R1003
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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Número CAS:
UNSPSC Code:
12352204
NACRES:
NA.54
EC Number:
232-809-1
MDL number:
Specific activity:
300,000-600,000 units/mg protein
Biological source:
Aspergillus sp. (Aspergillus oryzae)
Servicio técnico
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Permítanos ayudarlebiological source
Aspergillus sp. (Aspergillus oryzae)
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
Quality Level
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.
ppe
Eyeshields, Gloves
Clase de almacenamiento
10 - Combustible liquids
wgk
WGK 3
flash_point_f
Not applicable
flash_point_c
Not applicable
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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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