Recombinant Human CXCL11 protein

CXCL11. a member of the CXC chemokine family, is a small cytokine primarily produced by dendritic cells, macrophages, and endothelial cells in response to interferon (IFN)-γ and IFN-β. It plays a critical role in immune regulation by binding to the G-protein-coupled receptor CXCR3. which is highly expressed on activated T cells, natural killer (NK) cells, and other immune cells. This interaction facilitates chemotaxis, directing immune cell migration to sites of inflammation, infection, or tumorigenesis. CXCL11 is structurally characterized by conserved cysteine residues, including four disulfide-bonded cysteines that stabilize its 3D conformation, essential for receptor activation.

Recombinant CXCL11 protein is engineered through genetic cloning and expression in prokaryotic (e.g., *E. coli*) or eukaryotic systems, followed by purification to >95% homogeneity. The recombinant form typically retains native bioactivity, enabling researchers to study its roles in vitro and in vivo. Key applications include modeling immune responses, investigating tumor microenvironment interactions, and exploring therapeutic strategies in autoimmune diseases (e.g., rheumatoid arthritis), chronic inflammation, or cancer immunotherapy. Functional assays, such as chemotaxis or calcium flux tests, confirm its ability to induce immune cell migration and receptor signaling.

Notably, CXCL11 exhibits overlapping functions with related chemokines CXCL9 and CXCL10 but displays distinct receptor-binding kinetics and stability under physiological conditions. Its upregulated expression in pathological states has positioned it as a potential biomarker or therapeutic target. Recombinant CXCL11 is often modified with tags (e.g., His-tag) for purification and detection, while ensuring minimal interference with functional domains. Quality validation includes endotoxin testing, mass spectrometry, and functional dose-response analyses to guarantee reproducibility in experimental settings.