DescriptionT4 DNA Ligase catalyzes the formation of a phosphodiester bond between juxtaposed 5"-phosphate and 3"-hydroxyl termini in duplex DNA or RNA. This enzyme will join blunt-end and cohesive end termini as well as repair single stranded nicks in duplex DNA, RNA, or DNA-RNA hybrids.
Concentrations 50 - 200u/μl
Features
- Ultrapure recombinant protein
- Seals single-stranded nicks in duplex DNA, RNA or DNA-RNA hybrids.
- ATP is an essential cofactor for the reaction.
Supplied With10X Buffer T4 Ligase 50mM Tris-HCl (pH7.8 at 25˚C), 10mM MgCl2, 10mM DTT, 1mM ATP and 25μg/ml BSA. Store at -20˚C.
Storage Buffer 10mM Tris-HCl (pH7.5), 50mM NaCl, 0.1mM EDTA, 10mM 2-mercaptoethanol and 50% glycerol. Store at -20˚C.
Thermal Inactivation 65˚C for 15 minutes
Unit Definition 1u (*Cohesive End Ligation Unit) is defined as the amount of enzyme that is required to give 50% ligation of Hind III fragments of lambda DNA (5" DNA termini concentration of 0.12μM [300μg/ml]) in 20μl of 1X T4 DNA Ligase Buffer in 30 minutes at 16˚C.*One Cohesive End Ligation Unit is equal to 0.015 Weiss units. Equivalently, one Weiss unit is equal to 67 Cohesive End Ligation Units.
Application
- Catalyzes the linkage of 5" or 3" blunt/cohesive ends of double-stranded DNA by formation of phosphodiester bond.
- Joining of oligonucleotide linkers or adapters to blunt ends.
- Repair nicks formation in duplex nucleic acids.
Quality ControlAll preparations are assayed for contaminating endonuclease, exonuclease and non-specific DNase activities.
Ordering Information
| Catalog No | Description | Pack Size |
|---|---|---|
| ME4303 | T4 DNA Ligase | 4000u |
| ME4304 | T4 DNA Ligase | 20000u |
DownloadManual
T4 DNA Ligase
PublicationThis Product Has Been Used In:Mahboudi et al. (2018)Prospect and Competence of Quantitative Methods via Real-time PCR in a Comparative Manner: An Experimental Review of Current Methods, . The Open Bioinformatics Journal,11:1-11. Dehnaiv, E., Fathi-Roudsari,M., Mirzaie, S., Arab., S.S., Siadat, S.O.R., Khajeh, K. (2017)Engineering disulfide bonds in Selenomonas ruminantium B-xylosidase by experimental and computational methods. International Journal of Biological Macromolecules. 95. Pp.248-255Mohandesi, N., Haghbeen, K., Ranaei, O., Arab, S.S., Hassani, S. (2017) Catalytic Efficiency and thermostability improvement of SUC2 invertase through rational site-directed mutagenesis. Enzyme and Microbial Technology.96. pp14-22Busayapongchai, P., Siri, S.(2017). Sensitive detection of estradiol based on ligand binding domain of estrogen receptor and gold nanoparticles. Analytical biochemistry. 518, pp.60-68.Kohnehrouz, B.B., & Nayeri, S. (2016)Design, Cloning and In silico Analysis of Efficient siRNA-inducing Casette for Silencing Wheat γ-gliadins. Jordan Journal of Biological Sciences9(1), p.35-40. Meidaninikkjeh, S., Vaziri,F., Siadat, S.D. (2015) Cloning of conserved regions of nontypeable Haemophilus influenzae hmw1 core binding domain. International Journal of Molecular and Clinical Microbiology.5(1) pp.510-515
