Extracellular plasminogen activator inhibitor type-2 (also known as PAI-2, Placental plasminogen activator inhibitor; Monocyte Arg-serpin; Urokinase inhibitor; SERPINB2 serpin peptidase inhibitor, clade B (ovalbumin), member 2) is a coagulation factor and a potent inhibitor of urokinase-type plasminogen activator (u-PA) and also acts as a multifunctional protein. It is present in most cells, especially monocytes and macrophages. PAI-2 exists in two forms, a 60-kDa, secreted, extracellular, glycosylated form and a 43-kDa intracellular form. It is a multifunctional protein that plays a role in cell differentiation, in prevention of programmed cell death, in the regulation of cell proliferation, in the inhibition of microbial proteinases and in the protection against stromal degradation. High levels of the PAI-2 protein are associated with a good prognosis in breast cancer, small cell lung, ovarian cancer, and inhibition of metastasis. PAI-2 also plays a role in inflammation on the surface of the eye. PAI-2 may cooperate with pRb2/p130 in modulating PAI-2 gene expression by chromatin remodeling.
PAI-2, Placental plasminogen activator inhibitor; Monocyte Arg-serpin; Urokinase inhibitor; SERPINB2 serpin peptidase inhibitor, clade B (ovalbumin), member 2
This affinity purified antibody was prepared from whole rabbit serum produced by repeated immunizations with a peptide corresponding to an internal area of human PAI-2 protein.