless

Water Solubility:             Soluble in water (10 mg/ml), phosphate buffers (10 mg/ml), and balanced salt solutions (1 mg/ml).

Merck:  13,9865

Stability:             Stable. Incompatible with strong oxidizing agents.

 

Safety

Chemical Safety:

Hazard Codes:   Xn,B

Risk Statements:             36/37/38-42-42/43

Safety Statements:         22-24-26-36/37-45-23

WGK Germany:               2

RTECS:  GC3050000

F:            1-3-10

TSCA:    Yes

 

Description

Trypsin is applicable for tissue disaggregation, due to its effective action and tolerance towards different cell type and serum-induced neutralization.

Trypsin is a serine protease in the digestive system of human and animals. The main function of this enzyme is to hydrolyze proteins into smaller peptides or even amino acids. Trypsin and other digestive proteases such as chymotrypsin are responsible for the digestion of food protein in the small intestine. This proteolytic function of trypsin has been widely used in the protein chemistry, proteomics, and nutrition research. This function is influenced by the sources of enzyme, and environmental factors such as pH, temperature, and the presence of trypsin inhibitors in the enzymatic reaction medium.

Trypsin is used in the food processing to improve the functional properties such as solubility, emulsification, foaming and gelling properties of food proteins, to improve the digestibility of vegetable and seed proteins. It is used to reduce the concentration of allergens in some foods and to produce protein hydrolysates and bioactive peptides that are used in infant formulas and for people with special health problems such as hypertension. In food science research, trypsin is used for the food protein sequencing, in-vitro determination of food protein digestibility.  In combination with bromelain and rutin, trypsin is used for osteoarthritis. Trypsin is used to remove necrotic tissue and debris during wound and ulcer cleaning. Trypsin supplements may be used to remove dead tissue cells that remain after trauma, infection or surgical procedures, allowing new skin or tissue cells to grow.

Uses

Trypsin-EDTA Solution 10X has been used to release adherent cells from tissue culture plates for passaging.

Proteolytic enzyme.

Trypsin is a digestive enzyme found in the digestive system. The enzyme catalyzes the hydrolysis of peptide bonds breaking down proteins into smaller peptides.

 

Definition

trypsin: An enzyme that digests proteins(see protease). It is secreted inan inactive form (trypsinogen) by thepancreas into the duodenum. There,trypsinogen is acted on by an enzyme(enterokinase) produced in theduodenum to yield trypsin. The activeenzyme plays an important rolein the digestion of proteins in the anteriorportion of the small intestine.It also activates other proteases inthe pancreatic juice.

 

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.

 

 

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