胰蛋白酶 来源于牛胰脏

T105533-100g

100g

EnzymoPure™

potency ≥3000 units/mg

胰蛋白酶是一种丝氨酸蛋白水解酶,属白色或微黄色冻干粉制品。它能特异性地水解碱性氨基酸精氨酸及赖氨酸羧基所组成的肽键。酶本身很容易自溶，其作用最佳的PH值为8.0～9.0。胰蛋白酶活性能被胰腺中的天然抑制剂所抑制。钙离子能延迟胰蛋白酶的自溶，并能促进胰蛋白酶原的活性。 or trypsin digestion of peptides, use a ratio of about 1:100 to 1:20 for trypsin:peptide. The typical use for this product is in removing adherent cells from a culture surface. The concentration of trypsin necessary to dislodge cells from their substrate is dependent primarily on the cell type and the age of the culture. Trypsins have also been used for the re-suspension of cells during cell culture, in proteomics research for digestion of proteins and in various in-gel digestionsns?. Additional applications include assessing crystallization by membrane-based techniques and in a study to determine that protein folding rates and yields can be limited by the presence of kinetic traps. Trypsin is a single chain polypeptide of 223 amino acid residues and is a member of the serine protease family. The active site amino acid residues of trypsin include HIs46 and Ser183. Trypsin is produced by removing the N-terminal hexapeptide from trypsinogen which is cleaved at the peptide bonds at Lys6 - lle7. This cleavage yields a single chain native form of trypsin called β-Trypsin. Ensuing autolysis of β-Trypsin results in α-Trypsin having two peptide chains bound by disulphide bonds. This enzyme predominantly cleaves peptide chains at the carboxyl side of Arginine and Lysine, with an exception when either one is followed by a Proline. or trypsin digestion of peptides, use a ratio of about 1:100 to 1:20 for trypsin:peptide. The typical use for this product is in removing adherent cells from a culture surface. The concentration of trypsin necessary to dislodge cells from their substrate is dependent primarily on the cell type and the age of the culture. Trypsins have also been used for the re-suspension of cells during cell culture, in proteomics research for digestion of proteins and in various in-gel digestionsns?. Additional applications include assessing crystallization by membrane-based techniques and in a study to determine that protein folding rates and yields can be limited by the presence of kinetic traps.

胰蛋白酶可在赖氨酸和精氨酸残基的 C 端侧裂解肽。如果酸性残基位于裂解位点的两侧，水解速度就会减慢；如果脯氨酸残基位于裂解位点的羧基侧，水解就会停止。胰蛋白酶活性的最佳 pH 值为 7-9。胰蛋白酶还能裂解氨基酸合成衍生物的酯和酰胺连接。在胰蛋白酶溶液中加入乙二胺四乙酸（EDTA）作为螯合剂，可中和钙镁离子，因为钙镁离子会遮蔽胰蛋白酶作用的肽键。去除这些离子可提高酶的活性。