Rat Neuropilin-1 Alexa Fluor® 700-conjugated Antibody Summary
Met1-Asp854 (Lys811Arg, Pro812-Gly828 del), predicted
Accession # Q9QWJ9
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Neuropilin-1 (Npn-1, previously neuropilin; also CD304) is a 130‑140 kDa type I transmembrane (TM) glycoprotein that regulates axon guidance and angiogenesis (1‑4). The mature 901 amino acid (aa) rat Npn-1 contains a 623 aa extracellular domain (ECD) that shares 98% aa identity with mouse and 93% aa identity with human, equine, bovine and canine Npn-1 (3, 4). The ECD contains two N-terminal CUB domains, two F5/8 type C domains with homology to coagulation factors V and VIII and a MAM (meprin) domain. In mouse and human, splice variants that lack the TM domain have been described and are either proven or presumed to be soluble antagonists (1, 5‑7). The sema domains of Class III secreted semaphorins such as Sema3A bind Npn-1 CUB domains (8). The heparin-binding forms of VEGF (VEGF165, VEGF-B and VEGF-E), PlGF (PlGF2), and the C-terminus of Sema3 bind the F5/8 type C domains (8, 9). Npn-1 and Npn-2 share 48% aa identity within the ECD and can form homo- and hetero-oligomers via interaction of their MAM domains (1). Neuropilins show partially overlapping expression in neuronal and endothelial cells during development (1, 2). Both neuropilins act as co-receptors with plexins, mainly plexin A3 and A4, to bind class III semaphorins that mediate axon repulsion (10). However, only Npn-1 binds Sema3A, and only Npn-2 binds Sema3F (1). Both are co-receptors with VEGF R2 (also called KDR or Flk-1) for VEGF165 binding (1). Sema3A signaling can be blocked by VEGF165, which has higher affinity for Npn-1 (11). Npn-1 is preferentially expressed in developing or remodeling arteries (1, 2). Npn-1 is also expressed on dendritic cells and mediates DC-induced T cell proliferation (12).
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Product Specific Notices
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