Human VEGF-C and VEGF-DSABio is an official partner in distribution of Human Recombinant VEGF-C and VEGF-D products from Vegenics Pty Ltd..
VEGENICS is an emerging leader in the field of angiogenesis focusing on a class of drug targets called Vascular Endothelial Growth Factors (VEGFs). Vegenics owns the world’s largest and most comprehensive intellectual property estate covering the key angiogenesis targets VEGF-C, VEGF-D and VEGFR-3. The products are intended for research use only. For enquiries and quotations, please contact us at orders@sabio.com.sg . We deliver in Singapore within 24 hours free of charge. |
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About VEGF-C
VEGF-C is a member of the VEGF family of secreted glycoprotein that are critical mediators of angiogenesis and lymphangiogenesis1,2. The VEGFs bind to VEGFR-1 (Flt-1), VEGFR-2 (KDR/Flk-1) and VEGFR-3 (Flt-4), a family of structurally related receptor tyrosine kinases that are predominantly expressed on the endothelial cells of blood and/or lymphatic vessels1. The VEGFs have distinct receptor binding specificities which contribute to their diversity of function. VEGF-C was first described in 1996 by Vegenics collaborators in the Laboratory of Prof. Kari Alitalo3. VEGF-C is synthesised as an immature protein consisting of the receptor binding domain (VEGF homology domain, VHD) flanked by amino and carboxyl-terminal propetides3. During secretion, the immature protein undergoes proteolytic processing to remove the propeptides, yielding the mature form of the protein, a VHD homodimer4. As a consequence of processing the affinity of the mature form of VEGF-C for its receptors is substantially increased4. VEGF-C induces angiogenesis via the activation of both VEGFR-2 and VEGFR-3, and lymphangiogenesis via activation of VEGFR-3. VEGF-C stimulates proliferation of endothelial cells in vitro4 and induces angiogenesis in several in vivo models5-7. VEGF-C is essential during embryonic formation of the lymphatic system8, whereas in the adult its expression is down regulated in normal tissues and up regulated in pathological states that require the formation of vascular and/or lymphatatic network, including wound healing and tumor growth9,10. Indeed high expression levels of VEGF-C in human colorectal11,12, lung13, breast14, gastric15 and pancreatic16 cancers indicates that increased expression of VEGF-C correlates with greater tumour aggression and a poorer prognosis. References
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About VEGF-D
VEGF-D is a member of the VEGF family of secreted glycoproteins that are critical mediators of angiogenesis and lymphangiogenesis2,3. The VEGFs bind to VEGFR-1 (Flt-1), VEGFR-2 (KDR/Flk-1) and VEGFR-3 (Flt-4), a family of structurally related receptor tyrosine kinases that are predominantly expressed on the endothelial cells of blood and/or lymphatic vessels2. The VEGFs have distinct receptor binding specificities which contribute to their diversity of function. VEGF-D was first described in the mouse as a c-fos-induced growth factor (FIGF)4 and subsequently identified in the human1. VEGF-D is synthesised as an immature protein consisting of the receptor binding domain (VEGF homology domain, VHD) flanked by amino and carboxyl-terminal propeptides1. Proteolytic processing by serine proteinases including plasmin5 and proprotein convertases6 remove both propeptides to yield the mature form of the protein, a VHD homodimer. As a consequence of processing the affinity of the mature form of VEGF-D for its receptors is substantially increased7. VEGF-D induces angiogenesis via the activation of both VEGFR-2 and VEGFR-3, and lymphangiogenesis via activation of VEGFR-3. VEGFD is expressed in adult lung, heart, muscle and small intestine, and is most abundantly expressed in foetal lungs and skin7,8, where it is thought play a modifying role in lymphangiogenesis during embryonic development. In the cancer setting VEGF-D promotes solid tumor growth and lymph node metastasis9, and is a poor prognostic marker for colorectal10, ovarian11, prostate12, gastric13 and lung14 cancers. In addition VEGF-D has been shown to have a role in the lung disease Lymphangioleiomyomatosis (LAM) and is a marker for evaluating disease severity15,16. References
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