Trypsin CAS No. 9002-07-7 CAS NO.9002-07-7

scale-up production, based on our rich laboratory experience and advanced equipment in production base, also depend on accumulation of advantages in many aspects as industrialized technology development, the production cost control, to provide from kg class to wt class custom synthesis scale-up production services to the global fine chemical industry, can be carried out oxidation, hydrogenation pressure , halide, and acylation, esterification, condensation, cyclization, formatting, ammoniation, diazotization and azide reaction, our experienced production management, strict and perfect management system can quickly provide customers with competitive and fine mass production services.

product name:	trypsin
synonyms:	trypzean solution, 1× ;mass spec reagent;mass spectrometry reagent;ms reagent;trypsin mass spec;trypsin (1x);sequencing recombinant trypsin;trypsin from bovine pancreas(2x,sterile,irradiated)
cas:	9002-07-7
mf:	c35h47n7o10
mw:	725.78858
einecs:	232-650-8
product categories:	enzyme for insulin production;#n/a;enzymes, inhibitors, and substrates;porcine trypsin;white or white-like lyophilized powder;recombinant protease;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;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;enzyme;sequence carboxypeptidase b
mol file:	9002-07-7.mol

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.
cas database reference	9002-07-7
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
ridadr	un 1789 8 / pgii
wgk germany	2
rtecs	gc3050000
f	1-3-10
tsca	yes
hs code	35079090
hazardous substances data	9002-07-7(hazardous substances data)

msds information

provider	language
cocoonase	english
sigmaaldrich	english

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.
references	[1] # [2] jianmei yu, mohamed ahmedna (2012) functions/applications of trypsin in food processing and food science research, 75-95 [3] # activeingredientid=879&activeingredientname=trypsin
chemical properties	white or almost white, crystalline or amorphous powder, hygroscopic if amorphous.
uses	proteolytic enzyme.

trypsin preparation products and raw materials

preparation products

chymotrypsin-->ec 1.1.3.22