T4 DNA Ligase

Product Code: ME430x
Price: £27.00

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Description
T4 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 With
10X 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 Control
All 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

Download
Manual

T4 DNA Ligase

Publication
This Product Has Been Used In:

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.248-255

Mohandesi, 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. pp14-22

Busayapongchai, 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

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