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
ppe
dust mask type N95 (US), Eyeshields, Faceshields, Gloves
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Adam W Barb et al.
Biochemistry, 48(14), 3068-3077 (2009-03-05)
The UDP-3-O-(R-3-hydroxyacyl)-N-acetylglucosamine deacetylase LpxC catalyzes the committed reaction of lipid A (endotoxin) biosynthesis in Gram-negative bacteria and is a validated antibiotic target. Although several previously described compounds bind to the unique acyl chain binding passage of LpxC with high affinity
Fredrick Van Goor et al.
Proceedings of the National Academy of Sciences of the United States of America, 108(46), 18843-18848 (2011-10-07)
Cystic fibrosis (CF) is caused by mutations in the CF transmembrane conductance regulator (CFTR) gene that impair the function of CFTR, an epithelial chloride channel required for proper function of the lung, pancreas, and other organs. Most patients with CF
Maciej Suski et al.
Biochimica et biophysica acta, 1834(12), 2463-2469 (2013-08-31)
Excessive action of angiotensin II on mitochondria has been shown to play an important role in mitochondrial dysfunction, a common feature of atherogenesis and kidney injury. Angiotensin-(1-7)/Mas receptor axis constitutes a countermeasure to the detrimental effects of angiotensin II on
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
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
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