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EMS0004

Sigma-Aldrich

SOLu-Trypsin

recombinant, expressed in Pichia pastoris, Proteomics Grade, liquid

Sinónimos:

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

Código UNSPSC:
12352204
NACRES:
NA.78

recombinante

expressed in Pichia pastoris

Nivel de calidad

200

grado

Proteomics Grade

descripción

Activity:≥ 10,000 unit/mg protein

formulario

ready-to-use solution

idoneidad

suitable for mass spectrometry

Nº de acceso UniProt

P00761

Condiciones de envío

wet ice

temp. de almacenamiento

2-8°C

Categorías relacionadas

Descripción general

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

Aplicación

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

Acciones bioquímicas o fisiológicas

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.

Características y beneficios

  • 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

Código de clase de almacenamiento

10 - Combustible liquids

Clase de riesgo para el agua (WGK)

WGK 1

Punto de inflamabilidad (°F)

Not applicable

Punto de inflamabilidad (°C)

Not applicable

Certificados de análisis (COA)

Busque Certificados de análisis (COA) introduciendo el número de lote del producto. Los números de lote se encuentran en la etiqueta del producto después de las palabras «Lot» o «Batch»

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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
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)
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
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Artículos

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.

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Protocolos

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).

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