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Key Documents

R8631

Sigma-Aldrich

Bcl I from Bacillus caldolyticus

Restriction Enzyme

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About This Item

CAS Number:
Enzyme Commission number:
MDL number:
UNSPSC Code:
12352204

grade

for molecular biology

form

buffered aqueous glycerol solution

concentration

10,000 units/mL

shipped in

wet ice

storage temp.

−20°C

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Specificity

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.

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.

Other Notes

Supplied with 10x Restriction Enzyme Buffer SM (B3158).
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.

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

Storage Class

10 - Combustible liquids

wgk_germany

WGK 1

flash_point_f

Not applicable

flash_point_c

Not applicable


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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
Rachel M Smith et al.
Nucleic acids research, 41(1), 391-404 (2012-11-14)
Type IIB restriction-modification systems, such as BcgI, feature a single protein with both endonuclease and methyltransferase activities. Type IIB nucleases require two recognition sites and cut both strands on both sides of their unmodified sites. BcgI cuts all eight target
Nico Mitro et al.
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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