grade
Molecular Biology
form
buffered aqueous glycerol solution
concentration
10,000 units/mL
shipped in
wet ice
storage temp.
−20°C
Application
EclXI is a DNA restricition enzyme used in molecular biology applications to cleave DNA at the recognition site 5′-C/GGCCG-3′ to generate fragments with 5′-cohesive ends.
Biochem/physiol Actions
Recognition sequence: 5′-C/GGCCG-3′
Ligation and recutting results: After 2-10-fold EclX I overdigestion of 1 μg λ DNA substrate, results in 100% cutting, >95% of fragments can be ligated, and >95% recut.
Heat inactivation: 65 °C for 20 minutes.
Ligation and recutting results: After 2-10-fold EclX I overdigestion of 1 μg λ DNA substrate, results in 100% cutting, >95% of fragments can be ligated, and >95% recut.
Heat inactivation: 65 °C for 20 minutes.
Physical form
Solution in 20 mM Tris-HCl, pH 7.5, 0.1 mM EDTA, 100 mM NaCl, 10 mM 2-mercaptoethanol, 50% glycerol (v/v),100 μg/ml BSA, 0.05% polydocanol, 100 mg/ml hydroxy-ectione at 4°C
Other Notes
Supplied with 10x Restriction Enzyme Buffer SB (B8781).
Isoschizomer: Xma III
存储类别
12 - Non Combustible Liquids
wgk
WGK 1
flash_point_f
Not applicable
flash_point_c
Not applicable
法规信息
新产品
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EclXI, a novel isoschizomer of XmaIII from Enterobacter cloacae 590 recognizing 5'-C/GGCCG-3'.
B J Bolton et al.
Nucleic acids research, 18(2), 381-381 (1990-01-25)
Sabine Traver et al.
The Biochemical journal, 379(Pt 3), 627-632 (2004-04-29)
RGS (regulator of G-protein signalling) proteins stimulate the intrinsic GTPase activity of the a subunits of heterotrimeric G-proteins, and thereby negatively regulate G-protein-coupled receptor signalling. RGS14 has been shown previously to stimulate the GTPase activities of Ga(o) and Ga(i) subunits
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