Serpin F1, also known as pigment epithelium derived factor (PEDF), is a member of the serpin family. However, Serpin F1 does not display the serine protease inhibitory activity as shown by many of its family members. Similar to other serpin family members, it is composed of three beta-sheets, 8 - 10 alpha-helixes, and a C-terminal reactive center loop. The function of these proteins is controlled by structural constraints of the serpin molecule that allow them to modulate processes controlling proteolytic cascades such as fibrinolysis, coagulation, and complement activation. Serpin F1 has been shown to possess anti-angiogenic and neurotrophic activities. The anti-angiogenic activty of Serpin F1 was mapped to amino acids 20 - 70 along with Ser114 and Ser277, while the neurotrophic activity of the protein was mapped to amino acids 32 - 141. Additionally, Serpin F1 serves as the chaperone and circulating transporter. In the past decade, researchers has identified Serpin F1 as a key prognostic marker in the development and progression of several tumors such as breast, lung, prostate, glioma, and pancreatic carcinoma. It appears that the decreased intra-tumoral expression of Serpin F1 is associated with a higher microvessel density, a more metastatic phenotype, and poor clinical outcome of tumors. Recently, it was shown that Serpin F1 secreted by retinal pigmented epithelial cells could support the survival of retinal progenitor cells, which indicate that this protein may play a role in stem cell biology. The mature form of the Human Serpin F1 shares 86% of its sequence with its murine counterpart.
Size
100 μg
Concentration
n/a
Applications
BA
Other Names
Serpin peptidase inhibitor, clade F (alpha-2 antiplasmin, pigment epithelium derived factor), member 1, PEDF, OI6, OI12, EPC-1, PIG35