R8381
Dpn I from Diplococcus pneumoniae
Restriction Enzyme
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About This Item
Produtos recomendados
grau
for molecular biology
forma
buffered aqueous glycerol solution
concentração
10,000 units/mL
Condições de expedição
wet ice
temperatura de armazenamento
−20°C
Especificidade
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.
Aplicação
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.
Outras notas
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.
forma física
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
produto relacionado
tampão de incubação
Nº do produto
Descrição
Preços
Código de classe de armazenamento
10 - Combustible liquids
Classe de risco de água (WGK)
WGK 1
Ponto de fulgor (°F)
Not applicable
Ponto de fulgor (°C)
Not applicable
Certificados de análise (COA)
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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.
Journal of molecular endocrinology, 30(3), 359-368 (2003-06-07)
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The Journal of biological chemistry, 278(15), 12769-12778 (2003-02-01)
The human and rat forms of the Kv2.1 channel have identical amino acids over the membrane-spanning regions and differ only in the N- and C-terminal intracellular regions. Rat Kv2.1 activates much faster than human Kv2.1. Here we have studied the
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
Methods in molecular biology (Clifton, N.J.), 952, 137-144 (2012-10-27)
The role of certain amino acids in the interactions of ligands with their cognate nuclear receptors is usually achieved by the resolution of the crystal structure of the receptor complexed with the ligand. As a complementary functional approach, site-directed mutagenesis
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