Description
Product Characteristics:
The serine protease inhibitors (serpins) compose a superfamily of proteins with a diverse set of functions, including the control of blood coagulation, complement activation, programmed cell death and development. Serpins are secreted glycoproteins that contain a stretch of peptide that mimics a true substrate for a corresponding serine protease. Protease nexin-1 (PN-1) is a serpin that inactivates several proteases, including thrombin, urokinase, plasminogen activators (PA) and plasmin. It is involved in tissue remodeling, cellular invasiveness, matrix degradation and tumor growth. PN-1 expression is abundant in the nervous system, where it inhibits thrombin, thereby playing a role in neural injury and repair processes. An imbalance between PN-1 and thrombin may be a contributing factor in the pathology of Alzheimera ?s disease.
Subcellular location: Secreted, Extracellular domain
Synonyms: Glia derived nexin, Protease inhibitor 7, GDN, GDN_HUMAN, Glia-derived nexin, P17 antibody Peptidase inhibitor 7, Pi-7, Plasminogen activator inhibitor type 1, member 2, PN-1, PN1, PNI, Protease nexin 1, Protease nexin I, Serpin E2, Serpin peptidase inhibitor, clade E nexin, plasminogen activator inhibitor type 1, member 2, SERPINE 2, Serpine2.
Target Information: This gene encodes a member of the serpin family of proteins, a group of proteins that inhibit serine proteases. Thrombin, urokinase, plasmin and trypsin are among the proteases that this family member can inhibit. This gene is a susceptibility gene for chronic obstructive pulmonary disease and for emphysema. Alternative splicing results in multiple transcript variants. [provided by RefSeq, Aug 2012]