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Merck
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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:
9026-12-4
EC Number:
3.1.27.3 (BRENDA, IUBMB)
EC Number:
232-809-1
MDL number:
MFCD00132191
UNSPSC Code:
12352204
NACRES:
NA.54

Key Documents

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biological source

Aspergillus sp. (Aspergillus oryzae)

Quality Level

200

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

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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.

Physical form

Suspension in 2.8 M (NH4)2SO4 solution

Analysis Note

Protein determined by E1%/280

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.

Storage Class Code

10 - Combustible liquids

WGK

WGK 3

Flash Point(F)

Not applicable

Flash Point(C)

Not applicable

Personal Protective Equipment

dust mask type N95 (US), Eyeshields, Gloves

Regulatory Information

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Certificates of Analysis (COA)

Lot/Batch Number
0000497745
0000497745
0000497742
0000497742
0000491215

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Rasmus Lybech Jensen et al.
Journal of the American Chemical Society, 134(23), 9820-9826 (2012-05-19)
Singlet molecular oxygen, O(2)(a(1)Δ(g)), can influence many processes pertinent to the function of biological systems, including events that result in cell death. Many of these processes involve a reaction between singlet oxygen and a given amino acid in a protein.
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
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
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
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
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