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R1003

Sigma-Aldrich

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
Enzyme Commission number:
3.1.27.3 (BRENDA, IUBMB)
EC Number:
232-809-1
MDL number:
MFCD00132191
UNSPSC Code:
12352204
NACRES:
NA.54

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.

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

WGK

WGK 3

Flash Point(F)

Not applicable

Flash Point(C)

Not applicable

Personal Protective Equipment

dust mask type N95 (US), Eyeshields, Gloves

Regulatory Listings

Regulatory Listings are mainly provided for chemical products. Only limited information can be provided here for non-chemical products. No entry means none of the components are listed. It is the user’s obligation to ensure the safe and legal use of the product.

JAN Code

R1003-100KU:
R1003-VAR:
R1003-BULK:
R1003-500KU:

Certificates of Analysis (COA)

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Caroline Haupt et al.
Journal of the American Chemical Society, 133(29), 11154-11162 (2011-06-15)
Slow protein folding processes during which kinetic folding intermediates occur for an extended time can lead to aggregation and dysfunction in living cells. Therefore, protein folding helpers have evolved, which prevent proteins from aggregation and/or speed up folding processes. In
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
Patrizia Contursi et al.
Extremophiles : life under extreme conditions, 14(5), 453-463 (2010-08-25)
The pSSVx from Sulfolobus islandicus, strain REY15/4, is a hybrid between a plasmid and a fusellovirus. A systematic study previously performed revealed the presence of nine major transcripts, the expression of which was differentially and temporally regulated over the growth
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
Colette M Castleberry et al.
Nucleic acids research, 38(16), e162-e162 (2010-07-01)
Transfer ribonucleic acids (tRNAs) are challenging to identify and quantify from unseparated mixtures. Our lab previously developed the signature digestion approach for identifying tRNAs without specific separation. Here we describe the combination of relative quantification via enzyme-mediated isotope labeling with
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