R4503
Sma I from Serratia marcescens Sb
Restriction Enzyme
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About This Item
CAS Number:
EC 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
Specificity
Recognition sequence: 5′-CCC/GGG-3′
Cutting results: a 2-10-fold Sma I overdigestion of 1 μg λ DNA substrate results in 100% cutting
Heat inactivation: 65 °C for 15 minutes.
Cutting results: a 2-10-fold Sma I overdigestion of 1 μg λ DNA substrate results in 100% cutting
Heat inactivation: 65 °C for 15 minutes.
Application
SmaI is a restriction endonuclease used to cut DNA at the recognition sequence 5′-CCC/GGG-3′, generating DNA fragments with blunt termini.
Other Notes
Supplied with 10x Restriction Enzyme Buffer SA (B7531).
Comment: Half-life of Sma I at 37 °C is approximately 15 minutes.
Linkage
Isoschizomer: Xma I. Unlike Xma I, Sma I produces blunt-ended fragments.
Unit Definition
One unit is the enzyme activity that completely cleaves 1 mg of λDNA in 1 hr. at 25 °C in a total volume of 25 ml of 1x digestion buffer SA forrestriction enzymes.
Physical form
Solution in 10 mM potassium phosphate, pH 7.0, 1 mM EDTA, 300 mM NaCl, 5 mM dithiothreitol, 50% glycerol (v/v) , 0.02% polydocanol (v/v), at 4 °C
incubation buffer
Product No.
Description
Pricing
related product
Storage Class
12 - Non Combustible Liquids
wgk_germany
WGK 3
flash_point_f
Not applicable
flash_point_c
Not applicable
ppe
Eyeshields, Gloves, multi-purpose combination respirator cartridge (US)
Certificates of Analysis (COA)
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Leila C Campos et al.
Diagnostic microbiology and infectious disease, 65(2), 112-115 (2009-08-28)
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D Savoia et al.
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Two restriction-like enzymes from Xanthomonas malvacearum.
S A Endow et al.
Journal of molecular biology, 112(3), 521-529 (1977-05-25)
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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