You searched for: Enzymes
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.
Human recombinant Set7/9 Histone Methyltransferase
Supplier: Apollo Scientific
Human recombinant Set7/9 Histone Methyltransferase
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Bovine Ribonuclease A (from Pancreas)
Supplier: PanReac AppliChem
DNAse-free
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Aspergillus niger Glucose oxidase
Supplier: Apollo Scientific
Lyophilized powder. From Aspergillus niger. Specific activity: IU/mg protein>300 units. IU per 1mg powder is approximately 450 units.
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Leuconostoc mesenteroides Sucrose phosphorylase
Supplier: Apollo Scientific
Lyophilized powder. From Leuconostoc mesenteroides. Specific activity: IU/mg protein>100 units. IU per 1mg powder is approximately 100 units.
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Recombinant ProMatrix metalloproteinase-7
Supplier: Apollo Scientific
Recombinant ProMatrix metalloproteinase-7
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Porcine Enteropeptidase/Enterokinase
Supplier: Apollo Scientific
Porcine Enteropeptidase/Enterokinase
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Human recombinant Glycogen Phosphorylase
Supplier: Apollo Scientific
Human recombinant Glycogen Phosphorylase
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Human recombinant TBK1 (from Baculovirus (Insect cells))
Supplier: Cayman Chemical
Human recombinant TBK1 (from Baculovirus (Insect cells))
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DNase I
Supplier: AGILENT
Purified DNase I tested to be free of contaminating activity for the degradation of nucleic acids.
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Recombinant uridine phosphorylase Salmonella typhimurium
Supplier: Apollo Scientific
Recombinant uridine phosphorylase Salmonella typhimurium
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Proteinase K
Supplier: AGILENT
Proteinase K is a broad spectrum protease from Tritirachium album that is ideal for preparing chromosomal DNA.
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Human Recombinant Proprotein Convertase 9 (from Cells)
Supplier: ProSci Inc.
Human Proprotein Convertase Subtilisin/Kexin Type 9 (PCSK9) is a secretory subtilase belonging to the proteinase K subfamily.
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Clostridium kluyveri Diaphorase
Supplier: Apollo Scientific
Lyophilized powder. From Clostridium kluyveri. Specific activity: IU/mg powder>20 units. IU per 1mg powder is approximately 300 units.
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Proteinase K solution
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.
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Human Recombinant Acylphosphate Phosphohydrolase 2 (from E. coli)
Supplier: ProSci Inc.
ACYP2, also known as Acylphosphatase-2, Acylphosphatase, muscle type isozyme, Acylphosphate phosphohydrolase 2, is a protein which belongs to the acylphosphatase family.ACYP2 contains one acylphosphatase-like domain.
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Peroxidase, Horseradish, RZ3 (POD, HRP, HRPO)
Supplier: US Biological
Horseradish Peroxidase (HRP) is a hemoprotein catalysing the oxidation by hydrogen peroxide of a number of substrates such as ascorbate, ferrocyanide, cytochrome C and the leuko form of many dyes.
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Human Recombinant Superoxide Dismutase 1 (from E. coli)
Supplier: Novus Biologicals
The Recombinant Human SOD1/Cu-Zn SOD Protein is derived from E. coli. The Recombinant Human SOD1/Cu-Zn SOD Protein has been validated for the following applications: Functional, SDS-Page, Bioactivity.
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Deoxyribonuclease I
Supplier: Rockland Immunochemicals
Deoxyribonuclease I (usually called DNase I), is an endonuclease coded by the human gene DNASE1. DNase I is a nuclease that cleaves DNA preferentially at phosphodiester linkages adjacent to a pyrimidine nucleotide, yielding 5'-phosphate-terminated polynucleotides with a free hydroxyl group on position 3', on average producing tetranucleotides. It acts on single-stranded DNA, double-stranded DNA, and chromatin.
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Bovine MSG-Trypsin™
Supplier: G-Biosciences
Trypsin is a serine endopeptidase that specifically cleaves peptide bonds on the carboxy side of s-aminoethyl cysteine, arginine and lysine residues and typically there is little or no cleavage at arginyl-proline and lysyl-proline bonds. The distribution of these residues in proteins allows trypsin digestion to produce peptides that are readily identified by mass spectrometry.