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Merck
CN

R5628

Hae III 来源于埃及嗜血杆菌

Restriction Enzyme

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UNSPSC Code:
12352204
MDL number:
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grade

Molecular Biology

form

buffered aqueous glycerol solution

concentration

10,000 units/mL

shipped in

wet ice

storage temp.

−20°C

Application

HaeIII is a restriction enzyme that is used in molecular biology methods to cleave DNA at the recognition site 5′-GG/CC-3′ to generate DNA fragments with blunt termini.

Biochem/physiol Actions

Recognition sequence: 5′-GG/CC-3′
Ligation and recutting results: After 2-10-fold Hae III overdigestion of 1 μg λ DNA substrate, results in 100% cutting, >50% of fragments can be ligated, and >95% recut.
Heat inactivation: 80 °C for 20 minutes.

Physical form

Solution in 20 mM Tris-HCl, pH 7.7, 0.1 mM EDTA, 400 mM NaCl, 10 mM 2-mercaptoethanol, 50% glycerol (v/v) at 4°C

Other Notes

Comment: Inefficient for single-stranded DNA cleavage.
Hae III requires optimal reaction conditions in order to avoid star activity.
Supplied with 10x Restriction Enzyme Buffer SM (B3158).

存储类别

10 - Combustible liquids

wgk

WGK 2

flash_point_f

Not applicable

flash_point_c

Not applicable

法规信息

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Duplex regions in "single-stranded" phiX174 DNA are cleaved by a restriction endonuclease from Haemophilus aegyptius.
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Journal of immunology (Baltimore, Md. : 1950), 175(4), 2278-2285 (2005-08-06)
The potential tumor-recognizing capacity of B cells infiltrating human breast carcinoma is an important aspect of breast cancer biology. As an experimental system, we used human medullary breast carcinoma because of its heavy B lymphocytic infiltration paralleled to a relatively
Stefano Fazi et al.
Environmental microbiology, 10(10), 2760-2772 (2008-07-23)
We studied the diversity, community composition and activity of the primary microbial colonizers of the water above freshly re-wetted sediments from a temporary river. Dried sediments, collected from Mulargia River (Sardinia, Italy), were covered with sterile freshwater in triplicate microcosms
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
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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