R8381
Dpn I from Diplococcus pneumoniae
Restriction Enzyme
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About This Item
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Qualität
for molecular biology
Form
buffered aqueous glycerol solution
Konzentration
10,000 units/mL
Versandbedingung
wet ice
Lagertemp.
−20°C
Spezifität
Recognition sequence: 5′-GmA/TC-3′
Ligation and recutting results: After 2-10-fold Dpn I overdigestion of 1 μg pBR322 DNA substrate, results in 100% cutting, >30% of fragments can be ligated, and >90% recut.
Heat inactivation: 75 °C for 15 minutes.
Ligation and recutting results: After 2-10-fold Dpn I overdigestion of 1 μg pBR322 DNA substrate, results in 100% cutting, >30% of fragments can be ligated, and >90% recut.
Heat inactivation: 75 °C for 15 minutes.
Anwendung
DpnI is a restriction endonuclease that is used in molecular biological applications to cleave the recognition sequence 5′-GmA/TC-3′, generating DNA framents with blunt ends.
Sonstige Hinweise
Supplied with 10x Restriction Enzyme Buffer SA (B7531).
Comment: Since Dpn I will completely cleave only fully methylated pBR322 DNA, cleavage of 95% or more is considered complete digestion.
Physikalische Form
Solution in 10 mM Tris-HCl, pH 8.0, 400 mM NaCl, 0.1 mM EDTA, 1 mM dithiothreitol, 200 μg/ml BSA, 50% glycerol (v/v) at 4 °C
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S Lacks et al.
The Journal of biological chemistry, 250(11), 4060-4066 (1975-06-10)
A deoxyribonuclease specific for methylated DNA was isolated from Diplococcus pneumoniae. The enzyme, an endonuclease, degrades DNA for Escherichia coli to fragments of average molecular weight about half a million; it forms discrete fragments from phage lambda DNA. Methyl-deficient E.
Min Ju et al.
The Journal of biological chemistry, 278(15), 12769-12778 (2003-02-01)
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Journal of molecular endocrinology, 30(3), 359-368 (2003-06-07)
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C Kessler et al.
Gene, 92(1-2), 1-248 (1990-08-16)
The properties and sources of all known class-I, class-II and class-III restriction endonucleases (ENases) and DNA modification methyltransferases (MTases) are listed and newly subclassified according to their sequence specificity. In addition, the enzymes are distinguished in a novel manner according
Cong Zhu et al.
Nucleic acids research, 41(4), 2455-2465 (2013-01-11)
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