|VEGF R1/Flt‑1 in Human Breast. VEGF R1/Flt‑1 was detected in immersion fixed paraffin-embedded sections of human breast array using Human VEGF R1/Flt‑1 Biotinylated Antigen Affinity-purified Polyclonal Antibody (Catalog # BAF321) at 15 µg/mL overnight at 4 °C. Tissue was stained using the Anti-Goat HRP-DAB Cell & Tissue Staining Kit (brown; Catalog # CTS008) and counterstained with hematoxylin (blue). Lower panel shows a lack of labeling if primary antibodies are omitted and tissue is stained only with secondary antibody followed by incubation with detection reagents. View our protocol for Chromogenic IHC Staining of Paraffin-embedded Tissue Sections.|
VEGF R1 is one of the five receptor tyrosine kinases (RTKs) (Flt-1, KDR/Flk-1, Flt-4, tie-1, and tek/tie-2) whose expression is almost exclusively restricted to the endothelial cells. Tie-1 and tek/tie-2 define a new class of RTKs containing two immunoglobulin-like domains, three EGF homology domains and three fibronectin type III domains in their extracellular regions. Flt-1, KDR/Flk-1 and Flt-4 are members of the class III subfamily of RTKs containing seven immunoglobulin-like repeats in their extracellular domains. All five RTKs are likely to play central roles in vasculogenesis and angiogenesis.
The Flt-1 gene has been localized to chromosome 13q12. Full length Flt-1 mRNA encodes a 1338 amino acid (aa) residue precursor with a 22 aa residue signal peptide. Mature Flt-1 is composed of a 736 aa residue extracellular domain, a 22 aa residue transmembrane domain and a 558 aa residue cytoplasmic domain. As a result of alternative splicing of the mRNA, a cDNA encoding a truncated form of Flt-1, lacking the seventh immunoglobulin-like domain, the transmembrane and intracellular domains, has been cloned.
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