R6501
Ribonuclease H from Escherichia coli
recombinant, expressed in E. coli, buffered aqueous glycerol solution, 1,000-4,000 units/mL
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About This Item
CAS Number:
UNSPSC Code:
12352204
NACRES:
NA.54
MDL number:
Recombinant:
expressed in E. coli
Concentration:
1,000-4,000 units/mL
recombinant
expressed in E. coli
form
buffered aqueous glycerol solution
mol wt
17.6 kDa
packaging
vial of ~30 units
concentration
1,000-4,000 units/mL
shipped in
dry ice
storage temp.
−20°C
Application
Ribonuclease H from Escherichia coli has been used in a study to assess metallobiochemistry of the magnesium ion. Ribonuclease H has also been used in a study to investigate selective inhibitors of HIV-1 reverse transcriptase associated Rnase H activity.
Physical form
Solution in 50% glycerol containing 20 mM Tris-HCl, pH 7.5, 100 mM KCl, 10 mM MgCl2, 0.1 mM EDTA, 0.1 mM DTT and 0.05 mg BSA per ml
Other Notes
One unit hydrolyzes 1.0 nanomole RNA in 3H-labeled poly(A) • poly(dT) to acid soluble material in 20 min at 37 °C.
Storage Class
10 - Combustible liquids
wgk
WGK 2
flash_point_f
Not applicable
flash_point_c
Not applicable
Regulatory Information
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Jessica H Brehm et al.
Clinical infectious diseases : an official publication of the Infectious Diseases Society of America, 55(5), 737-745 (2012-05-24)
It is not known how often mutations in the connection and ribonuclease H domains of reverse transcriptase (RT) emerge with failure of first-line antiretroviral therapy (ART) in subtype C human immunodeficiency virus type 1 (HIV-1) infection and how these mutations
Virginie Suchaud et al.
Bioorganic & medicinal chemistry letters, 22(12), 3988-3992 (2012-05-23)
We report herein the synthesis of a series of 3-hydroxyquinolin-2(1H)-one derivatives. Esters and amide groups were introduced at position 4 of the basis scaffold and some modulations of the benzenic moiety were performed. Most compounds presented selective inhibitory properties in
H W Huang et al.
European journal of biochemistry, 219(1-2), 253-260 (1994-01-15)
Ribonuclease H (Escherichia coli) contains one strong magnesium-binding site, as determined by metal-titration experiments monitored by high field 1H-NMR and also by direct titration calorimetry. Kinetic and thermodynamic parameters were evaluated by 25Mg-NMR and were as follows: dissociation constant Kd
Mateusz Mendel et al.
Cell, 184(12), 3125-3142 (2021-05-01)
The N6-methyladenosine (m6A) RNA modification is used widely to alter the fate of mRNAs. Here we demonstrate that the C. elegans writer METT-10 (the ortholog of mouse METTL16) deposits an m6A mark on the 3' splice site (AG) of the S-adenosylmethionine
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