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N5661

Sigma-Aldrich

Nuclease S1 from Aspergillus oryzae

for single-strand DNA/RNA digestion

Synonyme(s) :

Endonuclease S1

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About This Item

Numéro CAS:
37288-25-8
Numéro de classification (Commission des enzymes):
3.1.30.1 (BRENDA, IUBMB)
Numéro MDL:
MFCD00131010
Code UNSPSC :
12352204
Nomenclature NACRES :
NA.54

Source biologique

Aspergillus sp. (A. oryzae)

Forme

solution

Concentration

≥100000 units/mL

Technique(s)

DNA purification: suitable

Adéquation

suitable for nucleic acid purification

Application(s)

cell analysis

Conditions d'expédition

wet ice

Température de stockage

−20°C

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Catégories apparentées

Description générale

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.

Actions biochimiques/physiologiques

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.
SI nuclease from Aspergillus oryzae can generate double-stranded DNA breaks in response to DNA nicks or abasic sites.

Définition de l'unité

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.

Forme physique

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

Composants de kit seuls

Réf. du produit
Description
  • 30mM Sodium acetate .25-.25 %
  • 50mM Sodium chloride .29 %
  • 1mM Zinc chloride .01 %
  • Glycerol 50 %
  • 2mg/mL Protein .2 %

Code de la classe de stockage

10 - Combustible liquids

Classe de danger pour l'eau (WGK)

WGK 2

Point d'éclair (°F)

Not applicable

Point d'éclair (°C)

Not applicable

Certificats d'analyse (COA)

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Consulter la Bibliothèque de documents

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
Robert Busch et al.
Nature protocols, 2(12), 3045-3057 (2007-12-15)
DNA replication occurs almost exclusively during S-phase of the cell cycle and represents a simple biochemical metric of cell division. Previous methods for measuring cell proliferation rates have important limitations. Here, we describe experimental protocols for measuring cell proliferation and
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
Rebecca Rodell et al.
Methods in molecular biology (Clifton, N.J.), 2444, 125-140 (2022-03-16)
Physiological and chemically induced modifications to nucleosides are common in both DNA and RNA. Physiological forms of these modifications play critical roles in gene expression, yet aberrant marks, if left unrepaired, may be associated with increased genome instability. Due to
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
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Protocoles

Nuclease S1 Enzymatic Assay

Spectrophotometric assay at 260 nm measures nuclease S1 activity, vital for nucleic acid research, with defined enzyme unit criteria.

Notre équipe de scientifiques dispose d'une expérience dans tous les secteurs de la recherche, notamment en sciences de la vie, science des matériaux, synthèse chimique, chromatographie, analyse et dans de nombreux autres domaines..

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