R4756
Rsa I from Rhodopseudomonas sphaeroides
Restriction Enzyme
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About This Item
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′-GT/AC-3′
Cutting results: a 2-10-fold Rsa I overdigestion of 1 μg λ DNA substrate results in 100% cutting
Heat inactivation: Inactivated at 65 °C for 20 minutes.
Cutting results: a 2-10-fold Rsa I overdigestion of 1 μg λ DNA substrate results in 100% cutting
Heat inactivation: Inactivated at 65 °C for 20 minutes.
Application
RsaI is a restriction endonuclease that is used in molecular biology methods to cut DNA at the recognition sequence 5′-GT/AC-3′ to generate DNA fragments with blunt termini.
Other Notes
Supplied with 10x Restriction Enzyme Buffer SL (B3782).
Comment: Rsa I cuts single-stranded DNA poorly.
Physical form
Solution in 40 mM Tris-HCl, pH 8.0, 0.1 mM EDTA, 100 mM NaCl, 10 mM 2-mercaptoethanol, 50% glycerol (v/v), 0.25% polydocanol (v/v) at 4 °C
related product
Storage Class
12 - Non Combustible Liquids
wgk_germany
WGK 1
flash_point_f
Not applicable
flash_point_c
Not applicable
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Characterization of nine microsatellite loci on endemic kangaroo rats Dipodomys simulans peninsularis from southern Baja California Peninsula.
Molecular Ecology Notes, 7, 127-127 (2007)
Journal of bacteriology, 142(2), 380-383 (1980-05-01)
A new type II sequence-specific endonuclease, RsaI, has been identified from Rhodopseudomonas sphaeroides strain 28/5. An RsaI purification scheme that yields enzyme which is free of contaminating exonuclease and phosphatase activities after a single column fractionation has been developed. The
Applied and environmental microbiology, 72(4), 2971-2981 (2006-04-07)
The structure and dynamics of small eukaryotes (cells with a diameter less than 5 microm) were studied over two consecutive years in an oligomesotrophic lake (Lake Pavin in France). Water samples were collected at 5 and 30 m below the
FEMS microbiology ecology, 70(1), 66-78 (2009-07-23)
This study examined the effects of temporal changes in bacterial community composition (BCC) and environmental factors on potential ectoenzymatic activities (alpha-glucosidase, beta-glucosidase, alkaline phosphatase and leucine aminopeptidase) in a lacustrine ecosystem (Sep reservoir, France). BCC was assessed by terminal restriction
Nucleic acids research, 41(1), 391-404 (2012-11-14)
Type IIB restriction-modification systems, such as BcgI, feature a single protein with both endonuclease and methyltransferase activities. Type IIB nucleases require two recognition sites and cut both strands on both sides of their unmodified sites. BcgI cuts all eight target
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