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N5386

Sigma-Aldrich

Nuclease micrococcal from Staphylococcus aureus

100-300 units/mg protein

Synonym(s):

Endonuclease micrococcal, MNase, Micrococcal endonuclease

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About This Item

CAS Number:
9013-53-0
Enzyme Commission number:
3.1.31.1 (BRENDA, IUBMB)
EC Number:
232-748-0
MDL number:
MFCD00131731
UNSPSC Code:
12352204
NACRES:
NA.54

biological source

Staphylococcus aureus

Quality Level

200

form

powder

specific activity

100-300 units/mg protein

composition

Protein, ≥40% E1%/280 (Balance primarily sodium acetate)

technique(s)

DNA extraction: suitable
DNA purification: suitable

suitability

suitable for molecular biology

application(s)

cell analysis

storage temp.

−20°C

Gene Information

Staphylococcus aureus subsp. aureus Mu50 ... nuc(1120790)

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Application

Micrococcal Nuclease can be used for the digestion of chromatin to identify the location of nucleosomes.
Nuclease micrococcal from Staphylococcus aureus has been used in a study to monitor hybridization reactions with DNA. It has also been used in a study to investigate the optimal conditions for assay of staphylococcal nuclease.

Biochem/physiol Actions

Hydrolyzes 5′-phosphodiester bonds of DNA.

Other Notes

Note: One μmolar unit = approx. 85 A260 units, where an A260 unit is equivalent to a ΔA260 of 1.0 in 30 min at pH 8.8 at 37 °C in a 3.55 mL reaction volume. Light path = 1 cm.

Storage Class Code

11 - Combustible Solids

WGK

WGK 3

Flash Point(F)

Not applicable

Flash Point(C)

Not applicable

Personal Protective Equipment

dust mask type N95 (US), Eyeshields, Gloves

Certificates of Analysis (COA)

Search for Certificates of Analysis (COA) by entering the products Lot/Batch Number. Lot and Batch Numbers can be found on a product’s label following the words ‘Lot’ or ‘Batch’.

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Use of micrococcal nuclease to monitor hybridization reactions with DNA.
D L Kacian et al.
Analytical biochemistry, 58(2), 534-540 (1974-04-01)
Optimal conditions for assay of staphylococcal nuclease
KAMMAN, J. and S. TATINI
Journal of Food Science, 42, 421-424 (1977)
Julien Roche et al.
Biochemistry, 51(47), 9535-9546 (2012-11-03)
The folding of staphylococcal nuclease (SNase) is known to proceed via a major intermediate in which the central OB subdomain is folded and the C-terminal helical subdomain is disordered. To identify the structural and energetic determinants of this folding free
Gang Wei et al.
Methods in enzymology, 513, 297-313 (2012-08-30)
Gene transcription can be regulated through alteration of chromatin structure, such as changes in nucleosome positioning and histone-modification patterns. Recent development of techniques based on the next-generation sequencing technology has allowed high-resolution analysis of genome-wide distribution of these chromatin features.
Julien Roche et al.
Journal of the American Chemical Society, 135(39), 14610-14618 (2013-08-31)
The time required to fold proteins usually increases significantly under conditions of high pressure. Taking advantage of this general property of proteins, we combined P-jump experiments with NMR spectroscopy to examine in detail the folding reaction of staphylococcal nuclease (SNase)
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