Anti-LRRC32 Purified Monoclonal Antibody

GARP (glycoprotein A repetitions predominant protein), also known as garpin or LRRC32 (leucin-rich repeat containing protein 32) is an approximately 80 kDa transmembrane glycoprotein detected on the surface of megakaryocytes, platelets, and activated Treg cells. It binds to the latency-associated peptide (LAP) domain of pro-TGF beta and regulates its storage and activation. The expression of GARP on Treg cells seems to be necessary for their suppressive functions.

Purified human sGARP protein. The mouse monoclonal antibody GARP5 recognizes GARP / LRRC32, an approximately 80 kDa glycoprotein expressed e.g. on the surface of megakaryocytes, platelets and activated Treg cells.

Key regulator of transforming growth factor beta (TGFB1, TGFB2 and TGFB3) that controls TGF-beta activation by maintaining it in a latent state during storage in extracellular space (PubMed:19750484, PubMed:19651619, PubMed:22278742) . Associates specifically via disulfide bonds with the Latency-associated peptide (LAP), which is the regulatory chain of TGF-beta, and regulates integrin-dependent activation of TGF-beta (PubMed:22278742) . Able to outcompete LTBP1 for binding to LAP regulatory chain of TGF-beta (PubMed:22278742) . Controls activation of TGF-beta-1 (TGFB1) on the surface of activated regulatory T-cells (Tregs) (PubMed:19750484, PubMed:19651619) . Required for epithelial fusion during palate development by regulating activation of TGF-beta-3 (TGFB3) (By similarity) .