Recombinant HAVCR (Hepatitis A Virus Cellular Receptor 1), also known as TIM-1 (T-cell Immunoglobulin and Mucin domain-1), proteins are engineered versions of this membrane glycoprotein. HAVCR/TIM-1 is involved in various cellular processes, including immune regulation, cell signaling, and viral infections. Recombinant HAVCR proteins are utilized in research to study their functions and potential therapeutic applications.

Technical Content

• Structure and Function:
  • HAVCR/TIM-1 Structure:
    • Domains: TIM-1 is a type I membrane protein consisting of several key domains:
      • Immunoglobulin-like Domain: This extracellular domain is involved in interactions with ligands and other proteins. It contributes to the protein’s role in immune regulation and cellular adhesion.
      • Mucin-like Domain: A heavily glycosylated region that provides structural stability and may play a role in protein interactions and signaling.
      • Transmembrane Domain: Anchors the protein in the cell membrane, facilitating its interaction with the cytoplasmic domain and external ligands.
• • Function:
    • Immune Regulation: TIM-1 is involved in regulating immune responses. It acts as a co-stimulatory receptor that enhances T-cell activation and differentiation, playing a role in immune tolerance and response.
    • Viral Infection: TIM-1 serves as a receptor for Hepatitis A virus (HAV) and other viruses, facilitating viral entry into host cells.
    • Cell Signaling: TIM-1 participates in various signaling pathways that impact cell proliferation, survival, and differentiation.
• Production:
  • Gene Cloning: The gene encoding TIM-1 is cloned into an expression vector. This vector contains elements for transcription and translation in the chosen host cell system.
  • Expression Systems:
    • Bacterial Systems: E. coli can be used for the production of recombinant TIM-1 proteins. However, bacterial systems may not support the complex post-translational modifications, such as glycosylation, that TIM-1 requires.
    • Yeast Systems: Pichia pastoris or Saccharomyces cerevisiae can be used to express TIM-1 proteins, providing some post-translational modifications but not fully replicating mammalian glycosylation patterns.
• • Purification: Recombinant TIM-1 proteins are purified using affinity chromatography, which isolates the protein based on specific interactions with a ligand or antibody. Additional purification steps, such as ion exchange or gel filtration chromatography, are often used to achieve high purity and biological activity.
• Applications:
  • Research: Recombinant TIM-1 proteins are used to study their role in immune regulation, viral infection, and cellular signaling. They help elucidate mechanisms of TIM-1 function and its implications in health and disease.
  • Therapeutics: Potential therapeutic applications include:
    • Viral Infections: Targeting TIM-1 could offer strategies for preventing or treating infections caused by HAV or other viruses that use TIM-1 as a receptor.
    • Autoimmune and Inflammatory Diseases: Modulating TIM-1 activity may provide therapeutic benefits in autoimmune diseases or inflammatory conditions where TIM-1 plays a role in immune regulation.
    • Cancer Immunotherapy: TIM-1 is involved in immune responses, and targeting it could enhance the efficacy of cancer immunotherapy by modulating T-cell activity.
  • Diagnostics: Recombinant TIM-1 proteins can be used in diagnostic assays to detect TIM-1 expression levels or to identify interactions with viruses or other ligands.
• Advantages:
  • Biological Activity: Recombinant TIM-1 proteins maintain their biological activity, making them suitable for research and therapeutic applications.
  • Consistency: The recombinant production process provides a consistent and reproducible source of TIM-1 proteins, which is important for experimental accuracy and therapeutic development.
  • Purity: High-purity recombinant TIM-1 proteins can be achieved, ensuring that observed effects are due to the specific protein.