Recombinant Human PLVAP protein

PLVAP (Plasmalemma Vesicle-Associated Protein), also known as PV1. is a transmembrane glycoprotein predominantly expressed in endothelial cells, where it plays a critical role in maintaining vascular and lymphatic barrier functions. It is a key structural component of endothelial caveolae, fenestrae, and transendothelial channels, regulating selective permeability and molecular transport across blood vessels. PLVAP forms diaphragms at the openings of these structures, acting as a size-selective filter to control the passage of plasma proteins, immune cells, and solutes. Its expression is tightly linked to vascular development, angiogenesis, and inflammatory responses.

Recombinant PLVAP protein is engineered for research and therapeutic applications, typically produced using mammalian or insect cell systems to ensure proper post-translational modifications, such as glycosylation. This protein serves as a vital tool for studying endothelial biology, vascular permeability disorders, and pathological conditions like cancer metastasis, where PLVAP overexpression correlates with tumor angiogenesis and immune evasion. Researchers utilize recombinant PLVAP to investigate its interactions with ligands, its role in leukocyte trafficking, and its potential as a biomarker or therapeutic target. Additionally, it aids in developing antibodies for diagnostic assays and exploring strategies to modulate vascular leakage in conditions like sepsis or edema. Dysregulation of PLVAP has been implicated in diseases such as diabetic retinopathy and pulmonary hypertension, underscoring its biomedical relevance. The recombinant form enables mechanistic studies and drug screening to advance therapies targeting endothelial dysfunction.