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BamH I from Bacillus amyloliquefaciens H

Restriction Enzyme

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CAS Number:
Enzyme Commission number:
MDL number:


for molecular biology


buffered aqueous glycerol solution


10,000 units/mL

shipped in

wet ice

storage temp.


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Recognition sequence: 5′-G/GATCC-3′
Cutting results: a 2-10-fold Bam HI overdigestion of 1 μg λ DNA substrate results in 100% cutting
Heat inactivation: 60 °C for 15 minutes.
Star activity: To prevent star activity, avoid suboptimal reaction conditions containing low salt concentration, high glycerol (>5%) and high pH 8.0.


BamHI is a DNA restriction endonuclease that is used in molecular biology applications to cleave DNA at the recognition sequence 5′-G/GATCC-3′ to generate 5′-cohesive termini.

Other Notes

Supplied with 10x Restriction Enzyme Buffer SB (B8781).

Physical form

Solution in 10 mM Tris-HCl, pH 7.4 , 1 mM EDTA, 1mM dithioerythritol, 300 mM KCl, 0.01% Polydocanol (v/v), 50% glycerol (v/v), at 4°C

incubation buffer

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J H Ellis et al.
Journal of immunology (Baltimore, Md. : 1950), 156(8), 2700-2709 (1996-04-15)
CD80 and CD86 are cell surface glycoproteins expressed on a variety of professional APCs. They have attracted much attention due to their function as potent costimulators of T lymphocyte function through their interaction with CD28 and possibly CTLA4. Because inhibitors
Isolation of a sequence-specific endonuclease (BamI) from Bacillus amyloliquefaciens H.
G A Wilson et al.
Journal of molecular biology, 97(1), 123-125 (1975-09-05)
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
TALENs and ZFNs are associated with different mutation signatures.
Yongsub Kim et al.
Nature methods, 10(3), 185-185 (2013-02-12)
Cong Zhu et al.
Nucleic acids research, 41(4), 2455-2465 (2013-01-11)
Zinc-finger nucleases (ZFNs) have been used for genome engineering in a wide variety of organisms; however, it remains challenging to design effective ZFNs for many genomic sequences using publicly available zinc-finger modules. This limitation is in part because of potential

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