Recombinant Human ENA78 protein

ENA78 (Epithelial Neutrophil-Activating Peptide 78), also known as CXCL5. is a member of the CXC chemokine family, which plays a critical role in inflammatory and immune responses. Initially identified in the 1990s, it is primarily secreted by epithelial cells, macrophages, and endothelial cells under inflammatory conditions. ENA78 functions by binding to the CXCR2 receptor on neutrophils, inducing chemotaxis, activation, and degranulation, thereby amplifying local immune responses. Its expression is tightly regulated by pro-inflammatory cytokines like IL-1β and TNF-α, as well as microbial components.

Structurally, ENA78 is a small, heparin-binding protein (~8 kDa) containing four conserved cysteine residues forming two disulfide bonds, a hallmark of CXC chemokines. Dysregulation of ENA78 has been implicated in chronic inflammatory diseases (e.g., rheumatoid arthritis, COPD), cancer progression (e.g., promoting angiogenesis, tumor growth, and metastasis), and infectious diseases. Elevated levels of ENA78 are observed in pathological tissues and bodily fluids, correlating with disease severity.

Recombinant ENA78 protein is produced via genetic engineering in systems like *E. coli* or mammalian cells, ensuring high purity and bioactivity. It serves as a vital tool for studying neutrophil biology, inflammation mechanisms, and drug screening. Therapeutic strategies targeting ENA78 or its receptor are under exploration to mitigate inflammation-related pathologies and cancer metastasis. Its dual role as a disease biomarker and therapeutic target underscores its biomedical significance.