胶原酶 NB 4 来源于溶组织梭菌

Collagenase I | Collagenase Type II | (5S,6S,9R,10S,13S,17S,23S,24S,27R,28S,31S,35S)-5,6,9,13,17,23,24,27,31,35-Decamethyl-10,28-dioctyl-2,20-diazanonacyclo[19.15.0.03,19.05,17.06,14.09,13.023,35.024,32.027,31]hexatriaconta-1(21),2,19-triene

C279013-500mg

500mg

EnzymoPure™

标准级,≥ 0.10 U/mg

描述 胶原酶NB 4是一种粗制胶原酶，包含胶原蛋白水解和其他酶促活性，包括梭菌蛋白酶和中性蛋白酶。这些活动的均衡比例确保了温和有效的组织解离。 应用 胶原酶NB 4适用于多种组织类型的解离。 规格 包含I类和II类胶原酶（1）和均衡比例的蛋白水解副活性。 活度：≥0.10 U / mg 适用于组织解离的不同应用，例如分离人和啮齿动物的肝细胞，软骨细胞，神经元和内皮细胞，成纤维细胞，来自脂肪组织的细胞（例如ADSC），干细胞和啮齿动物的成骨细胞。 （Clostridiopeptidase A） EC 3.4.24.3 • Mr ca. 70 000 - 120 000 (collagenases) • CAS [9001-12-1] 参考和定义 单位定义：1 U在25°C，pH 7.1下每分钟催化1 µmol 4-苯基偶氮苄氧基羰基-L-脯氨酰基-L-亮氨酰甘氨酰-L-脯氨酰基-D-精氨酸的水解。 References 1. Bond, M.D. & van Wart, H.E. (1984) Biochemistry 23, 3077-3091 2. Wünsch, E. & Heidrich, H.G. (1963) Hoppe-Seyler's Z. Physiol. Chem. 333, 149-51 Collagenase NB 4 is a crude collagenase that contains collagenolytic and additional enzymatic activities including clostripain and neutral protease. The balanced ratio of these activities ensures gentle and efficient tissue dissociation. Application Collagenase NB 4 is suitable for dissociation of a broad variety of tissue types. Specifications Contains class I and class II collagenase (1) and a balanced ratio of proteolytic side activities. Activity (Wünsch): ≥ 0.10 U/mg Suitable for different applications in tissue dissociation such as isolation of human and rodent hepatocytes, chondrocytes, neuronal and endothelial cells, fibroblasts, cells from adipose tissue (e.g. ADSCs), stem cells and rodent osteoblasts. (Clostridiopeptidase A) EC 3.4.24.3 • Mr ca. 70 000 - 120 000 (collagenases) • CAS [9001-12-1] References and Definitions Unit definition: 1 U according to Wünsch (2) catalyzes the hydrolysis of 1 µmole 4-phenylazobenzyloxycarbonyl-L-prolyl-L-leucylglycyl-L-prolyl-D-arginine per minute at 25 °C, pH 7.1. References 1. Bond, M.D. & van Wart, H.E. (1984) Biochemistry 23, 3077-3091 2. Wünsch, E. & Heidrich, H.G. (1963) Hoppe-Seyler's Z. Physiol. Chem. 333, 149-51