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Molecular Biology
form
buffered aqueous glycerol solution
concentration
10,000 units/mL
shipped in
wet ice
storage temp.
−20°C
Application
BglII is a DNA restriction enzyme used for molecular biology methods to cut the recognition sequence 5′-A/GATCT-3′,generating DNA fragments with 5′-cohesive ends.
Biochem/physiol Actions
Recognition sequence: 5′-A/GATCT-3′
Cutting results: a 2-10-fold Bgl II overdigestion of 1 μg λ DNA substrate results in 100% cutting
Heat Inactivation: This enzyme cannot be heat inactivated.
Cutting results: a 2-10-fold Bgl II overdigestion of 1 μg λ DNA substrate results in 100% cutting
Heat Inactivation: This enzyme cannot be heat inactivated.
Physical form
Solution in 20 mM Tris-HCl, pH 7.5, 1 mM EDTA, 200 mM NaCl, 10 mM 2-mercaptoethanol, 0.01% polydocanol (v/v), 50% glycerol (v/v) at 4°C
Other Notes
Supplied with 10x Restriction Enzyme Buffer SM (B3158).
存储类别
12 - Non Combustible Liquids
wgk
WGK 1
flash_point_f
Not applicable
flash_point_c
Not applicable
法规信息
新产品
此项目有
V Pirrotta
Nucleic acids research, 3(7), 1747-1760 (1976-07-01)
The sites of action of the restriction enzyme Bgl II on lambda DNA are mapped. This enzyme recognises the sequence 5' ...AGATCT...3' and makes staggered cuts producing sticky ends. In lambda DNA, the second A in this sequence is methylated
P Manivasakam et al.
Nucleic acids research, 29(23), 4826-4833 (2001-12-01)
Mammalian cells repair DNA double-strand breaks by illegitimate end-joining or by homologous recombination. We investigated the effects of restriction enzymes on illegitimate and homologous DNA integration in mammalian cells. A plasmid containing the neo(R) expression cassette, which confers G418 resistance
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