Recombinant Proteins

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CCDC101 Human

Coiled-Coil Domain Containing 101 Human Recombinant

Recombinant human CCDC101, expressed in E. coli, is a single polypeptide chain with a molecular weight of 35.4 kDa. It consists of 313 amino acids (residues 1-293) and includes a 20 amino acid His-tag fused at the N-terminus. Purification is achieved using proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT11412
Source
E.coli.
Appearance
A clear, sterile-filtered solution.

CCDC104 Human

Coiled-Coil Domain Containing 104 Human Recombinant

This product consists of the human CCDC104 protein, recombinantly produced in E. coli bacteria. The protein is a single, non-glycosylated polypeptide chain comprising 365 amino acids, encompassing the sequence from position 1 to 342. The molecular weight of the protein is 41.8 kDa. The recombinant protein includes a 23 amino acid His-tag attached to the N-terminus, facilitating purification using proprietary chromatographic methods.
Shipped with Ice Packs
Cat. No.
BT11484
Source
Escherichia Coli.
Appearance
A clear solution that has been sterilized by filtration.

CCDC23 Human

Coiled-Coil Domain Containing 23 Human Recombinant

Recombinant CCDC23 protein, specifically the human variant, is produced in E. coli. This protein is a single, non-glycosylated polypeptide chain composed of 91 amino acids, with the first 66 amino acids corresponding to the CCDC23 sequence. It has a molecular weight of 10.5 kDa. For purification and detection purposes, the CCDC23 protein is engineered with a 25 amino acid His-tag fused to its N-terminus. The purification process involves proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT11574
Source
E.coli.
Appearance
The product is a clear, colorless solution that has been sterilized by filtration.

CCDC25 Human

Coiled-Coil Domain Containing 25 Human Recombinant

Recombinant human CCDC25 is produced in E. coli bacteria. It is a single, non-glycosylated polypeptide chain that contains 231 amino acids (amino acids 1-208), with a molecular mass of 26.9 kDa. The protein has a 23 amino acid His-tag fused at the N-terminus and is purified using proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT11638
Source
E.coli.
Appearance
A sterile and colorless solution.

CCDC43 Human

Coiled-Coil Domain Containing 43 Human Recombinant

Recombinant human CCDC43, expressed in E. coli, is a single polypeptide chain with a molecular weight of 27kDa. It encompasses 247 amino acids, including amino acids 1-224 of the CCDC43 sequence, and a 23 amino acid His-tag at the N-terminus. Purification is achieved through proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT11700
Source
E.coli.
Appearance
A sterile, colorless, and clear solution.

CCDC69 Human

Coiled-Coil Domain Containing 69 Human Recombinant

Recombinant human CCDC69 protein, expressed in E. coli, is a single, non-glycosylated polypeptide chain. This protein consists of 319 amino acids (with amino acids 1-296 present) and has a molecular weight of 37.2 kDa. A 23 amino acid His-tag is fused to the N-terminus of CCDC69. Purification is carried out using proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT11749
Source
Escherichia Coli.
Appearance
A sterile, colorless solution.

CCDC90B Human

Coiled-Coil Domain Containing 90B Human Recombinant

Recombinantly produced in E. coli, CCDC90B Human Recombinant is a single, non-glycosylated polypeptide chain. It comprises 211 amino acids (specifically, residues 43 to 230) and exhibits a molecular weight of 24.1 kDa. A 23 amino acid His-tag is fused to the N-terminus of CCDC90B. Purification is achieved using proprietary chromatographic methods.
Shipped with Ice Packs
Cat. No.
BT11791
Source
E.coli.
Appearance
A clear, colorless solution that has been sterilized by filtration.

CHCHD3 Human

Coiled-Coil-Helix-Coiled-Coil-Helix Domain Containing 3 Human Recombinant

Recombinant human CHCHD3 protein, produced in E. coli, is a single, non-glycosylated polypeptide chain consisting of 250 amino acids (specifically, amino acids 1-227). It possesses a molecular mass of 28.5 kDa. A 23 amino acid His-tag is fused to the N-terminus of CHCHD3. Purification is achieved through proprietary chromatographic methods.
Shipped with Ice Packs
Cat. No.
BT11854
Source
Escherichia Coli.
Appearance
A clear solution that has undergone sterile filtration.

CHCHD7 Human

Coiled-Coil-Helix-Coiled-Coil-Helix Domain Containing 7 Human Recombinant

Recombinant CHCHD7 protein, expressed in E. coli, is a single, non-glycosylated polypeptide chain consisting of 120 amino acids (specifically, amino acids 1-97). It has a molecular weight of 13.9 kDa. The protein is engineered with a 23 amino acid His-tag at the N-terminus to facilitate purification, which is achieved through proprietary chromatographic methods.
Shipped with Ice Packs
Cat. No.
BT11918
Source
E.coli.
Appearance
Clear, colorless solution that has been sterilized by filtration.
Definition and Classification

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.

Biological Properties

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.

Biological Functions

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.

Modes of Action

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

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.

Applications

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 in the Life Cycle

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.

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