Anti-Human VEGFR2 (Ramucirumab) - Fc Muted™

VEGFR-2 is widely expressed by vascular endothelial cells, some vascular tumors, carcinomas, malignant melanomas, and lymphomas. Certain leukemia cells express functional VEGFR on the cell surface.

? 5.0 mg/ml

Purified No Carrier Protein

This biosimilar antibody is aseptically packaged and formulated in 0.01 M phosphate buffered saline (150 mM NaCl) PBS pH 7.2 - 7.4 with no carrier protein, potassium, calcium or preservatives added. Due to inherent biochemical properties of antibodies, certain products may be prone to precipitation over time. Precipitation may be removed by aseptic centrifugation and/or filtration.

This biosimilar antibody is aseptically packaged and formulated in 0.01 M phosphate buffered saline (150 mM NaCl) PBS pH 7.2 - 7.4 with no carrier protein, potassium, calcium or preservatives added. Due to inherent biochemical properties of antibodies, certain products may be prone to precipitation over time. Precipitation may be removed by aseptic centrifugation and/or filtration.

Human VEGFR2

Vascular endothelial growth factors (VEGF) and VEGF receptors (VEGFR) play an essential role in angiogenesis1. There are three VEGFRs: VEGFR-1, VEGFR-2, and VEGFR-3. VEGFR- 1 and VEGFR-2 are responsible for angiogenesis, and VEGFR-3 affects lymphogenesis. In the pathogenesis of diseases including diabetes mellitus, rheumatoid arthritis, and cancer, new blood vessel formation is highjacked. Changes at the VEGF/VEGFR-2 axis are particularly potent at allowing VEGF-induced proliferation, migration, and vascular endothelial cell differentiation during tumor angiogenesis. Additionally, VEGFR-2 is upregulated in tumor vascular endothelial cells, and VEGF levels are associated with poor prognosis and resistance to chemotherapy. Consequently, the VEGF/VEGFR axis is a prime anti-cancer target. Blocking VEGF/VEGFR-2 with Ramucirumab inhibits tumor growth in animal models and cancer patients2, 3, 4, and Ramucirumab is approved by the US Food and Drug Administration for treatment of various cancers5. Ramucirumab blocks all known VEGFs from binding to VEGFR-24, 6. Ramucirumab specifically and potently inhibits VEGFR-2 by binding to the VEGF-binding domain at an epitope located within VEGFR-2 extracellular Ig domain 37. Ramucirumab inhibits VEGF/VEGF-2 interaction 1 , VEGFR-2 phosphorylation7, VEGF-induced VEGFR-2 activation1, VEGF-stimulated cellular migration6 and proliferation1 , and prolongs the survival of leukemia-inoculated mice6. Ramucirumab (IMC-1121B) was fully humanized from chimeric antibody IMC-11211, which was constructed from a Fab fragment (Hu-1121 Fab) isolated by immunopanning against VEGFR-2 under stringent conditions using a VL-shuffled library and the VH gene segment Hu- 2C6 Fab6, 7. The original library was constructed from spleen cells of mice immunized with a soluble form of VEGFR-28. Ramucirumab was converted into a full length bivalent IgG1 antibody from the Fab fragment 11217. Ramucirumab, clone IMC-1121B, a non-therapeutic biosimilar antibody for research use only was developed recombinantly and has the same variable regions as the original therapeutic.

3791

?95% by SDS Page

VEGFR2