R7009
Sty I from Escherichia coli strain carrying pST27
buffered aqueous glycerol solution
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关于此项目
化学文摘社编号:
UNSPSC Code:
12352204
NACRES:
NA.53
MDL number:
Concentration:
10,000 units/mL
form
buffered aqueous glycerol solution
concentration
10,000 units/mL
shipped in
wet ice
storage temp.
−20°C
Biochem/physiol Actions
Recognition sequence: 5′-C/C(A,T)(T,A)GG-3′
Ligation and recutting results: After 2-10-fold Sty I overdigestion of 1 μg λ DNA substrate, results in 100% cutting, >95% of fragments can be ligated, and >95% recut.
Heat inactivation: Inactivated at 65 °C for 15 minutes.
Ligation and recutting results: After 2-10-fold Sty I overdigestion of 1 μg λ DNA substrate, results in 100% cutting, >95% of fragments can be ligated, and >95% recut.
Heat inactivation: Inactivated at 65 °C for 15 minutes.
Physical form
Solution in 20 mM Tris-HCl, pH 7.5, 0.1 mM EDTA, 50 mM KCl, 10 mM 2-mercaptoethanol, 0.1% gelatine (v/v), 0.01% polydocanol (v/v), 50% glycerol (v/v) at 4 °C
Other Notes
Supplied with 10x Restriction Endonuclease Buffer SH (B3657).
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K Mise et al.
Gene, 33(3), 357-361 (1985-01-01)
A new restriction endonuclease, StyI, free of contaminating nuclease activities, has been isolated from Escherichia coli carrying the hsd+ miniplasmid of Salmonella typhi origin. In the presence of 10 mM Mg2+, it recognizes and cleaves a hexanucleotide sequence of 5'-C
C Kessler et al.
Gene, 47(1), 1-153 (1986-01-01)
The properties and sources of all known restriction endonucleases and methylases are listed. The enzymes are cross-indexed (Table I), classified according to their recognition sequence homologies (Table II), and characterized within Table II by the cleavage and methylation positions, the
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