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Merck
CN

N5386

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

Key Documents

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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

Regulatory Information

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Certificates of Analysis (COA)

Lot/Batch Number
0000497066
0000497066
0000488208
0000488208
0000488218

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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.
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)
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.
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