CD177 Antibody - #DF2293

In association with beta-2 integrin heterodimer ITGAM/CD11b and ITGB2/CD18, mediates activation of TNF-alpha primed neutrophils including degranulation and superoxide production. In addition, by preventing beta-2 integrin internalization and attenuating chemokine signaling favors adhesion over migration. Heterophilic interaction with PECAM1 on endothelial cells plays a role in neutrophil transendothelial migration in vitro. However, appears to be dispensable for neutrophil recruitment caused by bacterial infection in vivo. Acts as a receptor for the mature form of protease PRTN3 allowing its display at the cell surface of neutrophils. By displaying PRTN3 at the neutrophil cell surface, may play a role in enhancing endothelial cell junctional integrity and thus vascular integrity during neutrophil diapedesis.

N-glycosylated.

A soluble form may also be produced by proteolytic cleavage at the cell surface (shedding).

Cell membrane>Lipid-anchor. Membrane raft>Lipid-anchor. Secreted. Cytoplasmic granule membrane. Cell projection>Lamellipodium.
Note: Cell surface expression on neutrophils is increased upon TNF-alpha, fMLP or CXCL8/IL8-mediated stimulation (PubMed:17244676, PubMed:17580308). In neutrophils, stored predominantly in secondary and tertiary granules (PubMed:18462208). Can also be shedded from the cell membrane (PubMed:12239154, PubMed:18462208). Localizes to lamellar protrusions in spreading neutrophils (PubMed:28807980).

Highly expressed in normal bone marrow and weakly expressed in fetal liver. During neutrophil differentiation, expression begins at the metamyelocyte stage and continues throughout the subsequent stages (at protein level). Expressed by a subset of mature neutrophils (at protein level). The percentage of neutrophils expressing CD177 varies across the population. Expressed in granulocytes of patients with polycythemia vera (PV) and with essential thrombocythemia (ET).

Found in a complex with integrin ITGAM/CD11b and ITGB2/CD18. Interacts with PECAM1 (via Ig-like C2-type domain 6); the interaction is Ca(2+)-dependent; the interaction is direct. Interacts with serine protease PRTN3/myeloblastin; the interaction tethers PRTN3 to the cell surface; the interaction is direct.