R5884
Nsi I from Neisseria sicca
Restriction Enzyme
grade
Molecular Biology
form
buffered aqueous glycerol solution
concentration
10,000 units/mL
shipped in
wet ice
storage temp.
−20°C
Application
NsiI is a restriction endonuclease used in molecular biology to cleave DNA at the recognition site 5′-ATGCA/T-3′, generating DNA fragments with 3′-cohesive ends.
Biochem/physiol Actions
Recognition sequence: 5′-ATGCA/T-3′
Heat inactivation: Inactivated at 65 °C for 20 minutes.
Heat inactivation: Inactivated at 65 °C for 20 minutes.
Physical form
Solution in 20 mM Tris-HCl, pH 8.0, 0.1 mM EDTA, 100 mM NaCl, 10 mM 2-mercaptoethanol, 50 % glycerol (v/v), 0.02% polydocanol (v/v), 0.01% gelatine (v/v), at 4 °C
Other Notes
Isoschizomer: Ava III
Supplied with 10x Restriction Enzyme Buffer SH (B3657).
Storage Class Code
12 - Non Combustible Liquids
WGK
WGK 1
Flash Point(F)
Not applicable
Flash Point(C)
Not applicable
Regulatory Information
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Daniel Wegmüller et al.
Stem cells (Dayton, Ohio), 25(5), 1178-1185 (2007-01-16)
Although differentiation of pluripotent embryonic stem cells is restricted by a hierarchy of transcription factors, little is known about whether post-transcriptional mechanisms similarly regulate early embryoid differentiation. We developed a system where small hairpin (sh)RNAs can be induced in embryonic
Cloned NsiI restriction-modification system.
Longo, M.C., and Smith, M.D.
Biotechnology Advances, 15, 83-83 (1997)
T H Ch'ng et al.
Journal of virology, 79(14), 8835-8846 (2005-07-05)
Pseudorabies virus (PRV) glycoprotein E (gE) is a type I viral membrane protein that facilitates the anterograde spread of viral infection from the peripheral nervous system to the brain. In animal models, a gE-null mutant infection spreads inefficiently from presynaptic
C Kessler et al.
Gene, 92(1-2), 1-248 (1990-08-16)
The properties and sources of all known class-I, class-II and class-III restriction endonucleases (ENases) and DNA modification methyltransferases (MTases) are listed and newly subclassified according to their sequence specificity. In addition, the enzymes are distinguished in a novel manner according
Nico Mitro et al.
Methods in molecular biology (Clifton, N.J.), 952, 137-144 (2012-10-27)
The role of certain amino acids in the interactions of ligands with their cognate nuclear receptors is usually achieved by the resolution of the crystal structure of the receptor complexed with the ligand. As a complementary functional approach, site-directed mutagenesis
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