Trypsin is a pancreatic serine protease with substrate specificity based upon positively charged lysine and arginine side chains. It is derived from a 34 kDa inactive precursor zymogen, trypsinogen, after enzymatic removal of an N-terminal 6-amino acid leader sequence resulting in the 23.8 kDa trypsin molecule. The optimum pH is 8.0. Trypsin is inhibited by organophosphorus compounds such as diisopropylfluorophosphate and natural inhibitors from pancreas. Soybean, lima bean, and egg white are also sources of natural inhibitors. Trypsin cleaves amide and ester bonds of Arg and Lys. The Worthington Sequencing Grade Trypsin has been further purified to remove trace contaminating proteases and autolysis products which could interfere in trypsin digestion experiments, and exhibits a single band on PAGE.
Uses: For tissue culture work, Worthington trypsin, Codes: TRL, TRLS, TRLVMF and TRTVMF have been used by many researchers.
Product Codes: TRSEQZ, TRSEQII and TRTPCK are typically used for protein sequencing, mapping and structure studies.
Worthington modified sequencing grade trypsin, SequENZ™, Product Code: TRSEQZ, is subjected to extensive purification to remove contaminating proteases and tryptic autolysis by-products which could affect the specificity of the digestion process. Subsequently, the enzyme is chemically modified to minimize the autolysis process as well as increase the stability. The modified trypsin is processed further to remove residual autodegradation products. The specificity of the enzyme is routinely checked after the chemical modification.
Stability/Storage: Most grades of Worthington trypsin are stable for 2-3 years when stored at 2-8°C. Protect from moisture.
Unit Definitions: TAME Unit: One Unit hydrolyzes 1 µmole of p-toluene-sulfonyl-L-arginine methyl ester (TAME) per minute at 25°C, pH 8.2, in the presence of 10 mM calcium.
Technical Notes: The Virus and Mycoplasma Free trypsin (Code: TRTVMF) has been filtered through an 0.22 micron pore size membrane, lyophilized, subjected to gamma irradiation, and tested for virus and mycoplasma.
Related Products:
Chymotrypsin (CDAG/CDS/CDI)
Collagenase (CLS1-4/CLSPA)
Deoxyribonuclease I (DP/D/DCLS/D2/DPFF/DPRF)
Hyaluronidase (HSE/HSEP)
Neutral Protease (Dispase, NPRO)
Proteinase K (PROK)
Trypsin Inhibitors (LBI/OI/SI/SIC)
Cell Isolation Optimizimg System (CIT)
Hepatocyte Isolation System (HIS)
Neonatal Cardiomyocyte Isolation System (NCIS)
Papain Dissociation System (PDS/PDS2)
Description
Activity
Code
Size
Cat. No.
Price
SequENZ® Trypsin, Modified, Sequencing Grade
Trypsin, treated with L-(tosylamido-2-phenyl) ethyl chloromethyl ketone to inhibit contaminating chymotryptic activity, chemically modified to promote stability and further purified to remove autolysis fragments, resulting in a highly stable trypsin product resistant to autolysis while retaining specificity.
Store at -20°C. PROTECT FROM MOISTURE.
REQUIRES SPECIAL SHIPPING: ICE PACK
≥150 units per mg protein (at least 8,625 BAEE/2875 USP/NF units per mg protein)
SequENZ® Trypsin, Modified, Sequencing Grade, Solution
Ready to use liquid preparation of Trypsin, treated with L-(tosylamido-2-phenyl) ethyl chloromethyl ketone to inhibit contaminating chymotryptic activity, chemically modified to promote stability and further purified to remove autolysis fragments, resulting in a highly stable trypsin product resistant to autolysis while retaining specificity. Supplied as 1mgP/ml in 1.0mM HCl.
Store at 2-8°C.
REQUIRES SPECIAL SHIPPING: ICE PACK
Trypsin, Purified, Sequencing Grade II
Bovine trypsin that has been treated with L-(tosylamido-2-phenyl) ethyl chloromethyl ketone (TPCK) to inhibit contaminating chymotryptic activity and extensively purified to remove autolysis products. Supplied as a lyophilized powder.
Store at -20°C. PROTECT FROM MOISTURE.
REQUIRES SPECIAL SHIPPING: ICE PACK
≥150 units per mg protein (at least 8,625 BAEE/2875 USP/NF units per mg protein)
Trypsin, TPCK Treated
A chromatographically purified, diafiltered, lyophilized powder that has been treated with L-(tosylamido-2-phenyl) ethyl chloromethyl ketone (TPCK) to inhibit contaminating chymotryptic activity [Kostka, V., and Carpenter, F.: JBC, 239, 1799 (1964)].
Store at 2-8°C. PROTECT FROM MOISTURE.
≥180 units per mg protein (10,350 BAEE/3,450 USP/NF units per mg protein)
Trypsin, TPCK-Treated, Irradiated
Chromatographically purified trypsin treated with L-(tosylamido-2-phenyl) ethyl chloromethyl ketone (TPCK) to inhibit contaminating chymotryptic activity according to Kostka, V., and Carpenter, F.H.: JBC, 239, 1799 (1964), Code: TRTPCK, lyophilized, irradiated and tested for the absence of mycoplasma and extraneous virus according to 9 CFR 113.53c. Each vial is filled to contain 100 mg.
Store at 2-8°C.
Trypsin, 2X, Sterile, Irradiated
Purified trypsin (Code: TRL), lyophilized, irradiated and tested for the absence of mycoplasma and extraneous virus according to 9 CFR113.53c. Each vial is filled to contain 100 mg.
Store at 2-8°C.
≥180 units per mg protein (10,350 BAEE/3,450 USP/NF units per mg protein)
Trypsin, 0.22µ Filtered
Trypsin chromatographically purified, diafiltered (Code TRL3) filtered thorugh a 0.22 micron pore size membrane and lyophilized in sterile vials. This product is not tested for pyrogenicity.
Store at 2-8°C.
≥180 units per mg protein (10,350 BAEE/3,450 USP/NF units per mg protein)
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