2012 Promega catalogue

Cell Signaling
Immobilized Trypsin
Product Size Cat.# Price ($)
Immobilized Trypsin 2 ml V9012 306.00
For Research Use Only. Not for Use in Diagnostic Procedures.
4 ml V9013 550.00
Description: Immobilized Trypsin provides a fast and convenient method for
digesting a range of concentrations of purified protein or complex protein mixtures.
Digested peptides are easily separated from the Immobilized Trypsin as
they flow through the spin column into the collection tube. Immobilized Trypsin
is easily removed from the peptide solution because the trypsin does not pass
though the column frit. Trypsin is a proteolytic enzyme, which cleaves at the
carboxyl side of positively charged Lysine (Lys) and Arginine (Arg). When these
amino acids are followed by the nonpolar Proline (Pro), the digestion of the site
is not efficient. When Lys and Arg are followed by acids [Aspartic Acid (Asp) and
Glutamic Acid (Glu)] the digestion is also not as efficient.
Features:
• Fast: Digestions can be accomplished in as little as 30 minutes.
• Scalable: Easily adjustable protocol accommodates various protein
concentrations.
• Easy-to-Use: No shaking or water baths necessary.
Storage Conditions: Store at 4°C.
Protocol Part#
Immobilized Trypsin Technical Manual TM077
Chymotrypsin, Sequencing Grade
Product Size Cat.# Price ($)
Chymotrypsin, Sequencing Grade 25 µg V1061 81.00
For Research Use Only. Not for Use in Diagnostic Procedures.
100 µg V1062 276.00
Description: Chymotrypsin is a highly-purified serine endopeptidase derived
from bovine pancreas that preferentially hydrolyzes at the carboxyl side of
aromatic amino acids: Tyr, Phe and Trp. Cleavage may also be observed, but at
a lower rate, at Leu and Met. Chymotrypsin 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#
Chymotrypsin Sequencing Grade Product Information 9PIV106
For complete and up-to-date product information visit: www.promega.com/catalog
Trypsin Gold, Mass Spectrometry Grade
Product Size Cat.# Price ($)
Trypsin Gold, Mass Spectrometry Grade
For Research Use Only. Not for Use in Diagnostic Procedures.
100 µg V5280 159.00
Description: 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. Trypsin is often
used for in-gel digestion. The digestion products are purified and concentrated,
then analyzed by mass spectrometry to determine their molecular weights.
Database searches can then be performed, using the mass of the peptides
to identify the protein(s) resolved on the gel. Each lot of quality-tested Trypsin
Gold, Mass Spectrometry Grade, is qualified for use with in-gel digestion and
mass spectrometric analysis.
Features:
• Pure: TPCK treatment followed by affinity purification.
• Application Qualified: Each lot is qualified by mass spectrometry.
• Convenient: Provided in one vial.
• Good Value: Stability ensured up to five freeze-thaw cycles, thus minimizing
leftover reagents.
• Choose Your Configuration: Learn more about our custom options for
this product at: www.promega.com/myway/
Storage Conditions: 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.
Protocol Part#
Trypsin Gold, Mass Spectrometry Grade Technical Bulletin TB309
231
13
Protein Expression and Analysis
Section
Contents
Table of
Contents