You searched for: DNases

Supplier: VWR Chemicals

VWR® Life Science's DNase, Double-Strand Specific, Heat-Labile is a recombinant endonuclease that cleaves phosphodiester bonds in DNA to yield 2 to 8 bp oligonucleotides with 5’-phosphate and 3’-hydroxyl termini.

Supplier: VWR Chemicals

Deoxyribonuclease I efficiently hydrolyses single-stranded or double-stranded DNA in the presence of divalent cations. Useful in RNA preparations from tissue or bacterial cell cultures, DNase I is a chromatographically purified preparation supplied as a lyophilised powder.

Supplier: PanReac AppliChem

DNAse-free

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.

Supplier: PanReac AppliChem

Proteinase K is used to destruct proteins in cell lysates (tissue, cultured cells) and to liberate nucleic acids, since it very effectively digests DNases and RNases.

Supplier: Thermo Fisher Scientific

Pig Desoxyribonuclease II (from Spleen)

Supplier: MP Biomedicals

Dissolve at a concentration of 1 mg/ml. Dilute further to a concentration of 20 to 60 U/ml immediately before the assay.

Supplier: PanReac AppliChem

Bovine desoxyribonuclease I (from Pancreas)

Supplier: Avantor

J.T.Baker® Endonuclease Ultrapure Bioreagent is designed for the degradation of both single stranded and double stranded DNA and RNA. J.T.Baker® Endonuclease Ultrapure Bioreagent is used to ensure host cell DNA impurities are removed; driving process efficiency by lowering viscosity and preventing aggregation. J.T.Baker® Endonuclease is an enzyme based upon the native endonuclease of Serratia marcescens, enabling rapid clearance of residual DNA and RNA during the production and purification of both recombinant proteins and viral vectors. Non-animal origin. The purity of materials in non-negotiable. J.T.Baker® Endonuclease Ultrapure Bioreagent acts to degrade and eliminate extraneous genetic material, ensuring the pristine quality of your final product.

Supplier: Avantor

J.T.Baker® Endonuclease Biotech Reagent meets the strictest cGMP standards and is designed for the degradation of both single stranded and double stranded DNA and RNA. J.T.Baker® Endonuclease Biotech Reagent is used to ensure host cell DNA impurities are removed; driving process efficiency by lowering viscosity and preventing aggregation. J.T.Baker® Endonuclease Biotech Reagent is an enzyme based upon the native endonuclease of Serratia marcescens, enabling rapid clearance of residual DNA and RNA during the production and purification of both recombinant proteins and viral vectors. Non-animal origin. Absence of proteolytic activity. The purity of materials in non-negotiable. J.T.Baker® Endonuclease Biotech Reagent acts to degrade and eliminate extraneous genetic material, ensuring the pristine quality of your final product.

Supplier: OMEGA BIO-TEK

For enzyme digestion during DNA and RNA preparation. Both OB Protease and Proteinase K offer broad substrate specificity with high activity for a wide range of salts, denaturant and detergent, pH, and temperature conditions. Proteinase K is a subtilisin-type protease isolated from the saprophytic fungus Tritirachiumalbum and is particularly suitable for short digestion times. It possesses a high specific activity which remains stable over a wide range of temperatures and pH values with substantially increased activity at higher temperature.

Supplier: MP Biomedicals

Suitable for both protein and nucleic acid isolation. Exhibits proteolytic activity on proteins, peptides, glycoproteins, amides and esters. Also active with nitroanilides of amino acids with protected amino groups, excluding arginine. Useful in the isolation of DNA and RNA, in the analysis of membrane structures and protein structure. Proteolytic activity: >30mAnson Units/mg Unit definition: One Anson unit is the amount of enzyme which liberates 1 µmol of Folin-positive amino acids per minute at pH 7,5 and 35 °C, using hemoglobin as substrate.

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.
Proteinase K is a stable and highly reactive serine protease. Evidence from crystal and molecular structure studies indicates the enzyme belongs to the subtilisin family with an active-site catalytic triad (Asp39-His69-Ser224). It is stable in a broad range of environments: pH, buffer salts, detergents (SDS), and temperature. In the presence of 0,1 to 0,5% SDS, proteinase K retains activity and will digest a variety of proteins and nucleases in DNA preparations without compromising the integrity of the isolated DNA.