Dimeric Siglecs
Native-like Structure. Bioactive Performance. Reliable Results.
Conigen’s recombinant Siglecs, including Siglec-6 mimic native structures essential for studying sialic acid recognition, immune modulation, and therapeutic intervention in inflammatory diseases and cancer.
Siglecs (Sialic acid-binding immunoglobulin-like lectins) are a family of immunoregulatory receptors expressed on immune cells. They modulate responses by binding glycosylated ligands and recruiting inhibitory signaling pathways via ITIM domains. Many Siglecs dimerize to enhance ligand binding and receptor clustering, mechanisms crucial for fine-tuning immune tolerance and inflammation. Native-like dimerization is key to understanding their role in immune evasion, autoimmune disease, and tumor-associated immune suppression.
Conigen’s recombinant proteins enable functional analysis of Siglec-ligand interactions and support antibody discovery and immune checkpoint targeting.
Spotlight: Siglec-6
Bioactive Performance
Siglec-6 is an inhibitory receptor expressed on B cells, mast cells, and select tumor-infiltrating lymphocytes. Conigen’s recombinant Siglec-6 protein dimer mimics its native configuration, enabling high-affinity binding to sialoglycan ligands and detection of ligand-specific antibody responses.
Human Siglec 6 protein dimer, His-Avi Tag (CSP-25203-01) potently binds to Siglec 6 specific monoclonal antibody (mAb) as measured by ELISA. The Siglec protein dimer (0.2 μg/ml) was coated on 96-well microtiter plates and detected by serial dilutions of anti-human Siglec 6 mAb.
This recombinant protein can potentially serve as a very useful immunogen and antigen for basic research and drug discovery.