R1003
Ribonuclease T1 from Aspergillus oryzae
ammonium sulfate suspension, 300,000-600,000 units/mg protein
동의어(들):
Guanyloribonuclease, Ribonucleate 3′-guanylo-oligonucleotidohydrolase
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크기 선택
제품정보 (DICE 배송 시 비용 별도)
CAS 번호:
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)
biological 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.
저장 등급
10 - Combustible liquids
wgk
WGK 3
flash_point_f
Not applicable
flash_point_c
Not applicable
ppe
Eyeshields, Gloves
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
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.
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
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
문서
Instructions for working with enzymes supplied as ammonium sulfate suspensions
관련 콘텐츠
Product Information Sheet
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