PLGF Protein, Human

The PLGF-2 protein is a key growth factor for angiogenesis and endothelial cell growth, crucially stimulating cell proliferation and migration by binding to the FLT1/VEGFR-1 receptor. It coordinates the angiogenic process, regulates blood vessel growth, and exhibits additional binding capabilities to NRP1/neuropilin-1 and NRP2/neuropilin-2. PLGF Protein, Human is the recombinant human-derived PLGF protein, expressed by E. coli , with tag free. The total length of PLGF Protein, Human is 131 a.a., with molecular weight of ~14.9 kDa.

The PLGF-2 Protein, a growth factor with significant activity in angiogenesis and endothelial cell growth, plays a crucial role in stimulating the proliferation and migration of these cells. Through binding to the FLT1/VEGFR-1 receptor, PLGF-2 orchestrates angiogenic processes and contributes to the regulation of vascular growth. Notably, the isoform PlGF-2 exhibits additional binding capabilities, forming interactions with NRP1/neuropilin-1 and NRP2/neuropilin-2 in a heparin-dependent manner. Beyond its angiogenic functions, PLGF-2 also promotes tumor growth, implicating its involvement in pathological angiogenesis associated with cancer. Structurally, PLGF-2 exists as an antiparallel homodimer linked by disulfide bonds, and it can further manifest as a heterodimer with VEGFA/VEGF. The presence of isoform PlGF-3 as both a homodimer and monomer adds to the complexity of PLGF proteins, highlighting their diverse roles in modulating vascular processes and tumorigenesis.

Human

E. coli

Tag Free

P49763-2 (L19-R149)

5228  [NCBI]

Approximately 14.9 kDa

Greater than 90% as determined by reducing SDS-PAGE.

<1 EU/μg, determined by LAL method.