EMS0004
SOLu-Trypsin Protease
Ready-to-use stable solution for automation, suitable for mass spectrometry, recombinant, expressed in Pichia pastoris
Synonym(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
UNSPSC Code:
12352204
NACRES:
NA.78
Form:
ready-to-use solution
Recombinant:
expressed in Pichia pastoris
Product Name
SOLu-Trypsin, recombinant, expressed in Pichia pastoris, Proteomics Grade, liquid
recombinant
expressed in Pichia pastoris
grade
Proteomics Grade
description
Activity:≥ 10,000 unit/mg protein
form
ready-to-use solution
suitability
suitable for mass spectrometry
UniProt accession no.
shipped in
wet ice
storage temp.
2-8°C
Quality Level
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
wgk
WGK 1
flash_point_f
Not applicable
flash_point_c
Not applicable
Storage Class
12 - Non Combustible Liquids
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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
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
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