| Identification | Back Directory | [Name]
Trypsin | [CAS]
9002-07-7 | [Synonyms]
500mg
C00298
u-4858
TRYPSIN
tryptar
trypure
Tryprar
Trypsevas
parenzyme
cocoonase
ec3.4.4.4
parenzymol
TRYPSIN NB
ms reagent
Trypsin1:75
EC 3.4.21.1
EC 3.4.21.4
TRYPSIN-EDTA
Trypsin (1X)
pseudotrypsin
TRYPSIN, 1-250
TRYPSIN, 1-300
Trypsin 1：2500
Trypsin/CH8530
allgemeineKarte
α-and β-trypsin
Trypsin(Zhu Yi)
TRYPSIN PORCINE
PORCINE TRYPSIN
TRYPSIN TYP IX-S
TrypZean? bovine
Trypsin 3x cryst
TRYPSIN TYPE IX-S
mass spec reagent
trypsin mass spec
TRYPSIN TYPE II-S
Trypsin,Crystalline
Trypsin (ParenzyMe)
CHYMOTRYPSIN, HUMAN
Trypsin Solution 10X
RecoMbinant Trypsin
TrypsinExPigPancreas
Typsin Solution 10X
Trypsin [Porcine 1:250]
TrypsinExBovinePancreas
TRYPSIN, HUMAN PANCREAS
TRYPSIN 1:250 (PORCINE)
TRYPSIN, PORCINE PANCREAS
trypsin from hog pancreas
Trypsin [>=2500 units/mg]
mass spectrometry reagent
Trypsin from beef pancreas
TRYPSIN 3 X crystallised ,
Trypsin-EDTA Solution 1X
Trypsin, bovine, USP Grade
Trypsin-EDTA Solution 10X
TRYPSIN (0.2 Anson units/g)
TRYPSIN NB SEQUENCING GRADE
cryst.40U/mgforbiochemistry
TrypZean? Solution, 1×
Trypsin froM bovin pancreas
sequence recoMbinant trypsin
exporcine,tissueculturegrade
ALPHA-CHYMOTRYPSIN TYPE IV-S
CHYMOTRYPSIN, HUMAN PANCREAS
CHYMOTRYPSIN PANCREAS, HUMAN
TRYPSIN BRP EPT(CRM STANDARD)
trypsin, pancreatic, type V-S
trypsin from porcine pancreas
Trypsin Crystallized (300 mg)
TrypZean bovine,Trypsin bovine
sequencing recombinant trypsin
TRYPSIN (EP) FIP(CRM STANDARD)
Trypsin Powder, Porcine 1:250
TRYPSIN, USP FROM BOVINE PANCREAS
Trypsin 1:250 from bovine pancreas
Trypsin 1:250 fromPorcine pancreas
TRYPSIN TYPE XX-S FROM GADUS MORHUA
TRYPSIN, PROTEOMICS SEQUENCING GRADE
TRYPSIN CRYSTALLINE BOVINE USP GRADE
Trypsin 1:2500 from Porcine pancreas
Trypsin, froM porcine pancreas, 1:250
TRYPSIN FROM HOG PANCREAS, ~1500 U/MG
trypsin type ix from porcine pancreas
Trypsin, TPCK treated, bovine pancreas
Trypsin, DPCC treated, bovine pancreas
TRYPSIN FROM HOG PANCREAS, ~13000 U/MG
TRYPSIN CRYSTALLIZED USP(CRM STANDARD)
Trypsin from porcine pancreas,lyophil.
