TIANFU CHEM Trypsin CAS NO.9002-07-7

product name: trypsin
synonyms: trypsin;trypsin, 1-250;trypsin, 1-300;trypsin-edta;trypsin, human pancreas;trypsin porcine;trypsin, porcine pancreas;ec3.4.4.4
cas: 9002-07-7
mf: c6h15o12p3
mw: 372.1
einecs: 232-650-8
product categories: hydrolases;specialty enzymes;diagnostic reagents;proteasesanalytical enzymes;trypsin for general research applicationscell culture;usp chemicals and reagentsenzyme class index;cell dissociationapplication index;reagents and supplements;enzymes, inhibitors, and substrates;dissociationanalytical enzymes;proteolytic enzymesproteolytic enzymes and substrates;trypsinanalytical enzymes;proteasesenzymes, inhibitors, and substrates;proteolytic enzymes and substrates;selective proteolytic enzymes;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;enzyme;sequence carboxypeptidase b;enzyme for insulin production;#n/a;porcine trypsin;white or white-like lyophilized powder;recombinant protease
mol file: mol file
trypsin structure
trypsin chemical properties
melting point 115°c
storage temp. −20°c
solubility reconstitute in aqueous buffer
form lyophilized powder
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.
epa substance registry system trypsin(9002-07-7)
safety information
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
hs code 35079090
hazardous substances data 9002-07-7(hazardous substances data)

trypsin usage and synthesis
description 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