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Key Documents

R4756

Sigma-Aldrich

Rsa I from Rhodopseudomonas sphaeroides

Restriction Enzyme

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About This Item

CAS Number:
Enzyme Commission number:
MDL number:
UNSPSC Code:
12352204

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.

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

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.
Vega, A.M., et al.
Molecular Ecology Notes, 7, 127-127 (2007)
S P Lynn et al.
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
Cécile Lepère et al.
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
Delphine Boucher et al.
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
Rachel M Smith et al.
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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