Proteinase K

产品编号：V3021 品牌：promega 原厂货号：V3021
产品分类：蛋白质检测与分析 > 蛋白质，多肽和酶 > 蛋白酶 > 蛋白酶K
应用分类：

包装：

100mg

运保温度:

-20℃

到货周期：

登录后查看

标准价：

￥客户可见

会员价：

￥客户可见

积分：

客户可见分

登录之后可加入购物车购买，请您

运费与支付说明：

1.含干冰类产品有运费；

2. 必须现金付款或有信用额度的会员才可以直接发货，否则需要等待现金付款信息。

其它组分：

Proteinase K【子货号：V302B，包装：1 x 100mg，，运保温度：-20℃】

描述：

说明

Proteinase K( 蛋白酶K) 是从林伯氏白色念球菌(Tritirachium album Limber ) 中纯化得到的一种丝氨酸蛋白酶，切割活性较广。它切割脂肪族氨基酸和芳香族氨基酸的羧基端肽键，用于生物样品中蛋白质的一般性消化。该酶经纯化去除了RNA 酶和DNA 酶活性。由于蛋白酶K 在尿素和SDS 中稳定，还具有降解天然蛋白质的能力，因而它应用广泛，包括制备脉冲场凝胶电泳的染色体DNA，蛋白质指纹图谱以及去除DNA 和RNA 制备中的核酸酶。蛋白酶K 的一般工作浓度是50-100μg/ml。

形态：冻干粉。

推荐反应缓冲液：50mM Tris-HCl (pH 7.5),10mM CaCl₂。

特点

• 稳定：当pH 值范围在4.3-12.0 时，在0.5% SDS 溶液或1%Triton® X-100 溶液中，Proteinase K 都能保持活性；在温度高达60℃时，活性仍>80%。

原厂资料：

Proteinase K, produced by the fungus Tritirachium album Limber, is a serine protease that exhibits broad cleavage activity. It cleaves peptide bonds adjacent to the carboxylic group of aliphatic and aromatic amino acids and is useful for general digestion of protein in biological samples. It has been purified to remove RNase and DNase activities. The stability of Proteinase K in urea and SDS and its ability to digest native proteins make it useful for a variety of applications including preparation of chromosomal DNA for pulsed-field gel electrophoresis, protein fingerprinting and removal of nucleases from preparations of DNA and RNA. A typical working concentration for Proteinase K is 50–100μg/ml.

Form: Lyophilized powder.

Recommended Reaction Buffer: 50mM Tris-HCl (pH 8.0), 10mM CaCl2.

Features - Benefits

Stable: Active over a pH range of 4.3–12.0, in 0.5% SDS or 1% Triton® X-100 and retains >80% of its activity at temperatures up to 60°C.

References

Ebeling, W. et al. (1974) Eur. J. Biochem. 47, 91–7.
Schwartz, D.C. and Cantor, C.R. (1984) Cell 37, 67–75.
Cleveland, D.W. et al. (1977) J. Biol. Chem. 252, 1102–6.
Hames, B.D. (1981) In: Gel Electrophoresis of Proteins: A Practical Approach, B.D. Hames and D. Rickwood, eds., IRL Press, Oxford, 219.
Herrmann, B.G. and Frischauf, A.M. (1987) Meth. Enzymol. 152, 180–3.
Lee, J.J. and Costlow, N.A. (1987) Meth. Enzymol. 152, 633–48.
Sambrook, J. et al. (1989) Molecular Cloning: A Laboratory Manual, Vol. 3, Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY.
Sweeney, P.J. and Walker, J.M. (1993) Enzymes of molecular biology. In: Methods in Molecular Biology, Vol. 16, M.M. Burrell, ed., Humana Press, Inc., Totowa, NJ, 305.