Recombinant Human AMBP protein

SERPINF2. also known as alpha-2-antiplasmin (α2AP), is a serine protease inhibitor encoded by the SERPINF2 gene. It plays a critical role in regulating fibrinolysis, the process that prevents excessive blood clot formation by breaking down fibrin networks. As the primary physiological inhibitor of plasmin, SERPINF2 binds irreversibly to plasmin, neutralizing its enzymatic activity and maintaining a balance between clot formation and dissolution. This glycoprotein is synthesized primarily in the liver and circulates in plasma, with a portion cross-linked to fibrin clots during coagulation to provide localized inhibition of fibrinolysis.

Recombinant SERPINF2 protein is produced using biotechnological platforms such as mammalian cell expression systems (e.g., CHO or HEK293 cells) to ensure proper post-translational modifications, particularly glycosylation, which is essential for its stability and functional activity. Researchers utilize recombinant SERPINF2 to study fibrinolysis dysregulation in conditions like bleeding disorders (e.g., congenital α2AP deficiency), thrombotic diseases, or trauma-associated coagulopathy. Its therapeutic potential is being explored for managing hemorrhagic complications or enhancing clot stability in hemophilia patients.

Recent studies also investigate SERPINF2's non-hemostatic roles, including its involvement in tissue remodeling, angiogenesis, and tumor progression. Structural analyses of recombinant SERPINF2 help elucidate its reactive center loop mechanism and interactions with plasmin. However, challenges remain in optimizing production yields and maintaining consistent glycosylation patterns for clinical applications. As a regulator at the intersection of coagulation, inflammation, and cellular signaling, recombinant SERPINF2 continues to be a valuable tool for both basic research and therapeutic development.

**Background of AMBP Recombinant Protein**

The AMBP (Alpha-1-Microglobulin/Bikunin Precursor) protein is a multifunctional glycoprotein encoded by the *AMBP* gene. It serves as the precursor for two distinct bioactive molecules: alpha-1-microglobulin (A1M) and bikunin, which are released through proteolytic cleavage. A1M, a 26 kDa protein, exhibits antioxidant, immunomodulatory, and heme-binding properties, playing roles in mitigating oxidative stress and inflammation. Bikunin, a 25 kDa glycosaminoglycan-linked protein, functions as a protease inhibitor, primarily inhibiting enzymes like plasmin and kallikrein, and is critical for extracellular matrix stability through its role in hyaluronan synthesis.

The AMBP protein is synthesized in the liver and secreted into the bloodstream, where its cleavage products contribute to systemic homeostasis. A1M is found in plasma and tissues, while bikunin circulates as part of the inter-α-inhibitor (IαI) family, essential for inflammation regulation and cellular migration. Dysregulation of AMBP-derived proteins has been linked to pathologies such as chronic kidney disease, preeclampsia, and cancer.

Recombinant AMBP proteins are produced using biotechnological platforms (e.g., *E. coli*, mammalian cells) to study their structural and functional properties. These engineered proteins retain biological activity, enabling research into their therapeutic potential. For example, recombinant A1M is explored for treating oxidative stress-related disorders, while bikunin-based therapies target inflammatory diseases and metastasis inhibition.

The development of AMBP recombinant proteins highlights their dual role as both biomarkers and therapeutic candidates, bridging insights into fundamental biology and clinical applications. Advances in protein engineering continue to enhance their stability and efficacy, driving preclinical and clinical investigations in diverse disease contexts.