GP5
GP5 (glycoprotein V platelet, also known as CD42d) is a membrane glycoprotein of platelets and a component of the GPIb-V-IX complex. This complex acts as the receptor for von Willebrand factor and supports platelet adhesion at sites of vascular injury. Browse Assay Genie's current range of GP5 research reagents below, or read on for the biology behind the target.
GP5 is one of the surface glycoproteins that make up the GPIb-V-IX system. This complex functions as the receptor for von Willebrand factor (vWF) and mediates vWF-dependent platelet adhesion to blood vessels. The adhesion of platelets to injured vascular surfaces in the arterial circulation is a critical initiating event in haemostasis, which places GP5 and its partners at the start of the platelet response to vessel damage.
The main portion of the receptor is a heterodimer of two polypeptide chains, an alpha chain (GP1BA) and a beta chain (GP1BB), linked by disulfide bonds. The complete receptor complex includes noncovalent association of these alpha and beta subunits with platelet glycoprotein IX (GP9) and GP5. UniProt lists the protein as platelet glycoprotein V and records it as a membrane protein. The human GP5 gene has mouse and rat orthologs, both named Gp5.
HGNC classifies the gene within the CD molecules group, and CD42d is a recognised alias. Its previous HGNC name was glycoprotein V (platelet). Mutations in GP1BA, GP1BB and GP9 have been shown to cause Bernard-Soulier syndrome, a bleeding disorder, which highlights the importance of the wider receptor complex in platelet function. Researchers studying GP5 typically do so in the context of this complex, platelet adhesion and haemostasis.
GP5 is part of the receptor complex that mediates vWF-dependent platelet adhesion to injured vascular surfaces.
Platelet adhesion in the arterial circulation is a critical initiating event in haemostasis, in which the GPIb-V-IX complex participates.
Mutations in GP1BA, GP1BB and GP9 cause Bernard-Soulier syndrome, making the complex relevant to inherited bleeding disorder research.
GP5 associates noncovalently with the GP1BA-GP1BB heterodimer and GP9, offering a route into how the vWF receptor is organised.
GP5 is a component of the GPIb-V-IX complex, which functions as the von Willebrand factor receptor on platelets. The complex mediates vWF-dependent platelet adhesion to blood vessels, a critical initiating event in haemostasis when vascular surfaces are injured in the arterial circulation.
GP5 is the HGNC symbol for glycoprotein V platelet, and UniProt names the protein platelet glycoprotein V. CD42d is a recognised alias, reflecting its place among the CD molecules. The previous HGNC name was glycoprotein V (platelet).
Mouse and rat both have a Gp5 ortholog; check the datasheet of any product for its validated reactivity. Bernard-Soulier syndrome is linked to mutations in GP1BA, GP1BB and GP9, the other subunits of the same receptor complex, rather than to GP5 in the source summary.
Other subunits of the GPIb-V-IX complex and related platelet glycoproteins with products at Assay Genie.
Gene and protein annotations from HGNC, NCBI Gene and UniProt P40197; product specifications from Assay Genie datasheets.