产品名称

英文名称：Trypsin from bovin pancreas

产品性质

CAS编号：9002-07-7

EC号：232-650-8

MDL号：MFCD00082094

酶学委员会编号：3.4.21.4

规格或纯度：potency ≥3000 units/mg

英文名称：Trypsin from bovin pancreas

单位定义：一个BAEE单位以BAEE作为底物，在25°C、pH 7.6条件下每分钟每毫升产生0.001的ΔA253 。一个BTEE单位=320个ATEE单位。反应体积=3.2mL（1cm的光径）。

生化机理：Trypsin cleaves peptides on the C-terminal side of lysine and arginine residues. The rate of hydrolysis of this reaction is slowed if an acidic residue is on either side of the cleavage site and hydrolysis is stopped if a proline residue is on the carboxyl side of the cleavage site. The optimal pH for trypsin activity is 7-9. Trypsin can also act to cleave ester and amide linkages of synthetic derivatives of amino acids. EDTA is added to trypsin solutions as a chelating agent that neutralizes calcium and magnesium ions that obscure the peptide bonds on which trypsin acts. Removing these ions increases the enzymatic activity.

储存温度：-20°C储存

运输条件：超低温冰袋运输

产品介绍：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 1100 to 120 for trypsinpeptide. 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 1100 to 120 for trypsinpeptide. 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.

WGK Germany：1

RTECS：YN5075000

溶解性：Soluble in Hank's Balanced Salt Solution (35 mg/ml), HCl (1 mM), and water. Insoluble in clycerol, and alcohol.

敏感性：对光和湿度敏感

象形图：

信号词：Danger

危险声明：H315 Causes skin irritationH319 Causes serious eye irritationH335 May cause respiratory irritationH334 May cause allergy or asthma symptoms or breathing difficulties if inhaled

预防措施声明：P261,P342+P311

个人防护装备：dust mask type N95 (US), Eyeshields, Faceshields, Gloves

产品包装