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EMS0004

Sigma-Aldrich

SOLu-Trypsin

recombinant, expressed in Pichia pastoris, Proteomics Grade, liquid

Sinonimo/i:

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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100 μG
93,60 €
4 X 100 μG
349,00 €

93,60 €

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Cambia visualizzazione
100 μG
93,60 €
4 X 100 μG
349,00 €

About This Item

Codice UNSPSC:
12352204
NACRES:
NA.78

93,60 €

Per informazioni sulla disponibilità, contatta il Servizio Clienti.
Richiedi un ordine bulk

Ricombinante

expressed in Pichia pastoris

Livello qualitativo

200

Grado

Proteomics Grade

Descrizione

Activity:≥ 10,000 unit/mg protein

Stato

ready-to-use solution

Compatibilità

suitable for mass spectrometry

N° accesso UniProt

P00761

Condizioni di spedizione

wet ice

Temperatura di conservazione

2-8°C

Categorie correlate

Descrizione generale

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

Applicazioni

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)[1]
  • has been used in trypsin sensitivity assay[2]
  • may be used for the digestion of wine proteins[3]

Azioni biochim/fisiol

Trypsin is used in proteomics research[4] 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.[5]
  • 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.

Caratteristiche e vantaggi

  • 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

Codice della classe di stoccaggio

10 - Combustible liquids

Classe di pericolosità dell'acqua (WGK)

WGK 1

Punto d’infiammabilità (°F)

Not applicable

Punto d’infiammabilità (°C)

Not applicable

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Certificati d'analisi (COA)

Lot/Batch Number
0000395918
0000380442
0000395918
0000380442
0000400679

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I documenti relativi ai prodotti acquistati recentemente sono disponibili nell’Archivio dei documenti.

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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)
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)
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
Visualizza tutti i documenti correlati

Articoli

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

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

Improving Glycoform Coverage for Mucin Preparations

Pretreatment with Mucinase StcE increases glycopeptide identification from mucin samples, enhancing sample preparation efficiency for glycopeptide analysis.

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.

Simple Digestion Protocol for Proteomics Sample Prep

Rapid trypsin digest kit yields reliable results in less than 2 hours for mass spectrometry analysis.

Vedi tutto

Protocolli

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).

Contenuto correlato

Protein Research Guide

Find protein research tools to prepare, isolate, and analyze proteins. Organized by how to extract, protect, purify, enrich, modify, and quantify proteins.

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