R8761
Nco I from Nocardia corallina
Restriction Enzyme
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About This Item
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Molecular Biology
form
buffered aqueous glycerol solution
concentration
10,000 units/mL
shipped in
wet ice
storage temp.
−20°C
Application
NcoI is a DNA restriction endonuclease that is used in molecular biology applications to cleave the DNA recognition site 5′-C/CATGG-3′, resulting in DNA fragments with 5′-cohesive termini.
Biochem/physiol Actions
Recognition sequence: 5′-C/CATGG-3′
Cutting results: a 2-10-fold Nco I overdigestion of 1 μg λ DNA substrate results in 100% cutting
Heat inactivation: Inactivated at 65 °C for 15 minutes.
Cutting results: a 2-10-fold Nco I overdigestion of 1 μg λ DNA substrate results in 100% cutting
Heat inactivation: Inactivated at 65 °C for 15 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), 0.2%Triton X-100 (v/v) at 4 °C
Other Notes
Supplied with 10x Restriction Enzyme Buffer SH (B3657).
Storage Class
12 - Non Combustible Liquids
wgk
WGK 2
flash_point_f
Not applicable
flash_point_c
Not applicable
Regulatory Information
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Jonathan V Reddy et al.
Molecular biology of the cell, 17(10), 4353-4363 (2006-08-04)
Mannose 6-phosphate receptors (MPRs) deliver newly synthesized lysosomal enzymes to endosomes and then recycle to the Golgi. MPR recycling requires Rab9 GTPase; Rab9 recruits the cytosolic adaptor TIP47 and enhances its ability to bind to MPR cytoplasmic domains during transport
E M Van Cott et al.
Gene, 74(1), 55-59 (1988-12-25)
Methyltransferase genes from the FnuDI, NaeI, NcoI, and XbaI restriction-modification systems have been isolated in Escherichia coli by 'shot-gun' cloning bacterial DNA fragments into plasmid vectors and selecting for protectively modified molecules that resist digestion by the corresponding restriction endonuclease.
Retargeting of human T cells to tumor-associated MUC1: the evolution of a chimeric antigen receptor.
Scott Wilkie et al.
Journal of immunology (Baltimore, Md. : 1950), 180(7), 4901-4909 (2008-03-21)
MUC1 is a highly attractive immunotherapeutic target owing to increased expression, altered glycosylation, and loss of polarity in >80% of human cancers. To exploit this, we have constructed a panel of chimeric Ag receptors (CAR) that bind selectively to tumor-associated