IL-11 His Tag Protein, Cynomolgus

IL-11 (Interleukin-11) is a 178-amino-acid four-helix bundle cytokine belonging to the IL-6 family, which activates the JAK/STAT3 signaling pathway by binding to the specific IL-11 receptor alpha chain (IL-11Rα) and recruiting the gp130 co-receptor to form a heterodimeric complex. Structurally, IL-11 consists of four antiparallel α-helices (A-D) that constitute the typical cytokine fold, with helices A and C, as well as B and D, forming two pairs of parallel arrangements connected by two long loop regions—this structural feature determines its high-affinity binding to the receptor. Functionally, IL-11 exhibits pleiotropic biological activities: as a hematopoietic growth factor, it stimulates megakaryocyte maturation and thrombopoiesis; in mucosal protection, it promotes intestinal epithelial cell proliferation and repair; it also possesses anti-inflammatory properties by suppressing pro-inflammatory cytokine production from macrophages; additionally, it participates in bone metabolism regulation, neuroprotection, and reproductive processes. Clinically, recombinant human IL-11 (Oprelvekin) was the first approved therapeutic agent for chemotherapy-induced thrombocytopenia, significantly reducing bleeding risks and transfusion requirements in cancer patients; recent studies have revealed that IL-11 is overexpressed in pulmonary fibrosis, rheumatoid arthritis, and various malignancies (such as gastric and colorectal cancers), where it promotes tissue fibrosis and tumor invasion and metastasis, thereby establishing IL-11 signaling inhibition as a potential new therapeutic target for fibrotic diseases and cancer, with relevant antibody drugs currently under clinical development.