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.

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.

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.

LbCas12a Nuclease (RK20570)

Lb Cas12a Nuclease from Lachnospiraceae bacterium is a site-specific DNA endonuclease guided by a single 40-44 nucleotide guide RNA (crRNA). Targeting requires a crRNA complementary to the target site as well as a 5’ TTTV protospacer adjacent motif (PAM) on the DNA strand opposite the target sequence. Cleavage by LbCas12a Nuclease occurs ~17 bases 3′ of the PAM and leaves overhanging ends.This product also has a trans-cleavage activity, which produces high non-specific ssDNA cleavage activity when the target dsDNA, crRNA, and Cas12a protein form a ternary complex.

RecJf (RK20576)

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

RNase A (10 mg/mL) (RM29870)

Ribonuclease A (RNase A), molecular weight 13.7 kDa, is an endonuclease that specifically acts on the 3′ end of the pyrimidine residue on RNA, cleaving phosphodiester bonds formed with adjacent nucleotides, and the final product of the reaction is pyrimidine 3′ phosphate and an oligonucleotide with pyrimidine 3′ phosphate at the end. RNase A does not work on DNA. This product is DNase and protease free, and it can be used without heat treatment before use.
This product is provided in a solution form at a concentration of 10 mg/mL. The recommended working concentration is 1-100 μg/mL, which varies depending on specific applications.

RNase A (Powder) (RM21314)

Ribonuclease A (RNase A), molecular weight 13.7 kDa, is an endonuclease that specifically acts on the 3′ end of the pyrimidine residue on RNA, cleaving phosphodiester bonds formed with adjacent nucleotides, and the final product of the reaction is pyrimidine 3′ phosphate and an oligonucleotide with pyrimidine 3′ phosphate at the end. RNase A does not work on DNA.This product is sourced from bovine pancreas and is supplied in the form of white lyophilized powder with enzyme activity ≥ 50 Kunitz units/mg protein.
Its recommended working concentration is 1-100 μg/mL, which will vary depending on specific applications.