trypsin solution from porcine pancreas
trypsin type xii-S from bovine pancreas
trypsin 1X solution cell culture tested
trypsin from bovine pancreas ~8000 U/mg
trypsin 10X solution cell*culture tested
Trypsin, Excision Grade, Bovine Pancreas
TRYPSIN FROM BOVINE PANCREAS DCC TREATED
TRYPSIN FROM HOG PANCREAS, POWDER, ~90 U
TRYPSIN FROM BEEF PANCREAS 3X CRYSTALLINE
trypsin-edta solution cell*culture tested
Trypsin, Iodination Grade, Human Pancreas
TRYPSIN 1:250 PORCINE TISSUE CULTURE GRADE
TRYPSIN 1:300 PORCINE TISSUE CULTURE GRADE
TRYPSIN FROM BEEF PANCREAS 2X CRYSTALLIZED
trypsin, dpcc treated, from bovine pancreas
Trypsin from hog pancreas from hog pancreas
TRYPSIN FROM HOG PANCREAS, POWDER, ~90 U /MG
TRYPSIN FROM BOVINE PANCREAS SEQUENCING GRADE
Trypsin, froM porcine pancreas, 2500 units/Mg
TRYPSIN-EDTA SOLUTION 10X*CELL CULTURE T ESTED
trypsin-edta solution (1X)*cell culture tested
trypsin 1:250 from porcine pancreas*cell culture
trypsin from porcine pancreas cell*culture tested
trypsin type xi dpcc treated from*bovine pancreas
trypsin-edta solution for endothelial*cell cultur
TRYPSIN TYPE V-S: ACETYLATED FROM*BOVINE PANCREAS
TRYPSIN FROM BOVINE PANCREAS, CELL CULTU RE TESTED
TRYPSIN, TPCK TREATED, F. BOVINE PANC., ~7500 U/MG
TRYPSIN TABLETS 1 MG WITH BUFFER SALTS, TRU-MEASURE
TRYPSIN FROM PORCINE PANCREAS IMMUNOHISTOLOGY GRADE
Trypsin from bovine pancreas(2X,Sterile,Irradiated)
TRYPSIN TPCK TREATED FROM BOVINE*PANCREA S ASEPTICAL
TRYPSIN 1:250 FROM PORCINE PANCREAS*CELL CULTURE TE
TRYPSIN-EDTA SOLUTION FOR ENDOTHELIAL*CE LL CULTURES
TRYPSIN TYPE XIII TPCK TREATED*FROM BOVI NE PANCREAS
Trypsin Crystallized (300 mg) (COLD SHIPMENT REQUIRED)
Trypsin froM bovine pancreas(Modified,Sequencing Grade)
TRYPSIN FROM BOVINE PANCREAS, LYOPH, SALTFREE 7500 U/MG*
TRYPSIN FROM BOVINE PANCREAS 3XCRYST.LYO ST-FR. ~9000 U/MG
TRYPSIN FROM PORCINE PANCREAS 75,000-125,000 BAEE UNITS ML
TRYPSIN, DPCC TREATED, F. BOVINE PANC., LYOPH., ~8300 U/MG
TRYPSIN FROM BOVINE PANCREAS ~8000 U/MG LOW-MW-PEPT.FR-FREE
TRYPSIN FR. PORCINE PANCREASCA.60 U/MG 2XCRYST.LYOPH.SALT-FREE
Trypsin from bovine pancreas [EC 3.4.21.4] from bovine pancreas
Trypsin from porcine pancreas,MS reagent, Mass spec reagent, Protein digest | [EINECS(EC#)]
232-650-8 | [Molecular Formula]
C6H15O12P3 | [MDL Number]
MFCD01323069 | [MOL File]
9002-07-7.mol | [Molecular Weight]
372.1 |
| Chemical Properties | Back Directory | [Appearance]
White or almost white, crystalline or amorphous powder, hygroscopic if amorphous. | [Melting point ]
115°C | [bulk density]
200kg/m3 | [density ]
1.37[at 20℃] | [vapor pressure ]
0Pa at 25℃ | [storage temp. ]
−20°C
| [solubility ]
Reconstitute in aqueous buffer | [form ]
lyophilized powder
| [pka]
pK1:6.25 (25°C,μ=0.1) | [color ]
White powder | [Odor]
Odorless | [PH]
7.70-8.30 | [Stability:]
Stable. Incompatible with strong oxidizing agents. | [biological source]
Porcine pancreas | [Water Solubility ]
Soluble in water (10 mg/ml), phosphate buffers (10 mg/ml), and balanced salt solutions (1 mg/ml). | [Merck ]
13,9865 | [Specific Activity]
90-110% (compared to standard) | [Major Application]
diagnostic assay manufacturing | [Cosmetics Ingredients Functions]
SKIN CONDITIONING
HAIR CONDITIONING | [LogP]
-1.3 at 20℃ | [Uses]
Proteolytic enzyme. | [CAS DataBase Reference]
9002-07-7 | [EPA Substance Registry System]
Trypsin(9002-07-7) |
| Hazard Information | Back Directory | [Chemical Properties]
Powder | [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. |
| Questions And Answer | Back Directory | [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] http://www.cytospring.com/pages/TrypsinEDTA.pdf
[2] Jianmei Yu, Mohamed Ahmedna (2012) Functions/applications of trypsin in food processing and food science research, 75-95
[3] http://www.webmd.com/vitamins-supplements/ingredientmono-879-trypsin.aspx?activeingredientid=879&activeingredientname=trypsin
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| Company Name: |
J & K SCIENTIFIC LTD.
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| Telephone: |
18210857532 18210857532 |
| Website: |
https://www.jkchemical.com |
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