Recombinant Human ADAMTS16 protein

ADAMTS16 (A Disintegrin and Metalloproteinase with Thrombospondin Motifs 16) is a member of the ADAMTS family of extracellular proteases, known for their roles in extracellular matrix (ECM) remodeling, tissue development, and disease processes. This multidomain enzyme contains a conserved catalytic metalloproteinase domain, a disintegrin-like module, a thrombospondin type-1 repeat (TSR) domain, and a unique C-terminal ancillary domain that mediates substrate recognition and cellular interactions. Unlike some well-characterized ADAMTS members (e.g., ADAMTS13 or ADAMTS5), ADAMTS16 remains understudied, though emerging evidence links it to organogenesis, cancer, and cardiovascular and reproductive disorders.

Recombinant ADAMTS16 protein is typically produced in mammalian or insect expression systems to ensure proper post-translational modifications, such as glycosylation, which are critical for its structural stability and enzymatic activity. The purified protein enables functional studies to elucidate its substrate specificity, proteolytic mechanisms, and regulatory pathways. Known substrates include ECM components like proteoglycans, though its full range of biological targets is still being explored. Research suggests ADAMTS16 may modulate TGF-β signaling and influence cell adhesion/migration, implicating it in fibrosis, tumor metastasis, and vascular remodeling. Dysregulation of ADAMTS16 has been observed in cancers (e.g., breast, prostate) and polycystic ovarian syndrome, highlighting its potential as a therapeutic target or biomarker. However, its precise physiological and pathological roles require further investigation. Recombinant ADAMTS16 tools (e.g., active enzymes, mutants, or inhibitory antibodies) are vital for dissecting its contributions to tissue homeostasis and disease, bridging gaps between genetic associations and mechanistic understanding.