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Recombinant Proteins
Recombinant Human SEPTIN6 Protein, also known as Septin 6, is a protein encoded by the SEPTIN6 gene located on human chromosome 22q11.2. This protein is a member of the septin family, a group of GTP-binding proteins involved in various cellular processes, including cell division, cytoskeletal organization, and membrane trafficking. Recombinant Human SEPTIN6 Protein is a highly conserved protein found in a wide range of eukaryotic organisms, including humans.
The primary structure of Recombinant Human SEPTIN6 Protein consists of 437 amino acids with a molecular weight of approximately 50 kDa. It contains a GTP-binding domain, a coiled-coil domain, and a C-terminal domain. The GTP-binding domain is responsible for the protein’s GTPase activity, while the coiled-coil domain is involved in protein-protein interactions, allowing Recombinant Human SEPTIN6 Protein to form complexes with other septins. The C-terminal domain is thought to play a role in regulating the protein’s function.
The secondary structure of Recombinant Human SEPTIN6 Protein is characterized by a series of alpha-helices and beta-strands, forming a rod-like structure. This structure is essential for the protein’s function as it allows it to interact with other proteins and form higher-order structures.
Recombinant Human SEPTIN6 Protein plays a crucial role in various cellular processes, including cytokinesis, cell migration, and vesicle trafficking. It forms heteromeric complexes with other septins and interacts with actin, microtubules, and other cytoskeletal components to regulate their organization and dynamics.
One of the essential functions of Recombinant Human SEPTIN6 Protein is its involvement in cytokinesis, the process of cell division. It forms a ring-like structure at the midbody, a structure that forms between the two daughter cells during cell division. This ring-like structure is thought to act as a scaffold for the recruitment of other proteins involved in cytokinesis, allowing for the successful separation of the two daughter cells.
Recombinant Human SEPTIN6 Protein also plays a role in cell migration, a process essential for embryonic development, wound healing, and immune response. It forms complexes with other septins and actin, regulating the formation and dynamics of actin filaments, which are crucial for cell movement.
Moreover, Recombinant Human SEPTIN6 Protein is involved in vesicle trafficking, the process of transporting molecules and organelles within the cell. It forms complexes with other septins and interacts with proteins involved in vesicle formation and transport, allowing for the efficient movement of molecules and organelles within the cell.
Due to its crucial role in various cellular processes, Recombinant Human SEPTIN6 Protein has become a valuable tool in scientific research. It is commonly used in in vitro and in vivo studies to investigate the protein’s function and its interactions with other proteins.
Recombinant Human SEPTIN6 Protein is also used in drug discovery and development. Dysregulation of septins has been linked to various diseases, including cancer, neurodegenerative disorders, and infectious diseases. By understanding the role of Recombinant Human SEPTIN6 Protein in these diseases, researchers can develop targeted therapies to treat them.
Moreover, Recombinant Human SEPTIN6 Protein is also used in biotechnology and biopharmaceutical industries. It is produced in large quantities using recombinant DNA technology and used as an antigen in the production of antibodies for diagnostic and therapeutic purposes.
In conclusion, Recombinant Human SEPTIN6 Protein is a highly conserved protein with a crucial role in various cellular processes, including cytokinesis, cell migration
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