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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
BglI is a restriction enzymes used in molecular biology studies to cut DNA at the recognition sequence 5′-GCC(N)4/NGGC-3′, generating DNA fragments with 3′-cohesive termini.
Biochem/physiol Actions
Recognition sequence: 5′-GCC(N)4/NGGC-3′
Ligation and recutting results: After 2-10-fold Bgl I overdigestion of 1 μg λ DNA substrate, results in 100% cutting, >70% of fragments can be ligated, and >90% recut.
Heat inactivation: Inactivation is achieved at 65 °C for 15 minutes.
Ligation and recutting results: After 2-10-fold Bgl I overdigestion of 1 μg λ DNA substrate, results in 100% cutting, >70% of fragments can be ligated, and >90% recut.
Heat inactivation: Inactivation is achieved at 65 °C for 15 minutes.
Physical form
Solution in 50 mM Tris-HCl, pH 7.0, 1 mM EDTA, 200 mM NaCl, 7 mM 2-Mercaptoethanol, 50% glycerol (v/v) at 4°C
Other Notes
Supplied with 10x Restriction Endonuclease Buffer SH (B 3657).
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Polymerase chain reaction-restriction fragment length polymorphism (PCR-RFLP) analysis and plasmid profile of soil and clinical isolates of Nocardia.
Qasem, J.A., et al.
Journal of applied genetics, 154, 157-157 (1999)
Tomasz Szreder et al.
Journal of applied genetics, 45(2), 225-236 (2004-05-08)
Due to the functions that estrogens play in the regulation of reproduction, development of the mammary gland, growth and differentiation of cells, estrogen receptors and their genes are considered candidates for the markers of production and functional traits in farm
Y H Lee et al.
The Journal of biological chemistry, 254(15), 6838-6841 (1979-08-10)
The sequence-specific endonuclease Bgl I from Bacillus globigii (RUB561) has been purified to homogeneity as determined by denaturing polyacrylamide gel analysis. The active form of the enzyme is a single polypeptide with a molecular weight of 32,000. The enzyme requires
Virulence factors of Escherichia coli strains belonging to serogroups O127 and O142.
Ghilardi, A.C.R., et al.
Epidem. Inf., 131, 815-815 (2003)
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
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