HEK293 cells.
PIGF, PGF, PLGF-1.
Sterile Filtered colorless solution.
Greater than 90.0% as determined by SDS-PAGE.
PLGF1 Human Recombinant produced in HEK293 cells is a single, glycosylated polypeptide chain (a.a 19-149) containing 137 amino acids and having a molecular mass of 15.5kDa. PLGF1 is fused to a 6 amino acid His tag at C-terminus and purified by proprietary chromatographic techniques.
PIGF, PGF, PLGF-1.
HEK293 cells.
LPAVPPQQWA LSAGNGSSEV EVVPFQEVWG RSYCRALERL VDVVSEYPSE VEHMFSPSCV SLLRCTGCCG DENLHCVPVE TANVTMQLLK IRSGDRPSYV ELTFSQHVRC ECRPLREKMK PERCGDAVPR RHHHHHH.
Placental Growth Factor-1 (PLGF-1) is a member of the vascular endothelial growth factor (VEGF) family, which plays a crucial role in angiogenesis and vascular development. The human recombinant form of PLGF-1, produced in HEK293 cells, is a valuable tool for studying the molecular mechanisms of angiogenic signaling and exploring its potential therapeutic applications.
PLGF-1 is a homodimeric glycoprotein with a distinctive structural configuration essential for its interactions with VEGF receptors. The human recombinant form allows for controlled exploration of the three-dimensional intricacies of PLGF-1, providing insights into its binding affinities and conformational dynamics. Understanding its structure is fundamental for deciphering how PLGF-1 orchestrates angiogenic responses in different physiological and pathological contexts .
The human recombinant PLGF-1 is produced in HEK293 cells, a human embryonic kidney cell line. This production method ensures that the protein is glycosylated, which is important for its biological activity. The recombinant protein is typically fused to a 6 amino acid His-tag at the C-terminus and purified using proprietary chromatographic techniques .
PLGF-1 primarily functions by inducing angiogenesis through its binding to VEGF receptors on endothelial cells. This interaction triggers a cascade of signaling pathways that promote the formation of new blood vessels. The biological activity of PLGF-1 is measured by its binding ability in a functional ELISA with Human VEGFR1/Flt-1 .
The recombinant form of PLGF-1 is widely used in research to dissect the molecular intricacies of angiogenic signaling. It has significant implications in both physiological vascular development and pathological conditions such as cancer. By studying PLGF-1, scientists aim to deepen their understanding of angiogenesis and develop innovative strategies for vascular-targeted therapies .