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Ribonuclease T1 from Aspergillus oryzae

ammonium sulfate suspension, 300,000-600,000 units/mg protein

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Guanyloribonuclease, Ribonucleate 3′-guanylo-oligonucleotidohydrolase
CAS Number:
Enzyme Commission number:
EC Number:
MDL number:


ammonium sulfate suspension

Quality Level

specific activity

300,000-600,000 units/mg protein

mol wt

11068 by amino acid sequence

storage temp.


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This Item
specific activity

300,000-600,000 units/mg protein

specific activity

~10,000 units/mg protein

specific activity

≥40 units/mg protein

specific activity

≥70 Kunitz units/mg protein

mol wt

11068 by amino acid sequence

mol wt

53 kDa by equilibrium centrifugation

mol wt


mol wt

13.7 kDa, ~13,700

storage temp.


storage temp.


storage temp.


storage temp.



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.

Unit Definition

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

Storage Class Code

10 - Combustible liquids



Flash Point(F)

Not applicable

Flash Point(C)

Not applicable

Personal Protective Equipment

dust mask type N95 (US), Eyeshields, Gloves

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Ribonuclease T1: Structure, Function, and Stability
Pace, CN; Heinemann U, et al.
Angewandte Chemie (International Edition in English), 4, 343-360 (1991)
Elisa Bombarda et al.
The journal of physical chemistry. B, 114(5), 1994-2003 (2010-01-22)
Because of their central importance for understanding enzymatic mechanisms, pK(a) values are of great interest in biochemical research. It is common practice to determine pK(a) values of amino acid residues in proteins from NMR or FTIR titration curves by determining
Catherine Brands et al.
Journal of visualized experiments : JoVE, (160) (2020-07-07)
In situ hybridization is a powerful technique to identify specific RNA or DNA sequences within individual cells in tissue sections, providing important insights into physiological processes and disease pathogenesis. In situ hybridization (ISH) has been used for many years to
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


Instructions for working with enzymes supplied as ammonium sulfate suspensions

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