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DNA酶I 來源于牛胰腺(無Ribonuclease & Protease), ≥2,000 units/mg dry weight
??【編號(hào)】:128591

??【產(chǎn)品名稱】:DNA酶I 來源于牛胰腺(無Ribonuclease & Protease), ≥2,000 units/mg dry weight

??【規(guī)格】:2.5KU

??【用途】:

  DNA酶I 來源于牛胰腺(無Ribonuclease & Protease), ≥2,000 units/mg dry weight

  Product Name: Deoxyribonuclease I from Bovine Pancreas(Ribonuclease&Protease Free)
  別名:脫氧核糖核酸酶 I;脫氧核糖核酸 5′-寡核苷酸-水解酶
  CAS號(hào):9003-98-9
  介紹: Bovine pancreatic deoxyribonuclease is an endonuclease which splits phosphodiester linkages, preferentially adjacent to a pyrimidine nucleotide yielding polynucleotides with free hydroxyl group at the 3' position and phosphate group at the 5' position. The average chain length of a limit digest is a tetranucleotide.
  用途: 用于從蛋白質(zhì)樣品中除去 DNA。 Deoxyribonuclease I from bovine pancreas has been used in a study to compare several procedures for reducing RNase contamination in preparations of DNase. Deoxyribonuclease I from bovine pancreas has also been used in a study to investigate the effect of the composition of sodium dodecyl sulfate preparations on the renaturation of enzymes after polyacrylamide gel electrophoresis.
  貯存: 儲(chǔ)存溫度2-8℃
  敏感性: 易潮濕
  生化和生理學(xué)機(jī)理: DNase I is an endonuclease that acts on phosphodiester bonds adjacent to pyrimidines to produce polynucleotides with terminal 5′-phosphates. In the presence of Mg2+, DNAse I cleaves each strand of DNA independently and the cleavage sites are random. Both DNA strands are cleaved at approximately the same site in the presence of Mn2+. Divalent cations such as Mn2+, Ca2+, Co2+, and Zn2+ are activators of the enzyme. A concentration of 5 mM Ca2+ stabilizes the enzyme against proteolytic digestion. The pH optimum is found to be between 7 and 8. DNAse I from bovine pancreas consists of four chromatographically distinguishable components, A, B, C, and D, with their molar ratios being 4:1:1 respectively. Only minor amounts of D are found. 2-Mercaptoethanol, chelators, sodium dodecyl sulfate (SDS)6 and actin7 are known to inhibit the enzyme activity.
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