计算溶液所需的质量、体积或浓度。
EnzymoPure™,质谱级 (MS) 级 ,适用于对基线干扰要求严格的色谱和分析工作流程。
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在色谱分析、有机合成和交叉偶联反应领域已被 441 篇同行评审文献引用。
Trypsin is a pancreatic serine protease with substrate specificity based upon positively charged lysine and arginine side chains. It is derived from a 34 kDa inactive precursor zymogen, trypsinogen, after enzymatic removal of an N-terminal 6-amino acid leader sequence resulting in the 23.8 kDa trypsin molecule. The optimum pH is 8.0. Trypsin is inhibited by organophosphorus compounds such as diisopropylfluorophosphate and natural inhibitors from pancreas. Soybean, lima bean, and egg white are also sources of natural inhibitors. Trypsin cleaves amide and ester bonds of Arg and Lys. The Aladdin Sequencing Grade Trypsin has been further purified to remove trace contaminating proteases and autolysis products which could interfere in trypsin digestion experiments, and exhibits a single band on PAGE.Trypsin is a serine protease used to hydrolyze proteins. Trypsin from bovine pancreas has a molecular weight of 23.8 kDa. Trypsins are used for the re-suspension of cells during cell culture and in proteomics research for the digestion of various proteins
Specificity:
Trypsin cleaves peptides on the C-terminal side of lysine and arginine amino acid residues. If a proline residue is on the carboxyl side of the cleavage site, the cleavage will not occur. If an acidic residue is on either side of the cleavage site, the rate of hydrolysis has been shown to be slower.
Protein Accession Number: P00760
CATH Classification (v. 3.2.0):
Class: Mainly Beta
Architecture: Beta Barrel
Topology: Thrombin, subunit H
Molecular Weight: 23.3 kDa (Theoretical)
Optimal pH: 7.5-8.5 (Koutsopoulos et al. 2007)
Isoelectric Point:
Trypsinogen: pH 9.3 (Walsh and Neurath 1964)
Trypsin: pH 10.5 (Cunningham 1954).
Extinction Coefficient: Trypsinogen: 45,250 cm-1 M-1>
Active Site Residues:
Histidine (H63)
Aspartic acid (D107)
Serine (S200)
Activators: The rate of trypsinogen conversion is enhanced by using lanthanide in place of calcium ions (Gomez et al. 1974).
Inhibitors:
Pancreatic-, soybean-, lima bean-, and egg white- trypsin inhibitors (see section on Trypsin Inhibitors)
DFP
Aprotinin
Ag+
Benzamidine
EDTA
(White and White 1997)
Applications:
Tissue dissociation, especially when combined with other enzymes such as collagenase, and elastase
Cell harvesting by “trypsinization”
Mitochondria isolation
in vitro studies of proteins
Removing monolayers of cells from plastic and glass
Various hemagglutination procedures
Sample preparation for flow cytometric DNA analysis
Tryptic mapping
Fingerprinting and sequencing work
Environmental monitoring
Reduction of cell density in tissue culture
Subculturing cells
Cleavage fusion proteins
Generating glycopeptides from purified glycoproteins
(White and White 1997)
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