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R1003

Sigma-Aldrich

Ribonuclease T1 from Aspergillus oryzae

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

Synonyme(s) :

Guanyloribonuclease, Ribonucleate 3′-guanylo-oligonucleotidohydrolase

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About This Item

Numéro CAS:
9026-12-4
Numéro de classification (Commission des enzymes):
3.1.27.3 (BRENDA, IUBMB)
Numéro CE :
232-809-1
Numéro MDL:
MFCD00132191
Code UNSPSC :
12352204
Nomenclature NACRES :
NA.54

Source biologique

Aspergillus sp. (Aspergillus oryzae)

Forme

ammonium sulfate suspension

Activité spécifique

300,000-600,000 units/mg protein

Poids mol.

11068 by amino acid sequence

Technique(s)

cell based assay: suitable

Adéquation

suitable for separating native or denatured proteins, or nucleic acids

Application(s)

cell analysis

Température de stockage

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 .

Actions biochimiques/physiologiques

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.

Définition de l'unité

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.

Forme physique

Suspension in 2.8 M (NH4)2SO4 solution

Remarque sur l'analyse

Protein determined by E1%/280

Code de la classe de stockage

10 - Combustible liquids

Classe de danger pour l'eau (WGK)

WGK 3

Point d'éclair (°F)

Not applicable

Point d'éclair (°C)

Not applicable

Équipement de protection individuelle

Eyeshields, Gloves

Certificats d'analyse (COA)

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Ribonuclease T1: Structure, Function, and Stability
Pace, CN; Heinemann U, et al.
Angewandte Chemie (International Edition in English), 4, 343-360 (1991)
Rasmus Lybech Jensen et al.
Journal of the American Chemical Society, 134(23), 9820-9826 (2012-05-19)
Singlet molecular oxygen, O(2)(a(1)Δ(g)), can influence many processes pertinent to the function of biological systems, including events that result in cell death. Many of these processes involve a reaction between singlet oxygen and a given amino acid in a protein.
C Nick Pace et al.
Journal of molecular biology, 408(3), 514-528 (2011-03-08)
Our goal was to gain a better understanding of the contribution of hydrophobic interactions to protein stability. We measured the change in conformational stability, Δ(ΔG), for hydrophobic mutants of four proteins: villin headpiece subdomain (VHP) with 36 residues, a surface
S Dubey et al.
Journal of controlled release : official journal of the Controlled Release Society, 152(3), 356-362 (2011-03-15)
Cathodal iontophoresis of anionic macromolecules has been considered a major challenge owing to (i) the presence of a negative charge on the skin under physiological conditions and (ii) the electroosmotic solvent flow in the (opposite) anode-to-cathode direction. Moreover, electroosmosis, and
Isil Severcan et al.
Nature chemistry, 2(9), 772-779 (2010-08-24)
Supramolecular assembly is a powerful strategy used by nature to build nanoscale architectures with predefined sizes and shapes. With synthetic systems, however, numerous challenges remain to be solved before precise control over the synthesis, folding and assembly of rationally designed
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How to Work with Enzymes Supplied as Ammonium Sulfate Suspensions

Instructions for working with enzymes supplied as ammonium sulfate suspensions

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