R0754
Sal I from Streptomyces albus G
Restriction Enzyme
grade
Molecular Biology
form
buffered aqueous glycerol solution
concentration
10,000 units/mL
shipped in
wet ice
storage temp.
−20°C
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Application
SalI is a restriction endonuclease used for molecular biology methods to cleave DNA at the recognition sequence 5′-G/TCGAC-3′, generating fragments with 5′-cohesive ends.
Biochem/physiol Actions
Recognition sequence: 5′-G/TCGAC-3′
Cutting results: a 2-10-fold Sal I overdigestion of 1 μg λ DNA substrate results in 100% cutting
Heat inactivation: Inactivated at 65 °C for 15 minutes.
Cutting results: a 2-10-fold Sal I overdigestion of 1 μg λ DNA substrate results in 100% cutting
Heat inactivation: Inactivated at 65 °C for 15 minutes.
Physical form
Solution in 10 mM Tris-HCl, pH 7.5, 1 mM EDTA, 50% glycerol (v/v), 10 mM dithioerythritol, at 4 °C
Other Notes
One unit is the enzyme activity that completely cleaves 1 mg λDNA in 1 hr. at 37 °C in a total volume of 25 ml of buffer SH for restriction enzymes.
Supplied with 10x Restriction Enzyme Buffer SH (B3657)
Storage Class Code
12 - Non Combustible Liquids
WGK
WGK 3
Flash Point(F)
Not applicable
Flash Point(C)
Not applicable
Regulatory Information
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Antimicrobial agents and chemotherapy, 44(6), 1549-1555 (2000-05-19)
We have previously shown that the methicillin-resistance gene mecA of Staphylococcus aureus strain N315 is localized within a large (52-kb) DNA cassette (designated the staphylococcal cassette chromosome mec [SCCmec]) inserted in the chromosome. By sequence determination of the entire DNA
In situ preservation of DNA in plant species.
Pyle, M.M., and Adams, R.P.
Taxon, 38, 576-576 (1989)
A new restriction endonuclease from Streptomyces albus G.
J R Arrand et al.
Journal of molecular biology, 118(1), 127-135 (1978-01-05)
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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