Modifying Enzymes
New England Biolabs, Inc. Endo F3 – 240 units
Endo F3 is an endoglycosidase that cleaves within the chitobiose core of N-linked fucosylated-biantennary and triantennary complex oligosaccharides from glycoproteins. Endo F3 is tagged with chitin binding domain (CBD) for easy removal from a reaction.
AG Scientific Inc Proteinase K, 500 MG
Proteinase K is a highly reactive serine protease that displays an ability to digest native proteins, thereby inactivating enzymes such as DNase and RNase without recourse to a denaturation process. It is the most powerful proteinase among all proteinases characterized so far. It cleaves at the peptide bond adjacent to the carboxylic acid group of aliphatic, aromatic or hydrophobic amino acids. Recombinant Proteinase K is used in the isolation or preparation of high molecular weight nucleic acids. It is highly pure and has a higher specific activity and is more stable at room temperature when compared to native Proteinase K.CAS Number: 39450-01-06Molecular Weight: 29.3 kDaSolubility: 50mM Tris-HCl (pH 7.5), 3mM CaCl2, 50% GlycerolStorage Temperature: +4CResearch or further manufacturing use only, not for food or drug use.
New England Biolabs, Inc. mRNA Decapping Enzyme – 2000 units
mRNA Decapping Enzyme catalyzes the removal of 7-methylguanosine cap (m7G) from 5 end of mRNA, producing 5 monophosphate and releasing m7GDP. mRNA Decapping Enzyme is capable of decapping mRNAs of various lengths and removes both Cap0 and Cap1 structures with similar efficiency. mRNA Decapping Enzyme also converts 5 triphosphate ends to 5 monophosphate, albeit with reduced efficiency. 5' monophosphorylated RNA can be exploited in a variety of downstream applications, including 5' RNA Ligase-mediated RACE, RNA-seq, and 5' -> 3' exonuclease digestion.
New England Biolabs, Inc. Nuclease P1 – 10000 units
Nuclease P1 (from P. citrinum) is a zinc-dependent single-strand specific nuclease which hydrolyzes 3->5 phosphodiester bonds in RNA and ssDNA with no base specificity. Nuclease P1 also exhibits 3-phosphomonoesterase activity. Although a single-strand specific nuclease (ssDNA and RNA-specific), Nuclease P1 does display some activity toward dsDNA in Nuclease P1 Reaction Buffer. If preferentially degrading single-stranded nucleic acids (ssDNA or RNA) in the presence of double stranded DNA (dsDNA), we recommend using Nuclease P1 in 1X NEBuffer r1.1 to limit activity on dsDNA while maintaining single-strand nuclease activity.
New England Biolabs, Inc. beta-Agarase I – 100 units
B-Agarase I digests agarose, releasing trapped DNA and producing carbohydrate molecules which can no longer gel, purifying DNA fragments from gels.
New England Biolabs, Inc. PNGase F (Glycerol-free) – 15000 units
PNGase F is the most effective enzymatic method for removing almost all N-linked oligosaccharides from glycoproteins. PNGase F (Glycerol-free) is an amidase, which cleaves between the innermost GlcNAc and asparagine residues of high mannose, hybrid, and complex oligosaccharides.
- Glycerol-free for optimal performance in HPLC and mass spectrometry analysis
- >= 95% purity, as determined by SDS-PAGE and intact ESI-MS
- Non-recombinant with no detectable endoglycosidase F1, F2 or F3 contamination
- Optimal activity and stability for up to 24 months
- Can be used under native or denaturing conditions
New England Biolabs, Inc. E.coli DNA Ligase – 1000 units
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.
New England Biolabs, Inc. Pyrophosphatase, inorganic (yeast) – 50 units
Inorganic pyrophosphatase (PPase) catalyzes the hydrolysis of inorganic pyrophosphate to form orthophosphate. A variety of metabolic reactions generate inorganic pyrophosphate as a reaction byproduct. Such reactions are rendered irreversible when the pyrophosphate is degraded by pyrophosphatase. RNA and DNA synthesis are examples of reactions that can be pulled far in the synthesis direction by the action of inorganic pyrophosphatase.
New England Biolabs, Inc. α1-2,3 Mannosidase - 640 units
1-2,3 Mannosidase is a highly specific exoglycosidase that catalyzes the hydrolysis of 1-2 and 1-3 linked mannose residues from oligosaccharides
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. Bacteroides Heparinase I – 240 units
Bacteroides Heparinase I, also called Heparin Lyase I, is active on heparin and the highly sulfated domains of heparan sulfate. The reaction yields oligosaccharide products containing unsaturated uronic acids which can be detected by UV spectroscopy at 232 nm.
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.
Research Products International Corp Proteinase K, 100 Milligrams
From Tritirachium album. Serine protease for proteolytic inactivation of nucleases during isolation of DNA and RNA.
Description
Proteinase K is a highly reactive serine protease that displays an ability to digest native proteins, thereby inactivating enzymes such as DNase and RNase without recourse to a denaturation process. It is the most powerful proteinase among all proteinases characterized so far. It cleaves at the peptide bond adjacent to the carboxylic acid group of aliphatic, aromatic or hydrophobic amino acids.
Recombinant Proteinase K is used in the isolation or preparation of high molecular weight nucleic acids. It is highly pure and has a higher specific activity and is more stable at room temperature when compared to native Proteinase K.
Bioworld Cellulase (Onozuka R-10), 5 g
Cellulase (Onozuka R-10) From Trichadema Viride. Enzyme mixture often used in combination with Macerozyme R-10 (M22010) for isolation of plant protoplasts. One unit of Cellulase will liberate 1.0 µmole of glucose from carboxymethyl cellulose.Optimum pH range: 4-5.Soluble in water (10mg/ml)Contents:Cellulase: 1.0 U/mg Pectinase: 0.4 U/mg Hemicellulase: 1.0 U/mg alpha-Amylase: 0.6 U/mg Protease: 0.01 U/mg
New England Biolabs, Inc. Quick Ligation™ Kit – 150 reactions
The Quick Ligation Kit enables ligation of cohesive end or blunt end DNA fragments in 5 minutes at room temperature. (25C)