Reactivity | MuSpecies Glossary |
Applications | Bioactivity |
Format | Carrier-Free |
Details of Functionality | Measured by its binding ability in a functional ELISA. Immobilized Recombinant Mouse Neuropilin‑1 can bind recombinant human VEGF165 with an apparent KD <1 nM. |
Source | Mouse myeloma cell line, NS0-derived mouse Neuropilin-1 protein Phe22-Pro856, with a C-terminal 6-His tag |
Accession # | |
N-terminal Sequence | Phe22 |
Structure / Form | Noncovalently-linked homodimer |
Protein/Peptide Type | Recombinant Proteins |
Gene | Nrp1 |
Purity | >95%, by SDS-PAGE under reducing conditions and visualized by silver stain |
Endotoxin Note | <0.10 EU per 1 μg of the protein by the LAL method. |
Dilutions |
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Theoretical MW | 94.5 kDa (monomer). Disclaimer note: The observed molecular weight of the protein may vary from the listed predicted molecular weight due to post translational modifications, post translation cleavages, relative charges, and other experimental factors. |
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SDS-PAGE | 100-120 kDa, reducing conditions |
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Publications |
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Storage | Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
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Buffer | Lyophilized from a 0.2 μm filtered solution in PBS. |
Purity | >95%, by SDS-PAGE under reducing conditions and visualized by silver stain |
Reconstitution Instructions | Reconstitute at 500 μg/mL in PBS. |
U.S. Patent # 6,054,293, 6,623,738, and other U.S. and international patents pending.
This product is produced by and ships from R&D Systems, Inc., a Bio-Techne brand.
Neuropilin-1 (Npn-1, previously neuropilin; also CD304 or BDCA4 in humans) is a 130‑140 kDa type I transmembrane (TM) glycoprotein that regulates axon guidance and angiogenesis (1‑4). The full-length 923 amino acid (aa) mouse Npn-1 contains a 623 aa extracellular domain (ECD) that shares 98% aa identity with rat and 93% aa identity with human, equine, bovine and canine Npn-1 (3, 4). The ECD contains two N-terminal CUB domains (termed a1a2), two domains with homology to coagulation factors V and VIII (b1b2) and a MAM (meprin) domain (c). At least one splice variant that diverges at aa 587 and lacks the TM domain has been sequenced (5). This form is potentially a soluble antagonist, based on results from human Npn-1 splice variants (1, 6‑8). The sema domains of Class III secreted semaphorins such as Sema3A bind Npn-1 a1a2 (9). Heparin, the heparin-binding forms of VEGF (VEGF165, VEGF-B and VEGF-E), PlGF (PlGF2), and the C‑terminus of Sema3 bind the b1b2 region (9, 10). 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 (11). 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 (12). 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 (13).
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