Science Catalog 2012 Life Cell Signaling Sequencing Grade Modified Trypsin Product Sequencing Grade Modified Trypsin For Laboratory Use. Size Cat.# Price (Fr) 100 µg V5111 143.00 Description: Trypsin specifically hydrolyzes peptide bonds at the carboxylic sides of lysine and arginine residues. Unmodified trypsin is subject to autolysis, generating fragments that can interfere with protein sequencing, HPLC or mass spectrometry analysis of the peptides. In addition, autolysis can result in the generation of pseudotrypsin, which has been shown to exhibit an additional chymotrypsin-like specificity. Promega Trypsin has been modified by reductive methylation, rendering it extremely resistant to autolytic digestion. In functional stability tests, modified trypsin retains at least two times as much activity as unmodified trypsin after a 3-hour incubation at 37°C. The sequencing grade of modified trypsin has been further improved by TPCK treatment followed by affinity purification yielding a highly active and stable molecule. Sequencing Grade Modified Trypsin is provided as a lyophilized powder in convenient 20μg aliquots with a stability-optimized resuspension buffer. A protease:protein ratio of 1:100 to 1:20 (w/w) is recommended. Recommended Reaction Buffer: 50mM NH4HCO3 (pH 7.8). Features: • Pure: TPCK treatment followed by affinity purification. • Easy to Use: Resuspension buffer provided. • Convenient: Five tubes of lyophilized product are provided. • Choose Your Configuration: Learn more about our custom options for this product at: www.promega.com/myway/ Storage Conditions: Store lyophilized at –20°C. Protocol Sequencing Grade Modified Trypsin Product Information Part# 9PIV511 Product Sequencing Grade Modified Trypsin, Frozen Size Cat.# Price (Fr) Sequencing Grade Modified Trypsin, Frozen For Laboratory Use. 100 µg V5113 93.00 Description: Trypsin specifically hydrolyzes peptide bonds at the carboxylic sides of lysine and arginine residues. Unmodified trypsin is subject to autolysis, generating fragments that can interfere with protein sequencing, HPLC or mass spectrometry analysis of the peptides. In addition, autolysis can result in the generation of pseudotrypsin, which has been shown to exhibit an additional chymotrypsin-like specificity. Promega Trypsin has been modified by reductive methylation, rendering it extremely resistant to autolytic digestion. In functional stability tests, modified trypsin retains at least two times as much activity as unmodified trypsin after a 3-hour incubation at 37°C. The sequencing grade of modified trypsin has been further improved by TPCK treatment followed by affinity purification yielding a highly active and stable molecule. Sequencing grade modified trypsin is provided as a frozen liquid in convenient 20μg aliquots with a stability-optimized dilution buffer. A protease:protein ratio of 1:100 to 1:20 (w/w) is recommended for protein sequencing. Recommended Reaction Buffer: 50mM NH4HCO3 (pH 7.8). Storage Conditions: Store at –70°C. Protocol Part# Sequencing Grade Modified Trypsin, Frozen, Product Information 9PIV5113 Endoproteinase Lys-C, Sequencing Grade Product Endoproteinase Lys-C, Sequencing Grade For Research Use Only. Not for Use in Diagnostic Procedures. Description: Endoproteinase Lys-C is a sequencing grade serine protease isolated from Lysobacter enzymogenes as a highly purified protease that hydrolyzes specifically at the carboxyl side of Lys. Lys-C activity is optimal in the pH range of 7.0–9.0. This sequencing grade enzyme can be used alone or in combination with other proteases to produce protein digests for peptide mapping applications or protein identification by peptide mass fingerprinting or MS/ MS spectral matching. It is suitable for digestion reactions in-solution or in-gel. Storage Conditions: Store at 4°C. Protocol Endoproteinase Lys-C, Sequencing Grade Product Information rLys-C, Mass Spec Grade Product rLys-C, Mass Spec Grade For Research Use Only. Not for Use in Diagnostic Procedures. Description: rLys-C, Mass Spec Grade, is a recombinant Lys-C expressed in E. coli. Sequence origin of rLys-C is Protease IV from Pseudomonas aeruginosa. Similar to a native Lys-C, rLys-C cleaves at the carboxyl side of lysine residues with exceptional specificity. rLys-C retains proteolytic activity under protein denaturing conditions such as 8M urea, which is used to improve digestion of proteolytically resistant proteins. rLys-C activity is optimal in the pH range of 8-9. The protease is supplied in a lyophilized form along with a Reconstitution Buffer, which is formulated to increase stability of rLys-C solution. Frozen rLys-C solution can be stored for a month at –20ºC without detectable loss of activity. rLys-C is recommended for digestion of single proteins and complex protein mixtures in-solution and in-gel. Features: • Competitive Performance: Matches cleavage specificity of a native Lys-C. Proteolytic activity is similar. • Purity: No contaminating peptides are identified with reverse-phase HPLC. • Application-Qualified: Each lot is qualified by mass spectrometry. • Tolerance to Protein Denaturing Conditions: Retains activity in 8M urea. • Cost-Effective: Severalfold price reduction as compared to a native Lys-C. Storage Conditions: Store at –20°C. Protocol rLys-C, Mass Spec Grade Product Information Part# 9PIV167 Size Cat.# Price (Fr) 15 µg V1671 219.00 Part# 9PIV107 Size Cat.# Price (Fr) 5 µg V1071 199.00 234 For complete and up-to-date product information visit: www.promega.com/catalog Pagina 237
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