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Merck

R1003

Sigma-Aldrich

Ribonuclease T1 from Aspergillus oryzae

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

Sinónimos:

Guanyloribonuclease, Ribonucleate 3′-guanylo-oligonucleotidohydrolase

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About This Item

Número de CAS:
Comisión internacional de enzimas:
Número CE:
Número MDL:
Código UNSPSC:
12352204
NACRES:
NA.54

origen biológico

Aspergillus sp. (Aspergillus oryzae)

Nivel de calidad

formulario

ammonium sulfate suspension

actividad específica

300,000-600,000 units/mg protein

mol peso

11068 by amino acid sequence

técnicas

cell based assay: suitable

idoneidad

suitable for separating native or denatured proteins, or nucleic acids

aplicaciones

cell analysis

temp. de almacenamiento

2-8°C

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Aplicación

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

Acciones bioquímicas o fisiológicas

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.

Definición de unidad

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.

Forma física

Suspension in 2.8 M (NH4)2SO4 solution

Nota de análisis

Protein determined by E1%/280

Código de clase de almacenamiento

10 - Combustible liquids

Clase de riesgo para el agua (WGK)

WGK 3

Punto de inflamabilidad (°F)

Not applicable

Punto de inflamabilidad (°C)

Not applicable

Equipo de protección personal

Eyeshields, Gloves


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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

Artículos

Instructions for working with enzymes supplied as ammonium sulfate suspensions

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