Recombinant Human CXCL6 protein

CXCL6 (C-X-C motif chemokine ligand 6), also known as granulocyte chemotactic protein-2 (GCP-2), is a small secretory protein belonging to the CXC chemokine family. It is primarily produced by endothelial cells, fibroblasts, and immune cells in response to inflammatory stimuli, such as cytokines (e.g., IL-1β, TNF-α) or pathogens. CXCL6 plays a dual role in immune regulation and tissue homeostasis by binding to the G protein-coupled receptors CXCR1 and CXCR2. Its key functions include recruiting neutrophils to sites of inflammation, promoting angiogenesis, and modulating wound healing processes. Dysregulation of CXCL6 has been implicated in chronic inflammatory diseases, cancer progression, and fibrotic disorders.

Recombinant CXCL6 protein is engineered using prokaryotic (e.g., *E. coli*) or eukaryotic expression systems to mimic the native protein’s structure and bioactivity. The production typically involves cloning the CXCL6 gene into expression vectors, followed by purification via affinity chromatography (e.g., His-tag systems). Quality control includes SDS-PAGE, Western blotting, and functional assays (e.g., neutrophil migration tests) to confirm purity, molecular weight (~8-10 kDa), and receptor-binding capacity. Researchers utilize recombinant CXCL6 to study its role in inflammatory pathways, tumor microenvironments, and tissue repair mechanisms. It also serves as a tool for screening therapeutic agents targeting CXCR1/2 receptors. Despite its pro-inflammatory nature, emerging evidence suggests context-dependent roles in both promoting and suppressing disease progression, highlighting its therapeutic potential in regenerative medicine and immuno-oncology.