Trypsin Gold, Mass Spectrometry Grade, 100ug

Varenummer: V5280
Kort informasjon 100 µg Maximum Digest Specificity with Extreme Resistance to Autolytic Digestion
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Maximum Digest Specificity with Extreme Resistance to Autolytic Digestion 
  • Each lot qualified by mass spectrometry to ensures compatibility with your applications/instrumentation
  • Chymotrypsin activity eliminated for distinct, consistent data
  • Digest in gel, or in solution

Trypsin is a serine protease that specifically cleaves at the carboxylic side of lysine and arginine residues. The stringent specificity of trypsin is essential for protein identification. Native trypsin is subject to autolysis, generating pseudotrypsin, which exhibits a broadened specificity including a chymotrypsin-like activity. Such autolysis products, present in a trypsin preparation, would result in additional peptide fragments that could interfere with database analysis of the mass of fragments detected by mass spectrometry. Trypsin Gold, Mass Spectrometry Grade, has been manufactured to provide maximum specificity. Lysine residues in the porcine trypsin have been modified by reductive methylation, yielding a highly active and stable molecule that is extremely resistant to autolytic digestion. The specificity of the purified trypsin is further improved by TPCK treatment, which inactivates chymotrypsin. The treated trypsin is then purified by affinity chromatography and lyophilized to yield Trypsin Gold, Mass Spectrometry Grade. It is resistant to mild denaturing conditions such as 0.1% SDS, 1M urea or 10% acetonitrile and retains 50% of its activity in 2M guanidine HCl. The activity of trypsin is decreased when acidic residues are present on either side of a susceptible bond. If proline is at the carboxylic side of lysine or arginine, the bond is almost completely resistant to cleavage. Each lot of quality-tested Trypsin Gold, Mass Spectrometry Grade, is qualified for use with in-gel digestion and mass spectrometric analysis.|

Each Lot Qualified by Mass Spectrometry: Ensures compatibility with customer applications/instrumentation. TPCK Treatment Followed by Affinity Purification: Elimination of chymotrypsin activity enables distinct and consistent data. Stability Ensured up to Five Freeze-Thaw Cycles: Minimize leftover reagents. Referenced in Thousands of Papers: Reliable and customer proven.

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Ekstra spesifikasjoner
Store the lyophilized powder at -20°C. Reconstitute powder in 50mM acetic acid and store at -20°C. For long-term storage, freeze reconstituted trypsin at -70°C. Limit the number of freeze-thaw cycles to five.|

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