2012 Promega catalogue

Life
Science
Catalog
2012
Worldwide Contact List
Section
Contents
Table of
Contents
Cell Signaling
232
Sequencing Grade Modified Trypsin
Product Size Cat.# Price ($)
Sequencing Grade Modified Trypsin 100 µg V5111 119.00
For Laboratory Use.
Description: Trypsin specifically hydrolyzes peptide bonds at the carboxylic
sides of lysine and arginine residues. Unmodified trypsin is subject to autolysis,
generating fragments that can interfere with protein sequencing, HPLC or mass
spectrometry analysis of the peptides. In addition, autolysis can result in the
generation of pseudotrypsin, which has been shown to exhibit an additional
chymotrypsin-like specificity. Promega Trypsin has been modified by reductive
methylation, rendering it extremely resistant to autolytic digestion. In functional
stability tests, modified trypsin retains at least two times as much activity as
unmodified trypsin after a 3-hour incubation at 37°C.
The sequencing grade of modified trypsin has been further improved by TPCK
treatment followed by affinity purification yielding a highly active and stable
molecule. Sequencing Grade Modified Trypsin is provided as a lyophilized powder
in convenient 20μg aliquots with a stability-optimized resuspension buffer.
A protease:protein ratio of 1:100 to 1:20 (w/w) is recommended.
Recommended Reaction Buffer: 50mM NH 4HCO 3 (pH 7.8).
Features:
• Pure: TPCK treatment followed by affinity purification.
• Easy to Use: Resuspension buffer provided.
• Convenient: Five tubes of lyophilized product are provided.
• Choose Your Configuration: Learn more about our custom options for
this product at: www.promega.com/myway/
Storage Conditions: Store lyophilized at –20°C.
Protocol Part#
Sequencing Grade Modified Trypsin Product Information 9PIV511
Sequencing Grade Modified Trypsin, Frozen
Product Size Cat.# Price ($)
Sequencing Grade Modified Trypsin, Frozen
For Laboratory Use.
100 µg V5113 106.00
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 NH 4HCO 3 (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 Size Cat.# Price ($)
Endoproteinase Lys-C, Sequencing Grade
For Research Use Only. Not for Use in Diagnostic Procedures.
5 µg V1071 227.00
Description: Endoproteinase Lys-C is a sequencing grade serine protease
isolated from Lysobacter enzymogenes as a highly purified protease that
hydrolyzes specifically at the carboxyl side of Lys. Lys-C activity is optimal in the
pH range of 7.0–9.0. This sequencing grade enzyme can be used alone or in
combination with other proteases to produce protein digests for peptide mapping
applications or protein identification by peptide mass fingerprinting or MS/
MS spectral matching. It is suitable for digestion reactions in-solution or in-gel.
Storage Conditions: Store at 4°C.
Protocol Part#
Endoproteinase Lys-C, Sequencing Grade Product Information 9PIV107
rLys-C, Mass Spec Grade
Product Size Cat.# Price ($)
rLys-C, Mass Spec Grade
For Research Use Only. Not for Use in Diagnostic Procedures.
15 µg V1671 252.00
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 Part#
rLys-C, Mass Spec Grade Product Information 9PIV167
For complete and up-to-date product information visit: www.promega.com/catalog