Wyświetlanie 1–12 z 44 wyników

5′ Deadenylase (RK20580)

The 5′ Deadenylase derived from yeast can remove adenosine residues from the 5′-end of DNA and RNA, retaining the 5′-end phosphate group. It can cleave AppppA to produce ATP and AMP.

5’App-T4 DNA Ligase (RK20510)

5’App-T4 DNA Ligase is a mutant of T4 DNA Ligase without adenylation function, which can specifically ligates the pre-adenylated 5´ end of DNA or RNA to the 3´ end of DNA. This enzyme does not require ATP as a cofactor for ligation, but requires a pre-adenylated substrate. This enzyme reduces background ligation (chimera formation) during NGS library construction, because it can only use 5 ‘preadenylation adapter to the DNA fragments.

Circle Ligase (RK20508)

Circle Ligase is a thermostable ATP-dependent ligase that can catalyze the self-circularization of single-stranded DNA (ssDNA)/single-stranded RNA (ssRNA) strands simultaneously possessing a 5′-phosphate group and a 3′-hydroxyl group in the absence of complementary sequences, with the length of single-stranded DNA (ssDNA)/single-stranded RNA (ssRNA) being greater than 15bp.

DNA Polymerase I (E. coli) (RK20530)

DNA Polymerase I (E coli) is a DNA-dependent DNA polymerase with inherent 3´→ 5´ and 5´→ 3´ exonuclease activities. The 5´→ 3´ exonuclease activity removes nucleotides ahead of the growing DNA chain, allowing nick-translation.
It is applicable to nick translation of DNA for obtaining probes with a high specific activity and for second strand synthesis of cDNA.

DNA Polymerase I, Large (Klenow) Fragment (RK20525)

DNA Polymerase I, Large (Klenow) Fragment (about 68 kD) is a proteolytic product of E. coli DNA Polymerase I which retains polymerization and 3’→5′ exonuclease activity, but has lost 5’→3′ exonuclease activity. Klenow retains the polymerization fidelity of the holoenzyme without degrading 5′ termini.
It is applicable to DNA sequencing by the Sanger dideoxy method, fill-in of 5′ overhangs to form blunt ends, removal of 3′ overhangs to form blunt ends, second strand cDNA synthesis and second strand synthesis in mutagenesis protocols.

DNase I , RNase-free (5,000 U/mL) (RK20549)

DNase I (deoxyribonuclease, RNase-free ) is an endonuclease that nonspecifically cleaves DNA to release di-, tri-, and oligonucleotide products with 5’phosphorylated and 3´-hydroxylated ends. The activity of DNase I depends on Ca2+ and also be activated bydivalent metal ions Mg2+, Mn2+, etc.DNase I act on various DNAs such as single and double-stranded DNA, RNA:DNA hybrids.

DNase I (Powder) (RM29865)

Deoxyribonuclease I (DNase I) is an endonuclease that nonspecifically cleaves DNA to release di-, tri-, and oligonucleotide products with 5’phosphorylated and 3´-hydroxylated ends. This product is sourced from bovine pancreas and is supplied in powder form with enzyme activity ≥ 500 Kunitz units/mg protein.

E. coli Poly(A) Polymerase (RK20591)

Poly(A) polymerase catalyzes the addition of AMP, converted from ATP, to the 3′ end of RNA in a template-independent manner.

E.coli DNA Ligase (RK20501)

E. coli DNA Ligase catalyzes the formation of a phosphodiester bond between the 5′-phosphate and the 3′-hydroxyl of two adjacent DNA strands in duplex DNA with cohesive ends. It is not appreciably active on blunt-ended substrates. E. coli DNA Ligase uses NAD as a cofactor and can be heat-inactivated. E. coli DNA Ligase is active at a range of temperatures (4°C – 37°C).

Endonuclease III (Nth) (RK20569)

Endonuclease III (Nth) protein acts as both N-glycosylase and a AP-lyase.The N-glycosylase activity releases damaged pyrimidines from double-stranded DNA, generating a basic (AP site). The AP-lyase activity of the enzyme cleaves 3´ to the AP site leaving a 5´ phosphate and a 3´ ring opened sugar.

Endonuclease IV (RK20522)

Endonuclease IV derived from E. coli recognizes the depurine/depyrimidine (AP) site on the double- stranded DNA molecule, and cleaves the first phosphodiester bond at the 5′ ́end of the AP site to form 3′-OH and 5’dRP . In addition, Endonuclease IV has 3’́diesterase activity, which releases phosphoglyceraldehyde, intact deoxyribose 5′ -phosphate, and phosphoric acid from the 3′ ́end of DNA. The best substrate for this enzyme is AP double-stranded DNA, but it is also active against AP single-stranded DNA.

Endonuclease VIII (RK20534)

Endonuclease VIII originates from E.coli and possesses both N-glycosylase and AP-endonuclease activity. The N-glycosylase activity releases damaged pyrimidines from double-stranded DNA, generating an apurinic (AP site). The AP-endonuclease the phosphodiester bond at the AP site, forming 3’-P and 5’-P ends.
Damaged bases recognized and removed by Endonuclease VIII include: urea, 5, 6-dihydroxythymine, thymine glycol, 5-hydroxy-5-methylhyd antoin, uracil glycol, 6-hydroxy-5, 6-dihydrothymine and methylhydroxy- methyluracil.