PEDF Human, His

Pigment Epithelium-Derived Factor (PEDF), also known as serpin F1 (SERPINF1), is a multifunctional secreted protein with significant roles in anti-angiogenic, anti-tumorigenic, and neurotrophic functions . This protein has garnered attention for its potential therapeutic applications in conditions such as choroidal neovascularization, heart disease, and cancer .

PEDF was first discovered by Joyce Tombran-Tink and Lincoln Johnson in the late 1980s while studying human retinal cell development . The protein is encoded by the SERPINF1 gene located on chromosome 17 in humans . PEDF belongs to the serine protease inhibitors (serpin) superfamily, although it is a non-inhibitory member .

PEDF is a potent inhibitor of angiogenesis, the process of forming new blood vessels, which is crucial in limiting tumor growth and progression . It achieves this by binding to vascular endothelial growth factor receptors (VEGFR-1 and VEGFR-2), promoting their internalization and/or degradation, thereby inhibiting endothelial cell proliferation and migration . Additionally, PEDF induces apoptosis in endothelial cells through various pathways .

Recombinant PEDF is produced using human cells and is often tagged with a 6x-His tag for purification purposes . This recombinant form retains the biological activity of the native protein, making it valuable for research and therapeutic applications . The His tag facilitates easy purification and detection of the protein in experimental settings.

Research on PEDF has shown its potential in treating diseases characterized by abnormal blood vessel growth, such as diabetic retinopathy and certain cancers . Its neurotrophic properties also make it a candidate for neurodegenerative disease therapies . Ongoing studies aim to further elucidate its mechanisms and optimize its therapeutic use.