N5661

Sigma-Aldrich

Nuclease S1 from Aspergillus oryzae

for single-strand DNA/RNA digestion

Synonym(s):
Endonuclease S1
CAS Number:
Enzyme Commission number:
MDL number:
NACRES:
NA.54

Quality Level

form

solution

concentration

≥100000 units/mL

shipped in

wet ice

storage temp.

−20°C

Looking for similar products? Visit Product Comparison Guide

General description

The Nuclease S1 enzyme from Aspergillus oryzae has the ability to degrade single-stranded oligonucleotides composed of either deoxynucleotides or ribonucleotides.

Application

Nuclease S1 from Aspergillus oryzae has been used in a study to assess a biochemical method for mapping mutational alterations in DNA. It has also been used in a study to investigate the DNA damage and repair in a γ-irradiated rat brain tumor.

Biochem/physiol Actions

SI nuclease from Aspergillus oryzae can generate double-stranded DNA breaks in response to DNA nicks or abasic sites.
Nuclease S1 isolated from Aspergillus oryzae exhibits endo- and exolytic hydrolytic activity for the phosphodiester bonds of single-stranded DNA and RNA yielding 5′-phosphomononucleotide and 5′-phosphooligonucleotide end-products. It is used to digest non-annealed polynucleotide tails and hairpin loops in RNA and DNA duplexes and can be used to convert superhelical DNA to the linear form.

Unit Definition

One unit will cause 1.0 microgram of single-stranded nucleic acid to become perchloric acid soluble per minute at pH 4.6 at 37°C.

Physical form

Solution containing 30 mM sodium acetate, 50 mM NaCl, 1 mM ZnCl2, 50% glycerol, 2 mg/ml protein

Kit Components Only

Product No.
Description

  • 30mM Sodium acetate .25-.25 %

  • 50mM Sodium chloride .29 %

  • 1mM Zinc chloride .01 %

  • Glycerol 50 %

  • 2mg/mL Protein .2 %

RIDADR

NONH for all modes of transport

WGK Germany

WGK 2

Flash Point(F)

Not applicable

Flash Point(C)

Not applicable

M A Chaudhry et al.
Nucleic acids research, 23(19), 3805-3809 (1995-10-11)
Defined DNA substrates containing discrete abasic sites or paired abasic sites set 1, 3, 5 and 7 bases apart on opposite strands were constructed to examine the reactivity of S1, mung bean and P1 nucleases towards abasic sites. None of...
P Beard et al.
Journal of virology, 12(6), 1303-1313 (1973-12-01)
S(1) nuclease, the single-strand specific nuclease from Aspergillus oryzae can cleave both strands of circular covalently closed, superhelical simian virus 40 (SV40) DNA to generate unit length linear duplex molecules with intact single strands. But circular, covalently closed, nonsuperhelical DNA...
F Harada et al.
Nucleic acids research, 2(6), 865-871 (1975-06-01)
Nuclease S1 specifically hydrolizes tRNAs in their anticodon loops, forming new 5' phosphate and 3' OH ends. Some single-stranded regions are not cut by nuclease S1. The strong preference of nuclease S1 for the anticodon region can be used for...
Larissa A Balabanova et al.
Marine biotechnology (New York, N.Y.), 14(1), 87-95 (2011-06-08)
An extracellular nuclease was purified 165-fold with a specific activity of 41,250 U/mg poly(U) by chromatography with modified chitosan from the culture of marine fungus Penicillium melinii isolated from colonial ascidium collected near Shikotan Island, Sea of Okhotsk, at a...
Nicole M Nichols
Current protocols in molecular biology, Chapter 3, Unit3-Unit3 (2011-01-13)
Reaction conditions for a variety of endonucleases are detailed in this unit along with discussions of potential applications. Enzymes covered include BAL 31 nuclease, S1 nuclease, mung bean nuclease, micrococcal nuclease, and DNase I. A general discussion regarding the use...
Protocols
Enzymatic Assay of Nuclease S1
Read More

Our team of scientists has experience in all areas of research including Life Science, Material Science, Chemical Synthesis, Chromatography, Analytical and many others.

Contact Technical Service

Social Media

LinkedIn icon
Twitter icon
Facebook Icon
Instagram Icon

MilliporeSigma

Research. Development. Production.

We are a leading supplier to the global Life Science industry with solutions and services for research, biotechnology development and production, and pharmaceutical drug therapy development and production.

© 2021 Merck KGaA, Darmstadt, Germany and/or its affiliates. All Rights Reserved.

Reproduction of any materials from the site is strictly forbidden without permission.