Modifying Enzymes
New England Biolabs, Inc. PNGase F – 75000 units
PNGase F is the most effective enzymatic method for removing almost all N-linked oligosaccharides from glycoproteins. PNGase F is an amidase, which cleaves between the innermost GlcNAc and asparagine residues of high mannose, hybrid, and complex oligosaccharides.
- Leaves N-glycan core oligosaccharides intact and suitable for further analysis
- Non-recombinant with no detectable endoglycosidase F1, F2 or F3 contamination
- >= 95% purity, as determined by SDS-PAGE and intact ESI-MS
- Stored in 50% glycerol
- Optimal activity and stability for up to 24 months
- Can be used under native or denaturing conditions
New England Biolabs, Inc. PNGase F – 15000 units
PNGase F is the most effective enzymatic method for removing almost all N-linked oligosaccharides from glycoproteins. PNGase F is an amidase, which cleaves between the innermost GlcNAc and asparagine residues of high mannose, hybrid, and complex oligosaccharides.
- Leaves N-glycan core oligosaccharides intact and suitable for further analysis
- Non-recombinant with no detectable endoglycosidase F1, F2 or F3 contamination
- >= 95% purity, as determined by SDS-PAGE and intact ESI-MS
- Stored in 50% glycerol
- Optimal activity and stability for up to 24 months
- Can be used under native or denaturing conditions
New England Biolabs, Inc. Enterokinase, light chain – 2560 units
Enterokinase is a specific protease that cleaves after lysine at its cleavage site Asp-Asp-Asp-Asp-Lys. It will sometimes cleave at other basic residues, depending on the conformation of the protein substrate.
Sigma Aldrich Fine Chemicals Biosciences Alpha-1→(2,3,4)-Fucosidase solution from Xanthomonas sp. | 9037-65-4 | MFCD01632935 | 1vl
Alpha-1→(2,3,4)-Fucosidase solution from Xanthomonas sp. | 9037-65-4 | MFCD01632935 | 1vl
New England Biolabs, Inc. Exonuclease III (E.coli) – 25000 units
Catalyzes the stepwise removal of mononucleotides from 3'-hydroxyl termini of duplex DNA. A limited number of nucleotides are removed during each binding event, resulting in coordinated progressive deletions within the population of DNA molecules. The preferred substrates are blunt or recessed 3'-termini, although the enzyme also acts at nicks in duplex DNA to produce single-strand gaps. 3'-protruding termini are resistant to cleavage; the degree of resistance depends on the length of the extension,with extensions 4 bases or longer being essentially resistant to cleavage. Exonuclease III activity depends partially on helical structure and displays sequence dependence (C>A=T>G). Temperature, salt concentration and the ratio of enzyme to DNA greatly affect enzyme activity, requiring reaction conditions to be tailored to specific applications. Exonuclease III has also been reported to have RNase H, 3'-phosphatase and AP-endonuclease activities.
New England Biolabs, Inc. DNA Polymerase I (E. coli) – 500 units
DNA Polymerase I (E coli) is a DNA-dependent DNA polymerase with inherent 3' to 5' and 5' to 3' exonuclease activities. The 5' to 3' exonuclease activity removes nucleotides ahead of the growing DNA chain, allowing nick-translation.
New England Biolabs, Inc. DNA Polymerase I, Large (Klenow) Fragment – 1000 units
DNA Polymerase I, Large (Klenow) Fragment is a proteolytic product of E. coli DNA Polymerase I which retains polymerization and 3' to 5' exonuclease activity, but has lost 5' to 3' exonuclease activity. Klenow retains the polymerization fidelity of the holoenzyme without degrading 5' termini.
New England Biolabs, Inc. Klenow Fragment (3'-5' exo-) – 1000 units
Klenow Fragment (3' to 5' exo-) is an N-terminal truncation of DNA Polymerase I which retains polymerase activity, but has lost the 5' to 3' exonuclease activity and has mutations (D355A, E357A) which abolish the 3' to 5' exonuclease activity.
New England Biolabs, Inc. RNase If – 5000 units
Ribonuclease If (RNase If) is an RNA endonuclease which will cleave at all RNA dinucleotide bonds leaving a 5'hydroxyl and 2',3' cyclic monophosphate. It has a preference for single-stranded RNA over double-stranded RNA. RNase If is a recombinant protein fusion of RNase I (from E. coli) and maltose-binding protein. It has identical activity to RNase I.
New England Biolabs, Inc. Vent DNA Polymerase – 200 units
Vent DNA Polymerase is a high-fidelity thermophilic DNA polymerase. The fidelity of Vent DNA Polymerase is 5-15-fold higher than that observed for Taq DNA Polymerase. This high fidelity derives in part from an integral 3' to 5' proofreading exonuclease activity in Vent DNA Polymerase. Greater than 90% of the polymerase activity remains following a 1 hour incubation at 95C.
New England Biolabs, Inc. T7 Exonuclease – 1000 units
T7 Exonuclease acts in the 5' to 3' direction, catalyzing the removal of 5' mononucleotides from linear or nicked duplex DNA.
New England Biolabs, Inc. Antarctic Phosphatase – 5000 units
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 useful in many molecular biology applications such as the removal of phosphorylated ends of DNA and RNA for subsequent use in cloning or end-labeling of probes. In cloning, dephosphorylation prevents religation of linearized plasmid DNA. The enzyme acts on 5' protruding, 5' recessed, and blunt ends. AnP may also be used to degrade unincorporated dNTPs in PCR reactions to prepare templates for DNA sequencing or SNP analysis. AnP is completely and irreversibly inactivated by heating at 80C for 2 minutes, thereby making removal of AnP prior to ligation or end-labeling unnecessary.
New England Biolabs, Inc. Antarctic Phosphatase – 1000 units
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 useful in many molecular biology applications such as the removal of phosphorylated ends of DNA and RNA for subsequent use in cloning or end-labeling of probes. In cloning, dephosphorylation prevents religation of linearized plasmid DNA. The enzyme acts on 5' protruding, 5' recessed, and blunt ends. AnP may also be used to degrade unincorporated dNTPs in PCR reactions to prepare templates for DNA sequencing or SNP analysis. AnP is completely and irreversibly inactivated by heating at 80C for 2 minutes, thereby making removal of AnP prior to ligation or end-labeling unnecessary.
New England Biolabs, Inc. RNase H – 250 units
RNase H (Ribonuclease H ) is an endoribonuclease that specifically hydrolyzes the phosphodiester bonds of RNA which is hybridized to DNA. This enzyme does not digest single or double-stranded DNA.
New England Biolabs, Inc. Endonuclease VIII – 5000 units
Endonuclease VIII from E. coli acts as both an N-glycosylase and an AP-lyase. The N-glycosylase activity releases damaged pyrimidines from double-stranded DNA, generating an apurinic (AP site). The AP-lyase activity cleaves 3' and 5' to the AP site leaving a 5' phosphate and a 3' phosphate. Damaged bases recognized and removed by Endonuclease VIII include urea, 5, 6- dihydroxythymine, thymine glycol, 5-hydroxy-5- methylhydantoin, uracil glycol, 6-hydroxy-5, 6-dihydrothymine and methyltartronylurea. While Endonuclease VIII is similar to Endonuclease III, Endonuclease VIII has and lyase activity while Endonuclease III has only lyase activity.