From €116.00 €98.60
VEGF-D is a member of the PDGF/VEGF family of growth factors that promotes angiogenesis and lymphangiogenesis.{52590} VEGF-D exists as a secreted homodimer composed of a central VEGF homology domain containing the receptor binding region that is flanked by N- and C-terminal propeptides, which are proteolytically cleaved by furin and ADAMTS3 or plasmin to generate the mature, active protein.{57018,52591} VEGF-D is produced by macrophages, fibroblasts, smooth muscle cells, and tumor cells and VEGFD expression is dependent on FOS expression and decreased by stimulation with IL-1?.{52592,52593,52594} Binding of VEGF-D to its receptors, VEGFR2 and VEGFR3, which are expressed by endothelial cells, stimulates the survival, migration, and proliferation of endothelial cells and promotes lymphatic and vascular vessel growth and remodeling.{52590} VEGF-D induces proliferation and chemotaxis in KS-IMM cancer cells and stimulates growth and capillary-like structure formation in human umbilical vein endothelial cells (HUVECs).{52593} Vegfd-/- mice, unlike Vegfc-/- mice, are viable and have a functional lymphatic system, indicating that VEGF-D is dispensable for its development.{52595} Tumor VEGF-D levels are increased in patients with epithelial ovarian carcinoma and positively correlated with lymph node metastasis, poor prognosis, and decreased 10-year survival.{52596} Cayman’s VEGF-D (human, recombinant) protein can be used for cell-based assays applications. This protein consists of 120 amino acids and has a calculated molecular weight of 13.6 kDa. By SDS-PAGE, under reducing conditions, the apparent molecular mass of the protein is approximately 20 to 22 kDa due to glycosylation.
Territorial Availability: Available through Bertin Technologies only in France
| Size | 1 mg, 10 µg, 100 µg |
|---|---|
| Shipping | dry ice |
| Molecular weight | |
| Custom code | 3504.00 |
| Formulation | Lyophilized from sterile PBS, pH 7.4 |
| Purity | ≥95% as determined by SDS-PAGE |
| UNSPSC code | 12352204 |
Cayman Chemical’s mission is to help make research possible by supplying scientists worldwide with the basic research tools necessary for advancing human and animal health. Our utmost commitment to healthcare researchers is to offer the highest quality products with an affordable pricing policy.
Our scientists are experts in the synthesis, purification, and characterization of biochemicals ranging from small drug-like heterocycles to complex biolipids, fatty acids, and many others. We are also highly skilled in all aspects of assay and antibody development, protein expression, crystallization, and structure determination.
Over the past thirty years, Cayman developed a deep knowledge base in lipid biochemistry, including research involving the arachidonic acid cascade, inositol phosphates, and cannabinoids. This knowledge enabled the production of reagents of exceptional quality for cancer, oxidative injury, epigenetics, neuroscience, inflammation, metabolism, and many additional lines of research.
Our organic and analytical chemists specialize in the rapid development of manufacturing processes and analytical methods to carry out clinical and commercial GMP-API production. Pre-clinical drug discovery efforts are currently underway in the areas of bone restoration and repair, muscular dystrophy, oncology, and inflammation. A separate group of Ph.D.-level scientists are dedicated to offering Hit-to-Lead Discovery and Profiling Services for epigenetic targets. Our knowledgeable chemists can be contracted to perform complete sample analysis for analytes measured by the majority of our assays. We also offer a wide range of analytical services using LC-MS/MS, HPLC, GC, and many other techniques.
Accreditations
ISO/IEC 17025:2005
ISO Guide 34:2009
Cayman is a leader in the field of emerging drugs of abuse, providing high-purity Schedule I-V Controlled Substances to federally-licensed laboratories and qualified academic research institutions for forensic analyses. We are certified by ACLASS Accreditation Services with dual accreditation to ISO/IEC 17025:2005 and ISO Guide 34:2009.
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