N8630
Nuclease P1 from Penicillium citrinum
lyophilized powder, ≥200 units/mg protein (E1%/280, 3′-5′-Phosphodiesterase)
Synonym(s):
3′-Phosphohydrolase, Nuclease 5′-Nucleotidehydrolase, Endonuclease P1
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All Photos(2)
About This Item
CAS Number:
MDL number:
UNSPSC Code:
12352204
NACRES:
NA.54
Recommended Products
biological source
Penicillium citrinum
Quality Level
form
lyophilized powder
specific activity
≥200 units/mg protein (E1%/280, 3′-5′-Phosphodiesterase)
secondary activity
≥1,000 units/mg protein 3′-nucleotidase
mol wt
42-50 kDa
packaging
vial of ≥250 units (using RNA substrate)
technique(s)
DNA extraction: suitable
DNA purification: suitable
suitability
suitable for molecular biology
application(s)
cell analysis
storage temp.
2-8°C
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General description
Nuclease P1 is one of the most commonly known single-strand specific nucleases in molecular biology; Nuclease P1 is a single stranded specific endoduclease (of ssDNA or ssRNA). Nuclease P1 can also cleave single-stranded regions in double-stranded nucleic acids.
Nuclease P1 from Penicillium citrinum is a zinc-dependent endonuclease that exhibits increased activity in the presence of low concentrations of urea. Nuclease P1 selective activity has found useful applications in studies on nucleic acid structure.
Nuclease P1 from Penicillium citrinum is a zinc-dependent endonuclease that exhibits increased activity in the presence of low concentrations of urea. Nuclease P1 selective activity has found useful applications in studies on nucleic acid structure.
Application
- Nuclease P1 cleave of single stranded DNA or RNA to 5′ mononucleotides
- Nuclease P1 supports DNA damage and modification research
- Nucleic acids base composition and structural analysis can be done by Nuclease P1
- Nuclease P1 has historically been used for the industrial production of 5′-mononucleotides from yeast RNA.
- Removal of nucleic acids through protein purification can be done by Nuclease P1
- Nuclease P1 is a key reagent for the development of methods for studies involving t-RNA dependent amino acid biosynthesis and t-RNA dependent trans-amidation
- Nuclease P1 from Penicillium citrinum has been used in a study to assess crystal structures using ammonium sulphate or polyethylene glycol 4000 as a precipitating agent.
- Nuclease P1 was used in a study to investigate a method for the direct sequence analysis 20-25 nucleotides from the terinini of 5′ or 3′ end group labeled RNA.
- Nuclease P1 is used to improve the sensitivity of a 32P-labeling method for the detection of DNA adducts.
The enzyme has an optimal temperature of approximately 70 °C, but for a long incubation, a temperature below 60 °C is more suitable. It is stable in the pH range of 5 - 8.
Biochem/physiol Actions
Catalyzes the nonspecific endonucleolytic cleavage of single stranded DNA and RNA to yield nucleoside 5′-phosphates and 5′-phosphooligonucleotides. It does not appreciably degrade double-stranded nucleic acids, especially in the presence of more than 400 mM sodium chloride at pH 6.0.
Features and Benefits
Our highly active Nuclease P1 is tested for its 3′- 5′ - Phosphodiesterase Activity and 3′- Nucleotidase Activity and is the most active Nuclease P1 in the market
Physical properties
A zinc dependent glycoprotein consisting of 270 amino acid residues. Molecular mass: 42-50 kDa.
Unit Definition
3′-5′-Phosphodiesterase: One unit will liberate 1.0 μmole of acid soluble nucleotides from RNA per min at pH 5.3 at 37 °C.
3′-Nucleotidase: One unit will hydrolyze 1.0 μmole of orthophosphate from 3′-AMP per min at pH 7.2 at 37 °C.
3′-Nucleotidase: One unit will hydrolyze 1.0 μmole of orthophosphate from 3′-AMP per min at pH 7.2 at 37 °C.
Signal Word
Danger
Hazard Statements
Precautionary Statements
Hazard Classifications
Resp. Sens. 1
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)
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A Lahm et al.
Journal of molecular biology, 215(2), 207-210 (1990-09-20)
P1 nuclease, a zinc-dependent single-strand specific endonuclease from Penicillium citrinum, has been crystallized in three different space groups using either ammonium sulphate or polyethylene glycol 4000 as the precipitating agent. The crystals diffract to between 3 A and 2.2 A.
Fiona J Flett et al.
Nature communications, 9(1), 24-24 (2018-01-04)
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Gangadhara, K. and P. Gangadhara
Enzyme and Microbial Technology, 43, 7-7 (2008)
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