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Merck
모든 사진(1)

주요 문서

R1003

Sigma-Aldrich

Ribonuclease T1 from Aspergillus oryzae

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

동의어(들):

Guanyloribonuclease, Ribonucleate 3′-guanylo-oligonucleotidohydrolase

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About This Item

CAS Number:
효소 위원회 번호:
EC Number:
MDL number:
UNSPSC 코드:
12352204
NACRES:
NA.54

생물학적 소스

Aspergillus sp. (Aspergillus oryzae)

Quality Level

양식

ammonium sulfate suspension

특이 활성도

300,000-600,000 units/mg protein

분자량

11068 by amino acid sequence

기술

cell based assay: suitable

적합성

suitable for separating native or denatured proteins, or nucleic acids

응용 분야

cell analysis

저장 온도

2-8°C

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애플리케이션

Ribonuclease T1 (RNase T1) from Aspergillus oryzae is used to digest denatured RNA prior to sequencing and is used for protein folding studies .

생화학적/생리학적 작용

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.

단위 정의

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.

물리적 형태

Suspension in 2.8 M (NH4)2SO4 solution

분석 메모

Protein determined by E1%/280

Storage Class Code

10 - Combustible liquids

WGK

WGK 3

Flash Point (°F)

Not applicable

Flash Point (°C)

Not applicable

개인 보호 장비

Eyeshields, Gloves


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문서 라이브러리 방문

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

문서

Instructions for working with enzymes supplied as ammonium sulfate suspensions

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