Greater than 95.0% as determined by SDS-PAGE.
EG-VEGF Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 86 amino acids and having a molecular mass of 9.7kDa. The EG-VEGF is purified by proprietary chromatographic techniques.
EG-VEGF was first identified as a tissue-specific angiogenic factor with its expression pattern restricted to endocrine glands, including the testis, ovary, adrenal gland, and placenta . The highest expression of EG-VEGF is observed in the testis, particularly in Leydig cells . This factor is involved in promoting proliferation, migration, and fenestration of endothelial cells in these tissues .
EG-VEGF functions by binding to its receptors, Prokineticin Receptor 1 (PK-R1) and Prokineticin Receptor 2 (PK-R2), which are expressed in endothelial cells of endocrine glands . The binding of EG-VEGF to these receptors triggers a cascade of signaling events that lead to endothelial cell proliferation and new blood vessel formation . This process is vital for the transport of hormones and nutrients to and from the endocrine glands .
Human recombinant EG-VEGF is produced through genetic engineering techniques, allowing researchers to study its angiogenic properties and explore its potential therapeutic applications . Recombinant EG-VEGF has been used in various studies to understand its role in normal and pathological angiogenesis, particularly in endocrine-related disorders .
The expression of EG-VEGF has been linked to several clinical conditions. For instance, its expression in Leydig cell tumors suggests a role in tumor angiogenesis and growth . Additionally, EG-VEGF has been studied for its potential therapeutic applications in treating endocrine disorders and promoting tissue regeneration .