China Biggest Manufacturer factory sales TRYPSIN CAS 9002-07-7 CAS NO.9002-07-7

                                PRODUCT DETAILS                           

Trypsin Basic information Description References Product Name: Trypsin Synonyms: Trypsin-EDTA Solution 1X;α-and β-trypsin;Tryprar;Trypsevas;Trypsin Powder, Porcine 1:250;TRYPSIN TYPE V-S: ACETYLATED FROM*BOVINE PANCREAS;TRYPSIN, PROTEOMICS SEQUENCING GRADE;TRYPSIN-EDTA SOLUTION FOR ENDOTHELIAL*CE LL CULTURES 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   Trypsin Chemical Properties 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. 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 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. Uses Trypsin is a digestive enzyme found in the digestive system. The enzyme catalyzes the hydrolysis of peptide bonds breaking down proteins into smaller peptides. Uses Trypsin-EDTA Solution 10X has been used to release adherent cells from tissue culture plates for passaging. 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. Brand name Parenzyme;Trypsillin. General Description Trypsin is applicable for tissue disaggregation, due to its effective action and tolerance towards different cell type and serum-induced neutralization. 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.   Trypsin Preparation Products And Raw materials Preparation Products Chymotrypsin-->EC 1.1.3.22

                                Group profiles

Leader Biochemical Group is a large leader incorporated industry manufacturers and suppliers of advanced refined raw materials From the year of 1996 when our factory was put into production to year of 2020, our group has successively invested in more than 52 factories with shares and subordinates.We focus on manufacture Pharm & chemicals, functional active ingredients, nutritional Ingredients, health care products, cosmetics, pharmaceutical and refined feed, oil, natural plant ingredients industries to provide top quality of GMP standards products.All the invested factories' product lines cover API and intermediates, vitamins, amino acids, plant extracts, daily chemical products, cosmetics raw materials, nutrition and health care products, food additives, feed additives, essential oil products, fine chemical products and agricultural chemical raw materials And flavors and fragrances. Especially in the field of vitamins, amino acids, pharmaceutical raw materials and cosmetic raw materials, we have more than 20 years of production and sales experience. All products meet the requirements of high international export standards and have been recognized by customers all over the world. Our manufacture basement & R&D center located in National Aerospace Economic & Technical Development Zone Xi`an Shaanxi China. Now not only relying on self-cultivation and development as well as maintains good cooperative relations with many famous research institutes and universities in China. Now, we have closely cooperation with Shanghai Institute of Organic Chemistry of Chinese Academy of Science, Beijing Institute of Material Medical of Chinese Academy of Medical Science, China Pharmaceutical University, Zhejiang University. Closely cooperation with them not only integrating Science and technology resources, but also increasing the R&D speed and improving our R&D power. Offering Powerful Tech supporting Platform for group development. Keep serve the manufacture and the market as the R&D central task, focus on the technical research.  Now there are 3 technology R & D platforms including biological extract, microorganism fermentation and chemical synthesis, and can independently research and develop kinds of difficult APIs and pharmaceutical intermediates. With the strong support of China State Institute of Pharmaceutical Industry (hereinafter short for CSIPI), earlier known as Shanghai Institute of Pharmaceutical Industry (SIPI), we have unique advantages in the R & D and industrialization of high-grade, precision and advanced products.  Now our Group technical force is abundant, existing staff more that 1000 people, senior professional and technical staff accounted for more than 50% of the total number of employees, including 15 PhD research and development personnel, 5 master′ S degree in technical and management personnel 9 people. We have advanced equipment like fermentation equipment and technology also extraction, isolation, purification, synthesis with rich production experience and strict quality control system, According to the GMP required, quickly transforming the R&D results to industrial production in time, it is our advantages and our products are exported to North and South America, Europe, Middle East, Africa, and other five continents and scale the forefront in the nation, won good international reputation.  We believe only good quality can bring good cooperation, quality is our key spirit during our production, we are warmly welcome clients and partner from all over the world contact us for everlasting cooperation, Leader will be your strong, sincere and reliable partner in China.

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                                                       Product information

Trypsin Basic information Description References Product Name: Trypsin Synonyms: Trypsin-EDTA Solution 1X;α-and β-trypsin;Tryprar;Trypsevas;Trypsin Powder, Porcine 1:250;TRYPSIN TYPE V-S: ACETYLATED FROM*BOVINE PANCREAS;TRYPSIN, PROTEOMICS SEQUENCING GRADE;TRYPSIN-EDTA SOLUTION FOR ENDOTHELIAL*CE LL CULTURES 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   Trypsin Chemical Properties 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. 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 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. Uses Trypsin is a digestive enzyme found in the digestive system. The enzyme catalyzes the hydrolysis of peptide bonds breaking down proteins into smaller peptides. Uses Trypsin-EDTA Solution 10X has been used to release adherent cells from tissue culture plates for passaging. 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. Brand name Parenzyme;Trypsillin. General Description Trypsin is applicable for tissue disaggregation, due to its effective action and tolerance towards different cell type and serum-induced neutralization. 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.   Trypsin Preparation Products And Raw materials Preparation Products Chymotrypsin-->EC 1.1.3.22