SOLu-Trypsin

Stock Code: 3586926
Manufacturer Part No: EMS0004-4X100UG
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Application


Poster: Evaluation of Recombinant, Chemically Treated Trypsin in Proteomics and Protein Characterization Assays


SOLu-Trypsin:has been used to digest the gel pieces for mass spectrometry identification of active deubiquitnases (DUBs)has been used in trypsin sensitivity assaymay be used for the digestion of wine proteins


Biochem/physiol Actions


SOLu-Trypsin (EMS0004) is our exclusive, Advanced Proteomics Grade enzyme that is solution-stable for mass spectrometry. Designed to be stable in solution when refrigerated, SOLu-Trypsin can be used immediately without preparation. Other forms of trypsin require thawing or reconstitution, and must be discarded if not used immediately. SOLu-Trypsin allows excess product to be saved for future use, thus eliminating unnecessary waste and cost. It is formulated with a high-purity recombinant trypsin, free of chymotryptic activity, to ensure high fidelity digestion.


Trypsin is used in proteomics research for peptide mapping and protein sequence work due to its highly specific cleavage resulting in a limited number of tryptic peptides. It hydrolyzes peptide bonds specifically at the carboxyl side of arginine and lysine residues.


Features and Benefits


Ready to use - no preparation, such as reconstitution or thawing, is required Fits seamlessly into established workflow - no need to modify protocols Eliminates waste - remains stable in the refrigerator after use so there is no need to discard excess product Recombinant, porcine sequence - no chymotryptic activity Stable for short-term use at room temperature in an autosampler or on a liquid handling robot


General description


Trypsin is a pancreatic serine endoprotease. SOLu-Trypsin is made from recombinant trypsin, porcine sequence. It does not possess chymotryptic activity.

Quality Level200
ManufacturerSIGMA-ALDRICH
Further InfoActivity:≥ 10,000 unit/mg protein
Storage Temp.2-8°C
Suitabilitysuitable for mass spectrometry
Formliquid

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