Modifying Enzymes
Research Products International Corp Proteinase K, 500 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.
New England Biolabs, Inc. Cre Recombinase – 250 units
Cre Recombinase is a Type I topoisomerase from bacteriophage P1 that catalyzes the site-specific recombination of DNA between loxP sites. The enzyme requires no energy cofactors and Cre-mediated recombination quickly reaches equilibrium between substrate and reaction products. The loxP recognition element is a 34 base pair (bp) sequence comprised of two 13 bp inverted repeats flanking an 8 bp spacer region which confers directionality. Recombination products depend on the location and relative orientation of the loxP sites. Two DNA species containing single loxP sites will be fused. DNA between directly repeated loxP sites will be excised in circular form while DNA between opposing loxP sites will be inverted with respect to external sequences.
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. Endonuclease VIII – 1000 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.
New England Biolabs, Inc. Exonuclease T – 1250 units
Exonuclease T (Exo T), also known as RNase T, is a single-stranded RNA or DNA specific nuclease that requires a free 3' terminus and removes nucleotides in the 3' to 5' direction. Exonuclease T can be used to generate blunt ends from RNA or DNA molecules that have 3 extensions.
Cayman Chemical Octnoyl-Coenzyme AsodIum s 1mg
A medium-chain acyl CoA; levels increased in liver in patients with Reye’s syndrome and β-oxidation of octanoyl-CoA by MCADH is decreased in patients with MCD; inhibits citrate synthase and glutamate dehydrogenase
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.
Sino Biological SuperNuclease
SuperNuclease is a recombined Serratia marcescens’ extracellular endonuclease. The sequence is same with Benzonase (Benzonase is a trademark of Merck KGaA, Darmstadt, Germany).
American Research Products Inc AMERICAN RESEARCH PRODUCTS INC
5000615743 TOPOISOMERASE III ELISA KIT
Selleck Chemical LLC Dyngo-4a 10mg 1256493-34-1
Dyngo-4a is a potent dynamin inhibitor with IC50 of 0.38 ?M, 1.1??M, and 2.3 ?M for DynI (brain), DynI (rec), and DynII (rec), respectively. *For Research & Development use only. Product is not intended for drug, household, or human consumption.
Discovery Life Sciences HUM CYP2B6+REDUCTASE+B5 0.5NMO
Human CYP2B6 + P450 Reductase + Cytochromebeta5 SUPERSOMES 0.5 nmole cytochrome P450 in 0.5mL 7-Ethoxy-4-trifluoromethylcoumarin deethylase activity has replaced 7-ethoxycoumarin deethylase activity for this enzyme
Enzo Life Sciences p300 (catalytic domain) (human), (recombinant) (100 µg)
Synonyms: E1A binding protein p300, Histone acetyltransferase p300. MW: 45.1 kDa. UniProt ID: Q09472. Source: Produced in E. coli. Catalytic domain (aa 1284-1673) of human p300. Purification: Partially purified by single-step affinity chromatography and gel filtration. Formulation: Liquid. In 50mM TRIS/HCl, pH 8.0, containing 0.1mM EDTA, 10% glycerol.