Enzymes
Product List
APEX1 Human
APEX Nuclease-1 Human Recombinant
APEX1 protein is fused to a 14 amino acid T7-tag at N-terminus and is purified by standard chromatography.
Benzonase Nuclease, 90%
Benzonase Nuclease Serratia Marcescens Recombinant, 90%
Benzonase Nuclease Serratia Marcescens Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 245 amino acids and having a molecular mass of 30kDa with 2 essential disulfide bonds.
Benzonase Nuclease is purified by proprietary chromatographic techniques.
Escherichia Coli.
Benzonase Nuclease, 99%
Benzonase Nuclease Serratia Marcescens Recombinant, 99%
Benzonase Nuclease Serratia Marcescens Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 245 amino acids and having a molecular mass of 30kDa with 2 essential disulfide bonds.
Benzonase Nuclease is purified by proprietary chromatographic techniques.
Escherichia Coli.
CAS9 S. Pyogenes
CRISPR-Associated Protein-9 Nuclease S. Pyogenes Recombinant
DNase Human
Deoxyribonuclease I Human Recombinant
Deoxyribonuclease I Human Recombinant produced in CHO is a glycosylated, polypeptide chain containing 260 amino acids and having a total molecular mass of 37,000 Dalton with a molecular formula of C1321H1999N339O396S9.
DNase is purified by proprietary chromatographic techniques.
ELAC1 Human
ElaC Ribonuclease Z 1 Human Recombinant
ELAC1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
REXO1 Human
RNA Exonuclease 1 Human Recombinant
REXO2 Human
RNA Exonuclease 2 Human Recombinant
RNASE1 Human
Ribonuclease 1 Human Recombinant
RNASE1 Human Recombinant produced in HEK cells is a single, glycosylated, polypeptide chain (29-156 a.a) containing a total of 134 amino acids, having a molecular mass of 15.3kDa.
RNASE1 is fused to a 6 amino acid His-tag at C-terminus,and is purified by proprietary chromatographic techniques.
Introduction
Nucleases are enzymes that cleave the phosphodiester bonds between nucleotides in nucleic acids. They are broadly classified into two main types:
- Endonucleases: These enzymes cut nucleic acids at internal sites within the molecule.
- Exonucleases: These enzymes remove nucleotides from the ends of the nucleic acid chain.
Key Biological Properties: Nucleases are essential for various cellular processes, including DNA replication, repair, and recombination. They exhibit specificity for single-stranded or double-stranded nucleic acids and can be dependent on metal ions for their activity.
Expression Patterns: Nucleases are expressed in a wide range of organisms, from bacteria to humans. Their expression can be constitutive or inducible, depending on the cellular context and environmental conditions.
Tissue Distribution: In multicellular organisms, nucleases are distributed across various tissues. For example, DNase I is found in the pancreas, while RNase A is abundant in the pancreas and other tissues.
Primary Biological Functions: Nucleases play a critical role in maintaining genomic integrity by participating in DNA repair and recombination. They also facilitate the degradation of foreign nucleic acids, such as viral DNA or RNA.
Role in Immune Responses: Nucleases are involved in the immune response by degrading the nucleic acids of invading pathogens. For instance, DNase I helps to clear extracellular DNA during infections, preventing the formation of neutrophil extracellular traps (NETs).
Pathogen Recognition: Some nucleases, such as RNase L, are activated in response to viral infections and degrade viral RNA, thereby limiting viral replication.
Mechanisms with Other Molecules and Cells: Nucleases interact with various proteins and nucleic acids to exert their functions. For example, the CRISPR-associated nuclease Cas9 forms a complex with guide RNA to target specific DNA sequences for cleavage.
Binding Partners: Nucleases often require cofactors, such as metal ions (Mg²⁺, Mn²⁺), for their catalytic activity. They may also interact with other proteins that modulate their activity or specificity.
Downstream Signaling Cascades: The activity of nucleases can trigger downstream signaling pathways. For instance, the activation of RNase L leads to the degradation of viral RNA and the induction of interferon-stimulated genes, enhancing the antiviral response.
Transcriptional Regulation: The expression of nucleases is tightly regulated at the transcriptional level. Specific transcription factors can activate or repress the transcription of nuclease genes in response to cellular signals.
Post-Translational Modifications: Nucleases can undergo various post-translational modifications, such as phosphorylation, ubiquitination, and acetylation, which can modulate their activity, stability, and interactions with other molecules.
Biomedical Research: Nucleases are invaluable tools in molecular biology research. Restriction endonucleases are used for DNA cloning, while CRISPR-Cas9 has revolutionized genome editing.
Diagnostic Tools: Nucleases are employed in diagnostic assays, such as PCR and qPCR, to amplify and detect specific nucleic acid sequences.
Therapeutic Strategies: Nucleases have therapeutic potential in treating genetic disorders, cancers, and viral infections. For example, gene therapy approaches using CRISPR-Cas9 aim to correct genetic mutations.
Development: Nucleases are crucial during development for processes such as programmed cell death (apoptosis), where they degrade DNA in dying cells.
Aging: The activity of nucleases can influence aging by affecting genomic stability. Dysregulation of nuclease activity can lead to the accumulation of DNA damage, contributing to age-related diseases.
Disease: Nucleases play a role in various diseases. For instance, mutations in the gene encoding DNase I are associated with systemic lupus erythematosus (SLE), an autoimmune disease.
