R5628
Hae III from Haemophilus aegyptius
Restriction Enzyme
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About This Item
CAS Number:
MDL number:
UNSPSC Code:
12352204
Recommended Products
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′-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.
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.
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.
Other Notes
Supplied with 10x Restriction Enzyme Buffer SM (B3158).
Comment: Inefficient for single-stranded DNA cleavage.
Hae III requires optimal reaction conditions in order to avoid star activity.
Hae III requires optimal reaction conditions in order to avoid star activity.
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
related product
Storage Class Code
10 - Combustible liquids
WGK
WGK 2
Flash Point(F)
Not applicable
Flash Point(C)
Not applicable
Certificates of Analysis (COA)
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Beatrix Kotlan et al.
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
Duplex regions in "single-stranded" phiX174 DNA are cleaved by a restriction endonuclease from Haemophilus aegyptius.
R W Blakesley et al.
The Journal of biological chemistry, 252(20), 7300-7306 (1977-10-25)
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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