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EMS0004

Sigma-Aldrich

SOLu-Trypsin

recombinant, expressed in Pichia pastoris, Proteomics Grade, liquid

Synonyme(s) :

Protein Digestion for Mass Spectrometry, Ready to Use Recombinant Trypsin for Protein Digestion in Mass Spectrometry, Recombinant Trypsin for Protein Digestion in Mass Spectrometry, Trypsin for Protein Digestion, rTrypsin

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About This Item

Code UNSPSC :
12352204
Nomenclature NACRES :
NA.78

Produit recombinant

expressed in Pichia pastoris

Niveau de qualité

200

Qualité

Proteomics Grade

Description

Activity:≥ 10,000 unit/mg protein

Forme

ready-to-use solution

Adéquation

suitable for mass spectrometry

Numéro d'accès UniProt

P00761

Conditions d'expédition

wet ice

Température de stockage

2-8°C

Catégories apparentées

Description générale

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

Application

Poster: Evaluation of Recombinant, Chemically Treated Trypsin in Proteomics and Protein Characterization Assays
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

Actions biochimiques/physiologiques

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.

Caractéristiques et avantages

  • 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

Code de la classe de stockage

10 - Combustible liquids

Classe de danger pour l'eau (WGK)

WGK 1

Point d'éclair (°F)

Not applicable

Point d'éclair (°C)

Not applicable

Certificats d'analyse (COA)

Recherchez un Certificats d'analyse (COA) en saisissant le numéro de lot du produit. Les numéros de lot figurent sur l'étiquette du produit après les mots "Lot" ou "Batch".

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Retrouvez la documentation relative aux produits que vous avez récemment achetés dans la Bibliothèque de documents.

Consulter la Bibliothèque de documents

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)
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
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
Andrea Haag et al.
eLife, 9 (2020-02-14)
The intracellular trafficking of growth factor receptors determines the activity of their downstream signaling pathways. Here, we show that the putative HSP-90 co-chaperone CHP-1 acts as a regulator of EGFR trafficking in C. elegans. Loss of chp-1 causes the retention

Articles

Evaluation of Recombinant, Chemically Treated Trypsin in Proteomics and Protein Characterization Assays

Evaluation of Recombinant, Chemically Treated Trypsin in Proteomics and Protein Characterization Assays

An optimized Protocol for Peptide Mapping of Therapeutic Monoclonal Antibodies with Minimum Deamidation and Oxidation Artifacts

An optimized peptide mapping protocol using NISTmAb as a model monoclonal antibody, shorter incubation times, and improved digestion buffer to demonstrate minimal artificial asparagine deamidation and methionine oxidation.

Development of a Simple and Rapid Digestion Protocol for Proteomics Sample Preparation

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.

Three Methods for Critical Quality Attribute Determination of Monoclonal Antibodies

Step-by-step workflows for the intact mass analysis, peptide mapping, and N-glycan analysis of the monoclonal antibody― adalimumab, for an accurate characterization of the critical quality attributes (CQAs) to ensure drug safety and efficacy. Read more.

Protocoles

Peptide Mapping LC-MS/MS Analysis Workflow for Adalimumab

An optimized LC-MS/MS based workflow for low artifact tryptic digestion and peptide mapping of monoclonal antibody, adalimumab (Humira) using filter assisted sample preparation (FASP).

Notre équipe de scientifiques dispose d'une expérience dans tous les secteurs de la recherche, notamment en sciences de la vie, science des matériaux, synthèse chimique, chromatographie, analyse et dans de nombreux autres domaines..

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