Trypsin Gold, Mass Spectrometry Grade

• 产品编号：V5280      品牌：promega       原厂货号：V5280
• 产品分类：蛋白质检测与分析 > 蛋白质，多肽和酶 > 蛋白酶 > 胰蛋白酶
• 应用分类：蛋白质研究 > 质谱分析 > 质谱样品制备

其它组分：

描述：

原厂资料：

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, is 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.

Learn more about our custom options for this product at: www.promega.com/custom/

Features - Benefits

• 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.
• Choose Your Configuration: Learn more about our custom options for this product at: www.promega.com/custom/

Applications

• Trypsin digestion of proteins from 1 or 2-D gels.
• Tryptic digestion of proteins in-solution.

For more information, see the Protein Purification and Analysis chapter of the Protocols and Applications Guide.

Trypsin Gold, Mass Spectrometry Grade, has extremely high specific activity and is extremely resistant to autolytic digestion. Modified trypsin is maximally active in the range of pH 7–9 and is reversibly inactivated at pH <4. 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 by trypsin.

注意事项：

Storage Conditions: Store the lyophilized powder at –20°C. Reconstitute the
powder in 50mM acetic acid and store at –20°C for up to one month. For
long-term storage, freeze reconstituted trypsin at –70°C. Thaw the reconstituted
trypsin at room temperature, placing on ice immediately after thawing. Remove
the amount of trypsin needed, then refreeze the unused portion. To maintain
maximum product activity, limit the number of freeze-thaw cycles to 5.