NUDT1 Human

Nudix Type Motif 1 Human Recombinant

Recombinant human NUDT1, with a 20 amino acid His tag at the N-terminus, is produced in E. coli. This purified protein is a single, non-glycosylated polypeptide chain comprising 176 amino acids (with 156 a.a. from NUDT1) and has a molecular weight of 20.1kDa. The purification process employs proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT16275
Source
Escherichia Coli.
Appearance
A clear, colorless solution that has been sterilized by filtration.

NUDT10 Human

Nudix Type Motif 10 Human Recombinant

Recombinantly produced in E.Coli, NUDT10 is a single, non-glycosylated polypeptide chain consisting of 172 amino acids (with active residues spanning from 1 to 164) and possesses a molecular weight of 19.5kDa. The protein is engineered with an 8 amino acid His-tag at the C-terminus to facilitate purification, which is achieved through proprietary chromatographic methods.
Shipped with Ice Packs
Cat. No.
BT16358
Source
Escherichia Coli.
Appearance
The product is a sterile, filtered solution, colorless in appearance.

NUDT14 Human

Nudix Type Motif 14 Human Recombinant

Recombinant human NUDT14, expressed in E. coli, is a non-glycosylated polypeptide chain comprising 245 amino acids (residues 1-222). With a molecular weight of 26.5 kDa, this protein features a 23 amino acid His-tag at the N-terminus and undergoes purification through proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT16447
Source
Escherichia Coli.
Appearance
The product is a clear, sterile-filtered solution.

NUDT16 Human

Nudix Type Motif 16 Human Recombinant

Produced in E. coli, NUDT16 is a single, non-glycosylated polypeptide chain comprising 215 amino acids (1-195a.a.) with a molecular weight of 23.4kDa. This protein is expressed with a 20 amino acid His-tag at the N-terminus and purified using proprietary chromatographic methods.
Shipped with Ice Packs
Cat. No.
BT16511
Source
Escherichia Coli.
Appearance
Clear, sterile solution after filtration.

NUDT3 Human

Nudix Type Motif 3 Human Recombinant

Recombinant human NUDT3, fused with a 20-amino acid His tag at its N-terminus, is produced in E. coli. It exists as a single, non-glycosylated polypeptide chain composed of 192 amino acids (residues 1-172) and has a molecular weight of 21.6 kDa. Purification of NUDT3 is achieved through proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT16886
Source
Escherichia Coli.
Appearance
A sterile, colorless solution.

NUDT9 Human

Nudix Type Motif 9 Human Recombinant

Produced in E. coli, NUDT9 is a single, non-glycosylated polypeptide chain consisting of 325 amino acids (47-350 a.a.). It has a molecular mass of 36.5 kDa, although it may appear larger on SDS-PAGE due to the N-terminal 21 amino acid His-tag. Purification is achieved through proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT17991
Source
Escherichia Coli.
Appearance
Sterile, colorless, and filtered solution.

NUDT4 Human

Nudix Type Motif 4 Human Recombinant

This product consists of the recombinant NUDT4 protein, produced in E. coli. It is a single, non-glycosylated polypeptide chain with a molecular weight of 22.7 kDa. The protein sequence encompasses 203 amino acids, including a 23 amino acid His-tag fused at the N-terminus (amino acids 1-180 represent the NUDT4 sequence). The purification process involves proprietary chromatographic techniques to ensure high purity.
Shipped with Ice Packs
Cat. No.
BT17769
Source
Escherichia Coli.
Appearance
The product is a clear, colorless solution that has been sterilized through filtration.

NUDT5 Human

Nudix Type Motif 5 Human Recombinant

Recombinant Human NUDT5, produced in E. coli, is a single polypeptide chain that lacks glycosylation. It comprises 239 amino acids (specifically, amino acids 1 to 219) and has a molecular weight of 26.5 kDa. A 20 amino acid His-Tag is attached to the N-terminus of the NUDT5 protein. Purification is achieved using proprietary chromatographic methods.
Shipped with Ice Packs
Cat. No.
BT17832
Source
Escherichia Coli.
Appearance
A colorless solution that has been sterilized by filtration.

NUDT16L1 Human

Nudix Type Motif 16 Like-1 Human Recombinant

Recombinant human NUDT16L1, produced in E. coli, is fused with a 20 amino acid His tag at its N-terminus. This results in a single, non-glycosylated polypeptide chain comprising 231 amino acids (amino acids 1-211) with a molecular weight of 25.5kDa. The purification of NUDT16L1 is carried out using proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT16596
Source
Escherichia Coli.
Appearance
The product is a colorless solution that has undergone sterile filtration.

NUDT2 Human

Nudix Type Motif 2 Human Recombinant

Recombinant NUDT2, expressed in E. coli, is a single, non-glycosylated polypeptide chain comprising 167 amino acids (1-147a.a.) with a molecular weight of 19.0 kDa. It features a 20 amino acid His-tag at the N-terminus and undergoes purification using proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT16666
Source
Escherichia Coli.
Appearance
A clear solution that has been sterilized by filtration.
Definition and Classification

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).

Biological Properties

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.

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.

Modes of Action

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

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.

Applications

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 in the Life Cycle

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.

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