T6567
Trypsin Protease
Hydrolyzes peptide bonds specifically at the carboxyl side of arginine and lysine residues, suitable for mass spectrometry, from Porcine pancreas
Synonym(s):
Porcine Trypsin, Trypsin for Mass Spectropetry
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About This Item
Biological source:
Porcine pancreas
Product Name
Trypsin from porcine pancreas, Proteomics Grade, BioReagent, Dimethylated
biological source
Porcine pancreas
product line
BioReagent
solubility
1 mM HCl: soluble 1 mg/mL, clear, colorless
shipped in
wet ice
storage temp.
2-8°C
Quality Level
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General description
Trypsin is a serine protease that is usually used in biochemistry and biology as an important enzymatic reagent. This method produces a highly purified trypsin product suitable for proteomics research. Proteomics Grade ideal for use in both solution and in-gel tryptic digestions. Trypsin, a serine protease, is present in the digestive system of several vertebrates.
Application
Trypsin from porcine pancreas is used for the following applications:
- In-gel protein digestion and MALDI-TOF mass spectrometry analysis
- Electrospray Ionization Mass Spectrometry (ESI-MS) analysis
- Surface proteome profiling of L. plantarum
- Gel Filtration, Ultracentrifugation, and Rotary Shadowing Electron Microscopy
- Mass spectrometry
Biochem/physiol Actions
Trypsin is routinely 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.. The enzyme also exhibits esterase and amidase activities. Trypsin acts as a cell culture tool. It is used to hydrolyze allergenic proteins to produce hypoallergenic milk in industries.
signalword
Danger
hcodes
Hazard Classifications
Eye Irrit. 2 - Resp. Sens. 1 - Skin Irrit. 2 - STOT SE 3
target_organs
Respiratory system
Storage Class
11 - Combustible Solids
wgk
WGK 1
ppe
dust mask type N95 (US), Eyeshields, Faceshields, Gloves
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Shaoming Mao et al.
Molecular bioSystems, 7(5), 1660-1677 (2011-03-09)
The solventogenic bacterium Clostridium acetobutylicum is the most important species of Clostridium used in the fermentation industry. However, the intolerance to butanol hampers the efficient production of solvents. Butanol toxicity has been attributed to the chaotropic effect on the cell
Cristina C Santini et al.
Scientific reports, 9(1), 10865-10865 (2019-07-28)
Small molecule inhibitors of BRAF and MEK have proven effective at inhibiting tumor growth in melanoma patients, however this efficacy is limited due to the almost universal development of drug resistance. To provide advanced insight into the signaling responses that
Families of serine peptidases.
N D Rawlings et al.
Methods in enzymology, 244, 19-61 (1994-01-01)
Masayuki Shimoda et al.
Cell transplantation, 21(2-3), 465-471 (2012-07-17)
Porcine islets are considered to be a promising resource for xenotransplantation. However, it is difficult to isolate porcine islets because of the marked fragility and rapid dissociation. Endogenous trypsin is one of the main factors to damage islets during the
Daniela M Remus et al.
Journal of bacteriology, 195(3), 502-509 (2012-11-24)
Sortases are transpeptidases that couple surface proteins to the peptidoglycan of Gram-positive bacteria, and several sortase-dependent proteins (SDPs) have been demonstrated to be crucial for the interactions of pathogenic and nonpathogenic bacteria with their hosts. Here, we studied the role
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