R1003
Ribonuclease T1 from Aspergillus oryzae
ammonium sulfate suspension, 300,000-600,000 units/mg protein
Synonym(s):
Guanyloribonuclease, Ribonucleate 3′-guanylo-oligonucleotidohydrolase
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About This Item
CAS Number:
UNSPSC Code:
12352204
NACRES:
NA.54
EC Number:
232-809-1
MDL number:
Specific activity:
300,000-600,000 units/mg protein
Biological source:
Aspergillus sp. (Aspergillus oryzae)
biological source
Aspergillus sp. (Aspergillus oryzae)
form
ammonium sulfate suspension
specific activity
300,000-600,000 units/mg protein
mol wt
11068 by amino acid sequence
technique(s)
cell based assay: suitable
suitability
suitable for separating native or denatured proteins, or nucleic acids
application(s)
cell analysis
storage temp.
2-8°C
Quality Level
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Other Notes
One unit will produce acid soluble oligonucleotides equivalent to a ΔA260 of 1.0 in 15 min at pH 7.5 at 37°C, in a reaction volume of 1.0 mL. Substrate: Yeast RNA.
Physical form
Suspension in 2.8 M (NH4)2SO4 solution
Analysis Note
Protein determined by E1%/280
Application
Ribonuclease T1 (RNase T1) from Aspergillus oryzae is used to digest denatured RNA prior to sequencing and is used for protein folding studies .
Biochem/physiol Actions
Ribonuclease T1 (RNase T1) from Aspergillus oryzae is an endoribonuclease that hydrolyzes after G residues. Cleavage occurs between the 3′-phosphate group of a guanidine ribonucleotide and 5′-hydroxyl of the adjacent nucleotide. The initial product is a 2′:3′ cyclic phosphate nucleoside that is hydrolyzed to the corresponding 3′-nucleoside phosphate. It differs from Pancreatic RNase in that it attacks the guanine sites specifically to yield 3′-GMP and oligonucleotides with a 3′-GMP terminal group.
Storage Class
10 - Combustible liquids
wgk
WGK 3
flash_point_f
Not applicable
flash_point_c
Not applicable
ppe
Eyeshields, Gloves
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Herry Martadinata et al.
Biochemistry, 50(29), 6455-6461 (2011-06-16)
The discovery of long RNA transcripts of telomeric repeats (TERRA) and their potential to form G-quadruplexes stimulated studies on the possible arrangements of G-quadruplexes along TERRA. Here we performed ribonuclease protection assay to investigate the structures formed by long human
C Nick Pace et al.
Journal of molecular biology, 408(3), 514-528 (2011-03-08)
Our goal was to gain a better understanding of the contribution of hydrophobic interactions to protein stability. We measured the change in conformational stability, Δ(ΔG), for hydrophobic mutants of four proteins: villin headpiece subdomain (VHP) with 36 residues, a surface
S Dubey et al.
Journal of controlled release : official journal of the Controlled Release Society, 152(3), 356-362 (2011-03-15)
Cathodal iontophoresis of anionic macromolecules has been considered a major challenge owing to (i) the presence of a negative charge on the skin under physiological conditions and (ii) the electroosmotic solvent flow in the (opposite) anode-to-cathode direction. Moreover, electroosmosis, and
Isil Severcan et al.
Nature chemistry, 2(9), 772-779 (2010-08-24)
Supramolecular assembly is a powerful strategy used by nature to build nanoscale architectures with predefined sizes and shapes. With synthetic systems, however, numerous challenges remain to be solved before precise control over the synthesis, folding and assembly of rationally designed
Scott Quarrier et al.
RNA (New York, N.Y.), 16(6), 1108-1117 (2010-04-24)
Structure mapping experiments (using probes such as dimethyl sulfate [DMS], kethoxal, and T1 and V1 RNases) are used to determine the secondary structures of RNA molecules. The process is iterative, combining the results of several probes with constrained minimum free-energy
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