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Hind III from Haemophilus influenzae

Restriction Enzyme

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CAS Number:
Enzyme Commission number:
MDL number:


for molecular biology


buffered aqueous glycerol solution


≥10000 units/mL
10,000 units/mL

shipped in

wet ice

storage temp.


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Recognition sequence: 5′-A/AGCTT-3′
Cutting results: 2-10-fold Hind III overdigestion of 1 μg λ DNA substrate results in 100% cutting
Heat inactivation: 65 °C for 15 minutes


HindIII, a restriction endonuclease, is used in molecular biology applications to cleave DNA at the recognition site 5′-A/AGCTT-3′ to generate DNA fragments with cohesive 5′-ends.

Other Notes

Supplied with 10x Restriction Enzyme Buffer SB (B8781)
Comment: Hind III under suboptimal reaction conditions will cleave secondary recognition sites (star activity).

Physical form

Solution in 10 mM Tris-HCl, pH 7.5, 0.1 mM EDTA, 1 mM dithioerythritol, 250 mM NaCl, 0.01% polydocanol (v/v), 50% glycerol (v/v) at 4 °C

incubation buffer

Product No.

Storage Class Code

12 - Non Combustible Liquids



Flash Point(C)

Not applicable

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Stephen J King et al.
Molecular biology of the cell, 14(12), 5089-5097 (2003-10-21)
Cytoplasmic dynein and dynactin are megadalton-sized multisubunit molecules that function together as a cytoskeletal motor. In the present study, we explore the mechanism of dynein-dynactin binding in vitro and then extend our findings to an in vivo context. Solution binding
M Hsu et al.
Biochemistry, 17(1), 131-138 (1978-01-10)
In the presence of 100 mM Tris buffer (pH 7.5) and 1-10 mM Mg2+ EcoRI endonuclease cleaves DNA at a specific nucleotide sequence and in a characteristic way: -GAATTC-. But if Mg2+ is replaced by Mn2+, the specificity of the
Tomás Brdicka et al.
The Journal of experimental medicine, 196(12), 1617-1626 (2002-12-18)
A key molecule necessary for activation of T lymphocytes through their antigen-specific T cell receptor (TCR) is the transmembrane adaptor protein LAT (linker for activation of T cells). Upon TCR engagement, LAT becomes rapidly tyrosine phosphorylated and then serves as
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
Beata Podgórska et al.
Acta biochimica Polonica, 59(4), 669-672 (2012-11-07)
In this work we describe a novel, rapid and simple microscale procedure for identification of restriction endonuclease activity in bacteria lysates, which contain high levels of non-specific DNA nucleases.

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