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VEGF produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 171 amino acids (27-191 a.a.) and having a molecular mass of 19.9 kDa.
VEGF is expressed with a 6 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.
APMAEGGGQN HHEVVKFMDV YQRSYCHPIE TLVDIFQEYP DEIEYIFKPS CVPLMRCGGC CNDEGLECVP TEESNITMQI MRIKPHQGQH IGEMSFLQHN KCECRPKKDR ARQENPCGPC SERRKHLFVQ DPQTCKCSCK NTDSRCKARQ LELNERTCRC DKPRRHHHHH H.
The VEGF family consists of several proteins, including VEGF-A, VEGF-B, VEGF-C, VEGF-D, and Placental Growth Factor (PlGF). Among these, VEGF-A is the most studied and is often referred to simply as VEGF. VEGF-A binds to two primary receptors, VEGFR-1 (Flt-1) and VEGFR-2 (KDR/Flk-1), which mediate its angiogenic effects .
Human recombinant VEGF is produced using various expression systems, including Escherichia coli, yeast, and baculovirus-infected insect cells. The baculovirus expression system is particularly advantageous for producing complex proteins with post-translational modifications similar to those in mammalian cells .
The baculovirus expression system utilizes insect cells, such as Sf9 or Sf21, to produce recombinant proteins. This system is highly efficient and capable of producing large quantities of protein. The recombinant human VEGF produced in this system is often tagged with a histidine tag to facilitate purification using nickel affinity chromatography .
VEGF is a key player in promoting angiogenesis and vascular permeability. It is extensively studied for its role in cancer, where it promotes tumor growth and metastasis by enhancing blood supply to the tumor. Anti-VEGF therapies, such as monoclonal antibodies and small molecule inhibitors, are used in the treatment of various cancers and other diseases characterized by abnormal angiogenesis .