Recombinant Proteins
Product List
CCDC101 Human
Coiled-Coil Domain Containing 101 Human Recombinant
CCDC101 is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
CCDC104 Human
Coiled-Coil Domain Containing 104 Human Recombinant
CCDC23 Human
Coiled-Coil Domain Containing 23 Human Recombinant
CCDC23 is fused to a 25 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
CCDC25 Human
Coiled-Coil Domain Containing 25 Human Recombinant
CCDC25 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
CCDC43 Human
Coiled-Coil Domain Containing 43 Human Recombinant
CCDC69 Human
Coiled-Coil Domain Containing 69 Human Recombinant
CCDC69 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
CCDC90B Human
Coiled-Coil Domain Containing 90B Human Recombinant
CCDC90B is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
CHCHD3 Human
Coiled-Coil-Helix-Coiled-Coil-Helix Domain Containing 3 Human Recombinant
CHCHD7 Human
Coiled-Coil-Helix-Coiled-Coil-Helix Domain Containing 7 Human Recombinant
Introduction
The coiled-coil domain is a structural motif in proteins where 2-7 alpha-helices are coiled together like the strands of a rope. These domains are characterized by a heptad repeat pattern (abcdefg), where positions ‘a’ and ‘d’ are typically hydrophobic residues, facilitating the coiling interaction. Coiled-coil domains can be classified based on the number of helices involved (e.g., dimeric, trimeric) and their specific sequence patterns.
Key Biological Properties: Coiled-coil domains are known for their stability and ability to mediate protein-protein interactions. They often form elongated, rod-like structures that can span considerable distances within the cell.
Expression Patterns: These domains are found in a wide variety of proteins across different species, from bacteria to humans. They are particularly abundant in structural proteins and transcription factors.
Tissue Distribution: Coiled-coil domains are ubiquitous and can be found in various tissues, including muscle, skin, and the nervous system. Their distribution is often linked to the specific functions of the proteins they are part of.
Primary Biological Functions: Coiled-coil domains play crucial roles in the structural integrity of cells and tissues. They are involved in the formation of cytoskeletal elements, such as intermediate filaments, and in the assembly of protein complexes.
Role in Immune Responses and Pathogen Recognition: Some coiled-coil domain-containing proteins are involved in immune responses, acting as scaffolds for the assembly of signaling complexes that detect and respond to pathogens.
Mechanisms with Other Molecules and Cells: Coiled-coil domains facilitate the interaction between proteins by providing a stable interface for binding. This interaction can be homotypic (between identical proteins) or heterotypic (between different proteins).
Binding Partners and Downstream Signaling Cascades: Coiled-coil domains often interact with other coiled-coil domains or with different protein motifs. These interactions can trigger downstream signaling cascades that regulate various cellular processes, such as gene expression, cell division, and apoptosis.
Regulatory Mechanisms Controlling Expression and Activity: The expression of coiled-coil domain-containing proteins is tightly regulated at the transcriptional level by specific transcription factors. Post-translational modifications, such as phosphorylation and ubiquitination, can also modulate their activity and interactions.
Transcriptional Regulation: Specific promoter regions and transcription factors control the expression of genes encoding coiled-coil domain-containing proteins. These regulatory elements ensure that the proteins are produced in response to cellular needs.
Post-Translational Modifications: Coiled-coil domains can undergo various post-translational modifications that affect their stability, localization, and interaction with other proteins. Phosphorylation, for example, can alter the binding affinity of coiled-coil domains for their partners.
Biomedical Research: Coiled-coil domains are used as model systems to study protein-protein interactions and the principles of protein folding. They are also employed in the design of synthetic proteins and nanomaterials.
Diagnostic Tools: Coiled-coil domains can be engineered to create biosensors that detect specific biomolecules, making them valuable tools in diagnostics.
Therapeutic Strategies: Targeting coiled-coil domain interactions is a potential therapeutic strategy for diseases where these interactions are dysregulated, such as cancer and neurodegenerative disorders.
Role Throughout the Life Cycle: Coiled-coil domains are involved in various stages of the life cycle, from development to aging. During development, they contribute to the formation of tissues and organs. In adulthood, they maintain cellular structure and function. In aging and disease, alterations in coiled-coil domain interactions can lead to cellular dysfunction and pathology.
