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For reconstitution, add sterile, distilled water to achieve a final antibody concentration of 1 mg/mL. Gently shake to solubilize the protein completely. Do not vortex. Reconstituted products should be stored at -80 °.
ANG-2 binds to the endothelial cell receptor Tie-2 but, unlike ANG-1, does not trigger tyrosine phosphorylation. Instead, it regulates ANG-1-mediated Tie-2 activation and can act as either an agonist or antagonist of angiogenesis, depending on the biological context. Together with ANG-1, and the less well-characterized ANG-3 and ANG-4, these interactions are essential for blood vessel formation in both embryos and adults. ANG-1 and ANG-2 play key roles in vessel sprouting, tube formation, and maintaining the stability of newly formed vessels. Mature human ANG-2 is a secreted 480-amino acid protein composed of an N-terminal coiled-coil domain rich in alpha helices and a C-terminal fibrinogen-like domain. It primarily exists as a disulfide-linked dimer.
VEGF (vascular endothelial growth factor) is a 45 kDa homodimeric, disulfide-linked glycoprotein that is central to angiogenesis and promotes tumor growth and metastasis. It supports endothelial cell survival, proliferation, migration, and increases vascular permeability. The VEGF family includes VEGF-A, -B, -C, -D, -E, and PlGF. VEGF signaling through its tyrosine kinase receptors VEGFR-1 (FLT-1) and VEGFR-2 (FLK-1/KDR), expressed mainly on endothelial cells, is a fundamental regulator of angiogenesis and embryonic vascular development. Five VEGF isoforms arise from alternative splicing of a single gene. An alternatively spliced form of FLT-1 produces a soluble receptor (sFLT1) that binds VEGF with high affinity and inhibits angiogenesis. Elevated VEGF levels are associated with POEMS syndrome (Crow-Fukase syndrome), a multisystem disorder.
仅用于科研。不用于诊断过程。未经明确授权不得转售。