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.

Exonuclease I (E. coli) (RK20531)

Exonuclease I catalyzes the removal of nucleotides from single-stranded DNA in the 3′ to 5′ direction, and does not degrade DNA strands with the 3′-OH end blocked by phosphoryl or acetyl groups. Exonuclease I has strict substrate specificity and is incapable of degrading double-stranded DNA and RNA.

Exonuclease III (E. coli) (RK20533)

Exonuclease III (E.coli) catalyzes the stepwise removal of mononucleotides from 3´-hydroxyl termini of duplex DNA. The preferred substrates are dsDNA with blunt or recessed 3´-, termini although the enzyme also acts at nicks in dsDNA to produce single-strand gaps. dsDNA with 3´-overhang are resistant to cleavage; when overhang’s length is ≥ 4 bases,dsDNA are able to fully prevent ExoIII cleavage process.
Exonuclease III has also been reported to have RNase H, 3´-phosphatase and AP-endonuclease activities.

Lambda Exonuclease (RK20529)

Lambda Exonuclease digests linear or nicked dsDNA in the 5′ to 3′ ́direction. It exhibits the highest cleavage activity towards 5′-phosphorylated dsDNA, showing low enzymatic activity toward ssDNA and non-phosphorylated DNA. It remains inactive at DNA nicks but shows limited activity at gaps.

RecJf (RK20576)

RecJf is a DNA exonuclease that specifically catalyzes the degradation of ssDNA in the 5′ to 3′ direction.

T5 Exonuclease (RK20575)

T5 Exonuclease is a double-stranded DNA-specific exonuclease and single-stranded DNA endonuclease that degrades DNA in the 5′ ́to 3′ ́direction. T5 Exonuclease can digest nucleotides starting from the 5′ end or at gaps and nicks in linear or circular dsDNA. The enzyme does not digest supercoiled dsDNA and exhibits endonuclease activity on ssDNA

T7 Endonuclease I (RK20554)

T7 Endonuclease I (T7 Endo I, T7EI),can recognize and cleave non-perfectly mismatched DNA, cruciform DNA structures, holliday structures or junctions and Heteroduplex DNA. The cleavage site is at the first, second or third phosphodiester bond that is 5´ end to the mismatch.

T7 Exonuclease (RK20574)

T7 Exonuclease is a double-stranded DNA-specific exonuclease that degrades linear or nicked double-stranded DNA in the 5′to 3′direction. The enzyme does not digest supercoiled dsDNA.