Lactoferrin/LTF Protein, Human (691a.a, HEK293, His)

Lactoferrin (LTF), a major iron-binding and multifunctional protein present in exocrine fluids such as breast milk and mucosal secretions, exhibits diverse biological activities. Renowned for its antimicrobial properties, LTF hinders microbial growth through sequestering free iron and releasing lipopolysaccharides from the bacterial outer membrane, thereby displaying both bacteriostatic and bactericidal effects. Moreover, it plays a role in preventing bacterial biofilm development in Pseudomonas aeruginosa infections and demonstrates weak antifungal activity against Candida albicans. Beyond its antimicrobial functions, LTF impacts bone metabolism by exerting anabolic, differentiating, and anti-apoptotic effects on osteoblasts, while also inhibiting osteoclastogenesis. It contributes to adenovirus infection by promoting the binding of species C adenoviruses to epithelial cells and inhibits papillomavirus infections. LTF stimulates the TLR4 signaling pathway, leading to NF-kappa-B activation and pro-inflammatory cytokine production, while concurrently interfering with lipopolysaccharide-stimulated TLR4 signaling. Additionally, it exhibits inhibitory effects on neutrophil granulocyte migration and promotes VEGFA-mediated endothelial cell migration and proliferation. LTF's versatility extends to its binding capabilities, encompassing interactions with heparin, chondroitin sulfate, pneumococcal surface protein A, lysozyme, and DNA.