5000U

ABScript Full Length Reverse Transcriptase for Single Cell

Antarctic Phosphatase (AnP) is a heat-labile alkaline phosphatase purified from a recombinant source. AnP nonspecifically catalyzes the dephosphorylation of 5’and 3’ends of DNA and RNA phosphomonoesters. Also, AnP Hydrolyses ribo-, as well as deoxyribonucleoside triphosphates (NTPs and dNTPs). AnP is completely and irreversibly inactivated by heating at 80°C for 2 minutes, thereby making removal of AnP prior to ligation or end-labeling unnecessary.

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, 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 （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.

5’…GmA/TC…3′
3’…CT/mAG…5′
Isoschizomers: MalI

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 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 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.

HS Taq DNA Polymerase (50,000 U/mL)

HS Taq DNA Polymerase, Glycerol-free (50,000 U/mL)

Klenow Fragment (3’→ 5′ exo^–) is an N-terminal truncation of DNA Polymerase I which retains polymerase activity, but has lost the 5’→ 3′ exonuclease activity and has mutations (D355A, E357A) which abolish the 3’→ 5′ exonuclease activity. Klenow Fragment (3’→ 5′ exo^–) is isolated from a recombinant source. It generates probes using random primers and shows moderate strand displacement activity. It can be used in random primer labeling, DNA sequencing by the Sanger dideoxy method, second strand cDNA synthesis and second strand synthesis in mutagenesis protocols.

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.

5’…A/CGCGT…3′
3’…TGCGC/A…5′

5’…C/CGG…3′
3’…GGC/C…5′
Isoschizomers: HpaII、HapII、BsiSI

5’…C/CATGG…3′
3’…GGTAC/C…5′
Isoschizomers: Bsp19I

5’…G/CTAGC…3′
3’…CGATC/G…5′
Isoschizomers: AsuNHI

5’…GCTCTTCN…3′
3’…CGAGAAGN…5′

5’…CR/CCGGYG…3′
3’…GYGGCC/RC…5′

T4 RNA ligase 1 catalyzes the formation of a 3´ → 5´ phosphodiester bond by joining the 5´ phosphate end of a nucleotide to the 3´ hydroxyl end, accompanied by the hydrolysis of ATP to AMP and PPi. Substrates include single-stranded RNA, DNA, and dinucleoside pyrophosphates.

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 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.

T7 RNA Polymerase is a DNA-dependent 5’→3′ RNA polymerase that highly specifically recognizes the T7 promoter sequence. T7 RNA Polymerase uses double-stranded DNA containing the T7 promoter sequence as a template and NTP as a substrate to synthesize RNA complementary to the single-stranded DNA downstream of the T7 promoter.

Taq DNA Polymerase is a thermostable DNA polymerase that possesses a 5´→ 3´ polymerase activity and a 5´ flap endonuclease activity. Taq DNA Polymerase was isolated from a recombinant source and offers robust and reliable reactions. It tolerates a wide range of templates and incorporates dUTP, dITP, and fluorescently-labeled nucleotides.

E.coli Uracil-DNA Glycosylase (UDG) catalyses the release of free uracil from uracil-containing DNA. UDG efficiently hydrolyzes uracil from single-stranded or double-stranded DNA, but not from oligomers (6 or fewer bases).
It releases uracil from ss- or ds-DNA and is applicable to eliminates PCR carry-over contamination.

5’…C/TCGAG…3′
3’…GAGCT/C…5′
Isoschizomers: PaeR7I、Sfr274I、SlaI