Trypsin (MS) (C008B-268781)

Trypsin specifically cleaves the C-terminal peptide bonds of lysine and arginine residues. Unmodified trypsin is affected by residues generated from autoproteolysis, which interferes with HPLC peptide mapping. Additionally, autolysis can result in pseudo-trypsin products that exhibit chymotrypsin-like properties. Mass spectrometry (MS)-grade trypsin is a modified porcine trypsin. It is engineered to resist proteolytic digestion through reductive methylation compensation. MS-grade trypsin is further refined by TPCK treatment and affinity purification to yield highly active and stable molecules. Reconstitution Solution It is recommended to use 1 mM hydrochloric acid as the Trypsin reconstitution buffer. pH Range It exhibits maximum activity in the pH range of 7-9 and loses activity reversibly at pH 4. Application Scope Trypsin specifically cleaves lysine (K) and arginine (R) sites in denatured proteins and is recommended for use in combination with rLys-C. Recommended Standard Operating Procedure (SOP) General in-solution digestion protocol Use Trypsin at a protein-to-enzyme ratio (w/w) of 25:1 to 100:1, and incubate at a constant temperature of 37°C for 13-16 hours overnight. Tips To ensure maximum activity, reconstitute MS-grade trypsin using the provided trypsin reconstitution solution and incubate at 30°C for 15 minutes prior to use. The concentration of urea should preferably be less than 1 M.

Specifications & Purity: Trypsin specifically cleaves the C-terminal peptide bonds of lysine and arginine residues. Unmodified trypsin is affected by residues generated from autoproteolysis, which interferes with HPLC peptide mapping. Additionally, autolysis can result in pseudo-trypsin products that exhibit chymotrypsin-like properties. Mass spectrometry (MS)-grade trypsin is a modified porcine trypsin. It is engineered to resist proteolytic digestion through reductive methylation compensation. MS-grade trypsin is further refined by TPCK treatment and affinity purification to yield highly active and stable molecules. Reconstitution Solution It is recommended to use 1 mM hydrochloric acid as the Trypsin reconstitution buffer. pH Range It exhibits maximum activity in the pH range of 7-9 and loses activity reversibly at pH 4. Application Scope Trypsin specifically cleaves lysine (K) and arginine (R) sites in denatured proteins and is recommended for use in combination with rLys-C. Recommended Standard Operating Procedure (SOP) General in-solution digestion protocol Use Trypsin at a protein-to-enzyme ratio (w/w) of 25:1 to 100:1, and incubate at a constant temperature of 37°C for 13-16 hours overnight. Tips To ensure maximum activity, reconstitute MS-grade trypsin using the provided trypsin reconstitution solution and incubate at 30°C for 15 minutes prior to use. The concentration of urea should preferably be less than 1 M.

Grade: Suitable for mass spectrometry (MS);Native;EnzymoPure™

EC Number: 607-831-3

Storage Temperature: Store at -20°C;Avoid repeated freezing and thawing

Shipped in: Ice chest + Ice pads

UPC:

51283224

Weight:

1.09 Ounces

HazmatClass:

Yes

Quantity:

1

Unit of Measurement:

ST

WeightUOM:

LB

MPN:

T1523357-100μg

Country of Origin:

China

CAS:

9002-07-7

Product Size:

100μg

Harmonized Tariff Code:

2931.90.90