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EMS0004

SOLu-Trypsin Protease

Ready-to-use stable solution for automation, suitable for mass spectrometry, recombinant, expressed in Pichia pastoris

동의어(들):

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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UNSPSC Code:
12352204
NACRES:
NA.78
Form:
ready-to-use solution
Recombinant:
expressed in Pichia pastoris
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제품 이름

SOLu-Trypsin, recombinant, expressed in Pichia pastoris, Proteomics Grade, liquid

recombinant

expressed in Pichia pastoris

Quality Level

200

grade

Proteomics Grade

description

Activity:≥ 10,000 unit/mg protein

form

ready-to-use solution

suitability

suitable for mass spectrometry

UniProt accession no.

P00761

shipped in

wet ice

storage temp.

2-8°C

General description

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

Biochem/physiol Actions

  • 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.
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.

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

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저장 등급

12 - Non Combustible Liquids

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프로토콜

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).

문서

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

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

Simple Digestion Protocol for Proteomics Sample Prep

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

Improving Glycoform Coverage for Mucin Preparations

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

모든 기사 보기
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
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국제 무역 품목 번호

SKUGTIN
EMS0004-100UG04061833253205
EMS0004-4X100UG04061822415751