Recombinant Human MFAP5 protein

MFAP5 (Microfibril-associated protein 5), also known as MAGP-2. is a secreted extracellular matrix (ECM) protein that plays a critical role in maintaining tissue integrity and regulating cellular interactions. It belongs to the microfibril-associated protein family, which is closely associated with elastin fibers and fibrillin-rich microfibrils in the ECM. Structurally, MFAP5 contains two conserved epidermal growth factor (EGF)-like domains and a unique C-terminal region, enabling interactions with other ECM components like fibrillin-1 and integrins. These interactions contribute to microfibril organization, elastic fiber assembly, and cell-ECM signaling.

Functionally, MFAP5 is implicated in tissue development, wound healing, and modulation of transforming growth factor-beta (TGF-β) signaling pathways. It regulates cell adhesion, migration, and proliferation by influencing integrin-mediated signaling and ECM remodeling. Dysregulation of MFAP5 has been linked to various pathological conditions, including cancer progression, cardiovascular diseases, and fibrotic disorders. In cancers, elevated MFAP5 expression correlates with tumor angiogenesis, metastasis, and poor prognosis, potentially through promoting epithelial-mesenchymal transition (EMT) and matrix metalloproteinase (MMP) activation.

Recombinant MFAP5 protein is produced using heterologous expression systems (e.g., E. coli or mammalian cells) for in vitro studies. It serves as a tool to investigate MFAP5's biological roles, its interactions with ECM components, and its therapeutic potential. Researchers utilize purified recombinant MFAP5 to study its effects on cell behavior, ECM dynamics, and signaling pathways, aiming to develop biomarkers or targeted therapies for MFAP5-associated diseases. Its applications extend to tissue engineering, where ECM modulation is critical for scaffold design.