You searched for: RNases
Enzymes accelerate, or catalyze, chemical reactions, and they are known to catalyze more than 5,000 biochemical reaction types. Most enzymes are proteins, although a few are catalytic RNA molecules. Choose specific enzymes for cleaving bonds, removing genomic DNA from RNA preparations, for producing fragments of proteins, or for use in ion exchange chromatography. Enzymes are used in the chemical industry and other industrial applications when extremely specific catalysts are required.
E. coli Exonuclease III
Supplier: New England Biolabs (NEB)
Catalyzes the stepwise removal of mononucleotides from 3´-hydroxyl termini of duplex DNA.
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Proteinase K
Supplier: G-Biosciences
Proteinase K (also protease K, endopeptidase K, peptidase K or Tritirachium alkaline phosphatase) (EC 3.4.21.64) is a non-specifc, broad spectrum serine protease that is isolated from the saprophytic fungus Tritirachium album.
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Human Recombinant Flap Endonuclease 1 (from E. coli)
Supplier: Prosci
Flap Endonuclease 1 (FEN1) is a member of the XPG/RAD2 endonuclease family
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Human Recombinant Ribonuclease K6 (from Cells)
Supplier: Prosci
Ribonuclease K6 (RNASE6) is a secreted protein that belongs to the pancreatic ribonuclease family
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DNase I-XT
Supplier: New England Biolabs (NEB)
An engineered variant of DNase I, DNase I-XT is a salt-tolerant DNA endonuclease that nonspecifically cleaves DNA to release di-, tri- and oligonucleotide products with 5'-phosphorylated and 3'-hydroxylated ends (1,2).
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Endonuclease
Supplier: Lucigen
Remove all types of RNA and DNA with this robust, flexible nuclease
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APE 1
Supplier: New England Biolabs (NEB)
Human apurinic/apyrimidinic (AP) endonuclease, APE 1, also known as HAP 1 or Ref-1, shares homology with E
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E. coli Exonuclease III
Supplier: Lucigen
Digest duplex DNA in a 3´ to 5´ direction from a nick, blunt end, or 3´-recessed end, producing stretches of ssDNA
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M-MLV Reverse Transcriptase
Supplier: Promega Corporation
M-MLV RT is an RNA-dependent DNA polymerase that can be used in cDNA synthesis with long messenger RNA templates (>5kb).
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Tth Argonaute (TtAgo)
Supplier: New England Biolabs (NEB)
TtAgo is a prokaryotic argonaute from the Gram-negative, thermophilic bacterium Thermus thermophilus which functions as a DNA-guided endonuclease when provided with a 16-18 nucleotide long 5-phosphorylated single-stranded DNA oligonucleotide guide.
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AMV Reverse Transcriptase
Supplier: Promega Corporation
AMV RT catalyzes DNA polymerization using template DNA, RNA or RNA:DNA hybrids.
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AMV Reverse Transcriptase
Supplier: Promega Corporation
AMV RT catalyzes DNA polymerization using template DNA, RNA or RNA:DNA hybrids.
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Recombinant Fungi Proteinase K
Supplier: Alkali Scientific
Unlock the power of protein extraction with UltraPure Grade Proteinase K Powder, by Alkali Scientific™.
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Proteinase K
Supplier: Promega Corporation
Proteinase K, produced by the fungus Tritirachium album Limber, is a serine protease that exhibits broad cleavage activity. Proteinase K (PK) Solution is supplied at a concentration of 20 mg/ml in 10mM Tris-HCl (pH 7.5), 1 mM calcium chloride, 50% glycerol.
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Tritirachium album Proteinase K, MP Biomedicals
Supplier: MP Biomedicals
Proteinase K is a highly active stable endopeptidase with a broad spectrum of action was isolated by E. Merk's Darmstadt Biochemical Research Department in 1970 from a culture filtrate of the fungus, Tritirachium album Limber. This fungus is able to grow on Keratin (e.g., wool, horn particles) as the sole source of carbon and nitrogen. The isolated protease was, therefore, given the K designation.
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Bovine Deoxyribonuclease I (from Pancreas), MP Biomedicals
Supplier: MP Biomedicals
Deoxyribonuclease from beef pancreas, DNase I, was first crystallized by Kunitz. It is an endonuclease which splits phosphodiester linkages, preferentially adjacent to a pyrimidine nucleotide yielding 5'-phosphate terminated polynucleotides with a free hydroxyl group on position 3'. The average chain of limit digest is a tetranucleotide. DNase I acts upon single chain DNA, and upon double-stranded DNA and chromatin. In the latter case, although histones restrict susceptibility to nuclease action, over a period of time nearly all chromatin DNA is acted upon. According to Mirsky and Silverman, this could result from the looseness of histone attachment to DNA. They found that lysine-rich histones more effectively block DNase access to DNA than arginine-rich histones. Billing and Bonner suggest that DNase attacks the histone-free strand of chromatin DNA. Schmidt, et. al.indicate that hydrolysis of the histone-free region of DNA strands accounts for the initial rapid action of the enzyme on chromatin. Bollum reports degradation of synthetic homopolymer complexes by DNase I. The intracellular functions of the enzyme are probably controlled by a DNase inhibitor, which according to Lazarides and Lindberg is actin.