Recombinant Human VPRBP protein

VPRBP (Vascular Permeability Factor Receptor-Binding Protein), also known as RAMP2 (Receptor Activity-Modifying Protein 2), is a chaperone protein critical for regulating the activity of the calcitonin receptor-like receptor (CLR). Discovered in the early 2000s, it plays a pivotal role in modulating vascular and lymphatic functions by forming heterodimeric complexes with CLR. These complexes act as functional receptors for adrenomedullin (AM) and calcitonin gene-related peptide (CGRP), peptides involved in vasodilation, angiogenesis, and inflammation. VPRBP’s interaction with CLR ensures proper receptor trafficking, ligand specificity, and downstream signaling, impacting blood pressure homeostasis and vascular permeability.

Recombinant VPRBP protein is engineered using expression systems (e.g., E. coli, mammalian cells) to produce purified, bioactive forms for research and therapeutic applications. Its recombinant version retains the ability to bind CLR and influence receptor-ligand interactions, making it valuable for studying cardiovascular pathologies, sepsis, or tumor angiogenesis. Recent studies highlight its potential as a therapeutic target in conditions like preeclampsia, where disrupted adrenomedullin signaling contributes to vascular dysfunction. Additionally, recombinant VPRBP aids in structural studies to map binding domains and optimize peptide-based drugs targeting CLR-VPRBP complexes. Despite progress, challenges remain in understanding its tissue-specific regulation and post-translational modifications. Ongoing research focuses on leveraging recombinant VPRBP to develop novel biologics for cardiovascular and inflammatory diseases, underscoring its translational relevance in precision medicine.