EMS0004

Sigma-Aldrich

SOLu-Trypsin

recombinant, expressed in Pichia pastoris, Proteomics Grade, liquid

Synonym(s):
Ready to Use Recombinant Trypsin for Protein Digestion in Mass Spectrometry, Protein Digestion for Mass Spectrometry, Trypsin for Protein Digestion

Quality Level

recombinant

expressed in Pichia pastoris

description

Activity:≥ 10,000 unit/mg protein

form

liquid

suitability

suitable for mass spectrometry

UniProt accession no.

shipped in

wet ice

storage temp.

2-8°C

Related Categories

General description

Trypsin is a pancreatic serine endoprotease. SOLu-Trypsin is made from recombinant trypsin, porcine sequence. It does not possess chymotryptic activity.

Application

SOLu-Trypsin:
  • has been used to digest the gel pieces for mass spectrometry identification of active deubiquitnases (DUBs)
  • has been used in trypsin sensitivity assay
  • may be used for the digestion of wine proteins

Biochem/physiol Actions

Trypsin is used in proteomics research for peptide mapping and protein sequence work due to its highly specific cleavage resulting in a limited number of tryptic peptides. It hydrolyzes peptide bonds specifically at the carboxyl side of arginine and lysine residues.
  • SOLu-Trypsin (EMS0004) is our exclusive, Advanced Proteomics Grade enzyme that is solution-stable for mass spectrometry.
  • Designed to be stable in solution when refrigerated, SOLu-Trypsin can be used immediately without preparation.
  • Other forms of trypsin require thawing or reconstitution, and must be discarded if not used immediately.
  • SOLu-Trypsin allows excess product to be saved for future use, thus eliminating unnecessary waste and cost.
  • It is formulated with a high-purity recombinant trypsin, free of chymotryptic activity, to ensure high fidelity digestion.

Features and Benefits

  • Ready to use - no preparation, such as reconstitution or thawing, is required
  • Fits seamlessly into established workflow - no need to modify protocols
  • Eliminates waste - remains stable in the refrigerator after use so there is no need to discard excess product
  • Recombinant, porcine sequence - no chymotryptic activity
  • Stable for short-term use at room temperature in an autosampler or on a liquid handling robot

RIDADR

NONH for all modes of transport

WGK Germany

nwg

Flash Point(F)

Not applicable

Flash Point(C)

Not applicable

Søren Heissel et al.
PloS one, 14(6), e0218374-e0218374 (2019-06-28)
Trypsin is by far the most commonly used protease in proteomics. Even though the amount of protease used in each experiment is very small, digestion of large amounts of protein prior to enrichment can be rather costly. The price of...
Enhanced trypsin on a budget: Stabilization, purification and high-temperature application of inexpensive commercial trypsin for proteomics applications
Heissel S, et al.
PLoS ONE, 14 (2019)
Mass spectrometry of peptides and proteins using digestion by a grape cysteine protease at pH 3
Perutka Z and Sebela M
Journal of Mass Spectrometry : Jms (2019)
Zdeněk Perutka et al.
Journal of mass spectrometry : JMS, 55(7), e4444-e4444 (2019-10-12)
Cysteine protease from grapevine (Vitis vinifera) belongs to those resistant proteins, which survive the process of vinification and can therefore be detected as wine components. Its amino acid sequence shows a homology to other members of the papain family, but...
The CHORD protein CHP-1 regulates EGF receptor trafficking and signaling in C. elegans and in human cells
Haag A, et al.
eLife, 9, e50986-e50986 (2020)
Articles
Evaluation of Recombinant, Chemically Treated Trypsin in Proteomics and Protein Characterization Assays
Read More
In this study, we developed a rapid trypsin digest kit that, at elevated temperatures, yielded reliable, reproducible results in less than 2 hours on a wide variety of substrates for mass spectrometry.
Read More

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