Growth Factors
Product List
VEGF C Human
Vascular Endothelial Growth Factor C Human Recombinant
Recombinant Human VEGF-C encompasses 121 amino acid residues, including a C-terminally fused 6-amino acid His-tag. Glycosylation results in an observed molecular weight of 18-24 kDa for VEGF-C under reducing conditions in SDS-PAGE analysis.
VEGF C Rat
Vascular Endothelial Growth Factor Related Protein Rat Recombinant
VEGF C Rat (152 a.a.)
Vascular Endothelial Growth Factor-C (152 a.a) Rat Recombinant
VEGF D Human
Vascular Endothelial Growth Factor D Human Recombinant
VEGF E (Orf Virus)
Vascular Endothelial Growth Factor-E Recombinant (Orf Virus)
VEGF Mouse, Sf9
Vascular Endothelial Growth Factor Mouse Recombinant, Sf9
VEGF Mouse, Yeast
Vascular Endothelial Growth Factor Mouse Recombinant, Yeast
This recombinant Vascular Endothelial Growth Factor protein is produced in yeast and designed to mimic the native mouse protein. It exists as a disulfide-linked homodimer, meaning it comprises two identical polypeptide chains linked by a disulfide bond. Each chain consists of 165 amino acids, resulting in a molecular mass of approximately 40.0kDa per chain. The total molecular weight of the dimer is therefore around 80.0 kDa. The protein is purified using proprietary chromatographic techniques to ensure its quality and purity.
Saccharomyces cerevisiae
Sterile Filtered White lyophilized (freeze-dried) powder.
VEGF Human, Plant
Vascular Endothelial Growth Factor Human Recombinant, Plant
Recombinant Human Vascular Endothelial Growth Factor, produced in Oryza Sativa (rice), has a molecular weight of 19.2kDa. The purification of VEGF is achieved through proprietary chromatographic methods.
Rice Grain
VEGF Human, Yeast
Vascular Endothelial Growth Factor Human Recombinant, Yeast
VEGF Mouse
Vascular Endothelial Growth Factor Mouse Recombinant
Recombinant Mouse Vascular Endothelial Growth Factor, produced in E. coli, is a homodimeric protein with a disulfide bond. Each polypeptide chain consists of 165 amino acids, resulting in a molecular mass of 38.8 kDa for the dimer.
Introduction
Vascular Endothelial Growth Factor (VEGF) is a signal protein produced by many cells that stimulates the formation of blood vessels. It is a sub-family of growth factors, specifically the platelet-derived growth factor family of cystine-knot growth factors . The VEGF family in mammals comprises five members: VEGF-A, VEGF-B, VEGF-C, VEGF-D, and Placenta Growth Factor (PGF) . Additionally, VEGF-related proteins encoded by viruses (VEGF-E) and in the venom of some snakes (VEGF-F) have also been discovered .
VEGF proteins are crucial signaling molecules involved in vasculogenesis (the formation of the embryonic circulatory system) and angiogenesis (the growth of blood vessels from pre-existing vasculature) . They are expressed in various tissues, particularly in vascularized tissues . VEGF is also involved in the formation of new blood vessels during embryonic development, after injury, and in muscles following exercise . The expression of VEGF is regulated by factors such as oxygen tension, cytokines, and differentiation .
The primary function of VEGF is to promote the growth of new blood vessels. It plays a critical role in embryonic development, wound healing, and the formation of collateral circulation to bypass blocked vessels . VEGF is also involved in immune responses by being chemotactic for granulocytes and macrophages . It contributes to pathological conditions such as tumor growth and metastasis, as well as vascular diseases in the retina .
VEGF exerts its effects by binding to tyrosine kinase receptors (VEGFRs) on the cell surface, leading to receptor dimerization and activation through transphosphorylation . The primary receptors for VEGF are VEGFR-1 (Flt-1) and VEGFR-2 (KDR/Flk-1) . These receptors activate downstream signaling cascades that promote endothelial cell proliferation, migration, and survival . VEGF also interacts with co-receptors such as neuropilins, which modulate its activity .
The expression and activity of VEGF are tightly regulated at multiple levels. Transcriptional regulation is influenced by oxygen levels, with hypoxia being a major inducer of VEGF gene transcription . Other regulatory factors include growth factors, hormones, and oncogenes . Post-translational modifications, such as phosphorylation, also play a role in modulating VEGF activity . Additionally, VEGF signaling is regulated by the availability of its receptors and the presence of co-receptors .
VEGF has significant applications in biomedical research, diagnostics, and therapeutics. In research, recombinant VEGF proteins are used to study angiogenesis and related signaling pathways . Clinically, VEGF inhibitors such as bevacizumab (Avastin) are used to treat cancers by inhibiting tumor angiogenesis . VEGF is also targeted in therapies for age-related macular degeneration and diabetic retinopathy . Diagnostic tools measuring VEGF levels can help in assessing disease progression and treatment efficacy .
VEGF plays a vital role throughout the life cycle, from development to aging and disease. During embryogenesis, VEGF is essential for the formation of the vascular system . In adults, it is involved in physiological processes such as wound healing, menstrual cycles, and pregnancy . VEGF also contributes to pathological conditions, including cancer, retinopathy, and inflammatory diseases . Its role in promoting angiogenesis makes it a critical factor in both normal physiology and disease states .
