PRTN3
PRTN3 (proteinase 3, also known as myeloblastin, PR-3, ACPA, C-ANCA, AGP7, MBT and P29) is a serine protease of the elastase subfamily. It degrades extracellular matrix proteins and contributes to neutrophil behaviour during inflammation. Browse Assay Genie's current range of PRTN3 research reagents below, or read on for the biology behind the target.
PRTN3 is a serine protease that, in vitro, degrades elastin, fibronectin, laminin, vitronectin and collagen types I, III and IV. It also acts as a signalling modulator. By cleaving and activating the receptor F2RL1 (PAR-2), it enhances endothelial cell barrier function and so supports vascular integrity during neutrophil transendothelial migration. It is thought to play a role in this migration, probably in association with CD177, and it triggers inflammatory processes in neutrophils by interacting with ADGRG3 upstream of PAR-2 activation.
The PRTN3 gene encodes a member of the peptidase S1 family, elastase subfamily. HGNC places it in the group of granule-associated serine proteases of immune defence, alongside other elastases. UniProt records the protein in cytoplasmic granules, in secreted form, at the cell membrane and in membrane rafts. NCBI Gene describes it as located in the azurophil granule lumen, cytosol and plasma membrane raft. It is annotated with enzyme binding, serine-type endopeptidase and signalling receptor binding activities.
NCBI Gene links PRTN3 to several processes, including neutrophil extravasation, mature conventional dendritic cell differentiation and positive regulation of GTPase activity. The alias myeloblastin is the UniProt protein name, while C-ANCA and ACPA are among the other names listed for the gene. Researchers studying PRTN3 often work with the mouse ortholog, Prtn3, to examine its function in neutrophil biology and inflammation.
PRTN3 is implicated in neutrophil transendothelial migration, probably with CD177, and helps preserve endothelial barrier function during this process.
PRTN3 triggers inflammatory processes in neutrophils through ADGRG3 upstream of F2RL1/PAR-2 activation.
PRTN3 degrades elastin, fibronectin, laminin, vitronectin and several collagens in vitro, making it relevant to matrix remodelling.
PRTN3 cleaves and activates PAR-2 (F2RL1), offering a model for protease-driven receptor signalling in vascular biology.
PRTN3 is a serine protease that degrades extracellular matrix proteins in vitro, including elastin, fibronectin, laminin and collagens. It also cleaves and activates PAR-2 (F2RL1), which enhances endothelial barrier function and vascular integrity during neutrophil transendothelial migration.
PRTN3 is the HGNC symbol for proteinase 3. Other names include myeloblastin, PR-3, ACPA, C-ANCA, AGP7, MBT and P29. The enzyme carries the EC number 3.4.21.76 and belongs to the elastase subfamily of the peptidase S1 family.
A mouse ortholog, Prtn3, is recorded for the human PRTN3 gene, so mouse models can be used to study its function. No rat ortholog is given in the data supplied. Check the datasheet of any product for its validated reactivity.
Other granule serine proteases, receptor partners and neutrophil markers connected to PRTN3 biology.
Gene and protein annotations from HGNC, NCBI Gene and UniProt P24158; product specifications from Assay Genie datasheets.