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R1003

Sigma-Aldrich

Ribonuclease T1 from Aspergillus oryzae

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

Sinônimo(s):

Guanyloribonuclease, Ribonucleate 3′-guanylo-oligonucleotidohydrolase

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About This Item

Número CAS:
9026-12-4
Número da licença da enzima:
3.1.27.3 (BRENDA, IUBMB)
Número CE:
232-809-1
Número MDL:
MFCD00132191
Código UNSPSC:
12352204
NACRES:
NA.54

fonte biológica

Aspergillus sp. (Aspergillus oryzae)

Nível de qualidade

200

forma

ammonium sulfate suspension

atividade específica

300,000-600,000 units/mg protein

peso molecular

11068 by amino acid sequence

técnica(s)

cell based assay: suitable

adequação

suitable for separating native or denatured proteins, or nucleic acids

aplicação(ões)

cell analysis

temperatura de armazenamento

2-8°C

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Aplicação

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

Ações bioquímicas/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.

Definição da unidade

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 análise

Protein determined by E1%/280

Código de classe de armazenamento

10 - Combustible liquids

Classe de risco de água (WGK)

WGK 3

Ponto de fulgor (°F)

Not applicable

Ponto de fulgor (°C)

Not applicable

Equipamento de proteção individual

Eyeshields, Gloves

Certificados de análise (COA)

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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
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