Recombinant Mouse Ly6g protein (His tag)

Supplementary information

This supplementary information is collated from multiple sources and compiled automatically.

Ly6G also known as lymphocyte antigen 6 complex locus G6D 1A8 or 8C5 is a glycosylphosphatidylinositol (GPI)-anchored cell surface protein. The molecule has a molecular weight of about 25-30 kDa. Its expression is mainly on neutrophils and a subpopulation of eosinophils in mice. It plays a role in the innate immune system marking these immune cells for differentiation and response to infection. Researchers consider it a specific marker for detecting and isolating mouse neutrophils often using methods such as Ly6G staining or anti-Ly6G antibodies for identification.

Biological function summary

Ly6G functions in the immune response by facilitating the migration and adhesion of neutrophils to the site of infection or injury. It is part of a protein complex on the cell surface that includes other Ly6 proteins. This group of proteins helps to modulate signal transduction for immune cell functions. Ly6G serves as an anchor through its GPI linkage aiding cell-to-cell communication and signal amplification in inflammation processes.

Pathways

Ly6G is significantly integrated into the immune signaling pathways notably the toll-like receptor (TLR) signaling pathway. Through these pathways Ly6G influences neutrophil migration and activation. Closely associated proteins include CD11b and CD18 which interact with Ly6G in neutrophil functions including adhesion and transmigration. These pathways are essential for orchestrating the body's defense mechanisms against pathogens.

Ly6G plays an essential role in inflammatory conditions and autoimmune diseases such as rheumatoid arthritis and systemic lupus erythematosus. Aberrant expression or function of Ly6G can alter neutrophil behavior which contributes to disease pathology. Researchers are investigating the relationship between Ly6G and other immune-related proteins like myeloperoxidase (MPO) and elastase as these protein interactions may impact the development and progression of inflammatory diseases.