SEPT Recombinant Proteins 

SEPT (Septin) recombinant proteins represent a family of GTP-binding cytoskeletal proteins involved in various cellular processes, including cell division, membrane dynamics, intracellular trafficking, and cytoskeletal organization. Septins form highly ordered polymeric structures such as filaments, rings, and scaffolds, essential for cellular architecture and signaling.

Content on SEPT Recombinant Proteins

• Structure and Function
  • Septins are conserved across eukaryotes and characterized by:
    • GTPase Domain: Facilitates GTP binding and hydrolysis.
    • Coiled-Coil Domain: Promotes oligomerization and filament formation.
    • N-terminal Domain: Regulates interactions with other proteins and membranes.
  • SEPT proteins can form homo- or hetero-oligomers and interact with the cytoskeleton, lipid bilayers, and signaling molecules.
• Expression Systems
  • Prokaryotic Systems (e.g., E. coli): Efficient for producing SEPT domains or fragments for biochemical assays.
  • Eukaryotic Systems (e.g., insect or mammalian cells): Ensure proper folding, post-translational modifications, and assembly into functional complexes.

Applications of SEPT Recombinant Proteins

• Cell Division Studies
  • Examine the role of SEPT proteins in cytokinesis, particularly in forming the contractile ring and midbody structure.
  • Analyze septin dysfunction in abnormal mitosis and aneuploidy.
• Membrane Dynamics and Trafficking
  • Investigate septin functions in membrane remodeling, vesicle trafficking, and organelle segregation.
  • Study their role in endocytosis and exocytosis processes.
• Disease Research
  • Cancer: Explore septin overexpression or mutations in cancer progression and metastasis.
  • Neurological Disorders: Study septin aggregation and dysfunction in neurodegenerative diseases like Alzheimer’s or Parkinson’s.

SEPT recombinant proteins are indispensable tools for understanding the complex roles of septins in cellular and disease processes. They provide valuable insights into the structural and functional dynamics of these critical cytoskeletal components.