R8631
Bcl I from Bacillus caldolyticus
Restriction Enzyme
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About This Item
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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
BclI is a restriction endonuclease used in molecular biology applications to cut DNA at the recognition sequence 5′-T/GATCA-3′, resulting in fragments with 5′-cohesive termini.
Biochem/physiol Actions
Recognition sequence: 5′-T/GATCA-3′
Cutting results: a 2-10-fold Bcl I overdigestion of 1 μg λ DNA substrate results in 100% cutting.
Heat inactivation: This enzyme cannot be heat inactivated at 65 °C for 15 minutes.
Cutting results: a 2-10-fold Bcl I overdigestion of 1 μg λ DNA substrate results in 100% cutting.
Heat inactivation: This enzyme cannot be heat inactivated at 65 °C for 15 minutes.
Physical form
Solution in 20 mM Tris-HCl, pH 8.0, 0.1 mM EDTA, 200 mM NaCl, 10 mM 2-Mercaptoethanol, 0.2 % Triton X-100 (v/v), 50% glycerol (v/v) at 4°C
Other Notes
Cleavage activity: Bcl I will only partially cleave DNA isolated from E. coli strains that have the dam methylase (dam+ strains).
Comment: Bcl I is optimally active at 50°C.
Comment: Bcl I is optimally active at 50°C.
Supplied with 10x Restriction Enzyme Buffer SM (B3158).
Storage Class
10 - Combustible liquids
wgk
WGK 1
flash_point_f
Not applicable
flash_point_c
Not applicable
Regulatory Information
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Bernd Kneidinger et al.
The Journal of biological chemistry, 278(6), 3615-3627 (2002-12-05)
N-Acetyl-l-fucosamine is a constituent of surface polysaccharide structures of Pseudomonas aeruginosa and Staphylococcus aureus. The three P. aeruginosa enzymes WbjB, WbjC, and WbjD, as well as the S. aureus homologs Cap5E, Cap5F, and Cap5G, involved in the biosynthesis of N-acetyl-l-fucosamine
A H Bingham et al.
Nucleic acids research, 5(10), 3457-3467 (1978-10-01)
The purification and characterization of a new restriction endonuclease, BclI from the extreme thermophile Bacillus caldolyticus is reported. This enzyme recognizes the sequence : formula: (see text) and cleaves at the positions indicated by the arrows.
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