T6567
Trypsin from porcine pancreas
Proteomics Grade, BioReagent, Dimethylated
Synonym(s):
Porcine Trypsin, Trypsin for Mass Spectropetry
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About This Item
Recommended Products
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
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.
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Product No.
Description
Pricing
Signal Word
Danger
Hazard Statements
Precautionary Statements
Hazard Classifications
Eye Irrit. 2 - Resp. Sens. 1 - Skin Irrit. 2 - STOT SE 3
Target Organs
Respiratory system
Storage Class Code
11 - Combustible Solids
WGK
WGK 1
Personal Protective Equipment
dust mask type N95 (US), Eyeshields, Gloves
Certificates of Analysis (COA)
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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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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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A novel chemoenzymatic one-pot multicomponent synthesis of thiazole derivatives was developed. A series of thiazole derivatives were synthesized with high yields up to 94% under mild enzyme-catalyzed conditions. The blank and control experiments reveal that trypsin from porcine pancreas (PPT)
Pauline Floch et al.
Gut pathogens, 6, 20-20 (2014-07-06)
A gamma-glutamyl transpeptidase (GGT) is produced by up to 31% of strains of Campylobacter jejuni isolates. C. jejuni GGT is close to Helicobacter pylori GGT suggesting a conserved activity but unlike the latter, C. jejuni GGT has not been studied
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