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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
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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 [1].

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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Certificados de análisis (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.
Herry Martadinata et al.
Biochemistry, 50(29), 6455-6461 (2011-06-16)
The discovery of long RNA transcripts of telomeric repeats (TERRA) and their potential to form G-quadruplexes stimulated studies on the possible arrangements of G-quadruplexes along TERRA. Here we performed ribonuclease protection assay to investigate the structures formed by long human
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
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

Artículos

Instructions for working with enzymes supplied as ammonium sulfate suspensions

Questions

1–2 of 2 Questions  
  1. This product was in powder form before and is now in liquid form. Do you still have to inactivate 20 min at 80°C before use? Thank you very much

    1 answer
    1. This product is an ammonium sulfate suspension. This is an enzyme, and batch-specific Certificates of Analysis report the activity of the enzyme. Most customers use it as an active enzyme. Please reach out to local technical support for clarification on using the inactivated form of the enzyme.

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  2. Is it possible to store this product frozen at -20°C?

    1 answer
    1. Storing ammonium sulfate suspensions of proteins frozen can lead to the removal of ammonium sulfate from the protein crystal structure. This exposes the protein to a high amount of ammonium sulfate, potentially causing denaturation due to high salt content. Consequently, the enzyme activity may decrease, as may have occurred in this instance. It is recommended that the customer purchase a new bottle and store it at 2-8°C.

      Helpful?

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