Nudix Type Motif 4 Human Recombinant
Nudix Type Motif 5 Human Recombinant
Nudix Type Motif 9 Human Recombinant
NUDT9 produced in E.Coli is a single, non-glycosylated polypeptide chain containing 325 amino acids (47-350 a.a.) and having a molecular mass of 36.5kDa (molecular weight on SDS-PAGE will appear higher).
NUDT9 is fused to a 21 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Nudix Type Motif 1 Human Recombinant
Nudix Type Motif 10 Human Recombinant
NUDT10 produced in E.Coli is a single, non-glycosylated polypeptide chain containing 172 amino acids (1-164 a.a.) and having a molecular mass of 19.5kDa.
NUDT10 is fused to an 8 amino acid His-tag at C-terminus & purified by proprietary chromatographic techniques.
Nudix Type Motif 14 Human Recombinant
Nudix Type Motif 16 Human Recombinant
Nudix Type Motif 16 Like-1 Human Recombinant
Nudix Type Motif 2 Human Recombinant
Nudix Type Motif 21 Human Recombinant
The Nudix (nucleoside diphosphate linked to some other moiety X) type motif is a conserved protein domain found in a wide range of organisms, including bacteria, archaea, and eukaryotes. This motif is characterized by a conserved sequence of amino acids that form a specific structural fold, enabling the hydrolysis of nucleoside diphosphates linked to various moieties. Nudix hydrolases are classified based on their substrate specificity and the presence of the Nudix motif, which typically consists of the sequence GX5EX7REUXEEXGU (where X is any amino acid and U is a hydrophobic residue).
Key Biological Properties: Nudix hydrolases are involved in the hydrolysis of a wide range of substrates, including nucleoside diphosphates, nucleotide sugars, and capped mRNA. They play a crucial role in maintaining cellular homeostasis by eliminating potentially harmful nucleotide derivatives.
Expression Patterns: The expression of Nudix hydrolases varies across different tissues and developmental stages. Some Nudix proteins are ubiquitously expressed, while others show tissue-specific expression patterns.
Tissue Distribution: Nudix hydrolases are found in various cellular compartments, including the cytoplasm, mitochondria, and nucleus. Their distribution is often linked to their specific biological functions.
Primary Biological Functions: Nudix hydrolases are primarily involved in the detoxification of nucleotide derivatives, regulation of nucleotide pools, and maintenance of cellular homeostasis. They also play a role in mRNA decapping, which is essential for mRNA turnover and regulation of gene expression.
Role in Immune Responses: Some Nudix hydrolases are involved in the immune response by modulating the levels of signaling molecules such as ADP-ribose and cyclic ADP-ribose, which are important for immune cell activation and signaling.
Pathogen Recognition: Nudix hydrolases can recognize and hydrolyze pathogen-derived nucleotides, contributing to the host defense mechanisms against infections.
Mechanisms with Other Molecules and Cells: Nudix hydrolases interact with various molecules, including nucleotides, proteins, and RNA. These interactions are crucial for their enzymatic activity and substrate specificity.
Binding Partners: Nudix hydrolases often form complexes with other proteins, which can modulate their activity and substrate specificity. For example, some Nudix proteins interact with RNA-binding proteins to regulate mRNA decapping.
Downstream Signaling Cascades: The hydrolysis of nucleotide derivatives by Nudix hydrolases can generate signaling molecules that activate downstream signaling pathways. For example, the hydrolysis of ADP-ribose by Nudix hydrolases can generate AMP, which activates AMP-activated protein kinase (AMPK) signaling.
Regulatory Mechanisms that Control Expression and Activity: The expression and activity of Nudix hydrolases are tightly regulated at multiple levels, including transcriptional, post-transcriptional, and post-translational mechanisms.
Transcriptional Regulation: The transcription of Nudix genes is regulated by various transcription factors and signaling pathways. For example, the expression of some Nudix genes is induced by oxidative stress and other cellular stressors.
Post-Translational Modifications: Nudix hydrolases can undergo various post-translational modifications, such as phosphorylation, acetylation, and ubiquitination, which can modulate their activity, stability, and subcellular localization.
Biomedical Research: Nudix hydrolases are studied for their roles in various diseases, including cancer, neurodegenerative disorders, and infectious diseases. Understanding their functions and regulatory mechanisms can provide insights into disease pathogenesis and potential therapeutic targets.
Diagnostic Tools: Nudix hydrolases can serve as biomarkers for certain diseases. For example, altered expression levels of specific Nudix proteins have been associated with cancer and other pathological conditions.
Therapeutic Strategies: Targeting Nudix hydrolases with small molecules or other therapeutic agents can be a potential strategy for treating diseases. For example, inhibitors of specific Nudix hydrolases are being explored as potential anticancer agents.
Role Throughout the Life Cycle: Nudix hydrolases play essential roles throughout the life cycle, from development to aging and disease. During development, they are involved in regulating nucleotide pools and gene expression. In aging, their roles in maintaining cellular homeostasis and preventing the accumulation of harmful nucleotide derivatives are crucial for cellular health.
Development to Aging and Disease: Dysregulation of Nudix hydrolases has been linked to various age-related diseases, including cancer and neurodegenerative disorders. Understanding their roles in these processes can provide insights into the mechanisms of aging and disease progression.