Detects mouse Neuropilin-1 in direct ELISAs.
In direct ELISAs, less than 5%
cross-reactivity with recombinant rat (rr) Neuropilin-1 is observed and no
cross-reactivity with recombinant human (rh) Neuropilin-1, rhNeuropilin-2, or
rrNeuropilin-2 is observed.
Monoclonal Rat IgG2A Clone # 761705
Protein A or G purified from hybridoma culture supernatant
Detection of Neuropilin-1 in bEnd.3 Mouse Cell Line by Flow Cytometry.
bEnd.3 mouse endothelioma cell line was stained with Rat Anti-Mouse Neuropilin‑1 Monoclonal Antibody (Catalog # MAB5994, filled histogram) or isotype control antibody (Catalog # MAB006, open histogram), followed by Allophycocyanin-conjugated Anti-Rat IgG Secondary Antibody (Catalog # F0113).
Preparation and Storage
Sterile PBS to a final concentration of 0.5 mg/mL.
The product is shipped at ambient temperature. Upon receipt, store it immediately at the temperature recommended below. *Small pack size (SP) is shipped with polar packs. Upon receipt, store it immediately at -20 to -70 °C
Stability & Storage
Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
12 months from date of receipt, -20 to -70 °C as supplied.
1 month, 2 to 8 °C under sterile conditions after reconstitution.
6 months, -20 to -70 °C under sterile conditions after reconstitution.
Neuropilin-1 (Nrp-1, previously neuropilin; also CD304) 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 Nrp-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 Nrp-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 Nrp-1 splice variants (1, 6 - 8). The sema domains of Class III secreted semaphorins such as Sema3A bind Nrp-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). Nrp-1 and Nrp-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 Nrp-1 binds Sema3A, and only Nrp-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). Nrp-1 is preferentially expressed in developing or remodeling arteries (1, 2). Nrp-1 is also expressed on dendritic cells and mediates DC-induced T cell proliferation (13).
Bielenberg, D.R. et al. (2006) Exp. Cell Res. 312:584.
Gu, C. et al. (2003) Dev. Cell 5:45.
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Soker, S. et al. (1998) Cell 92:735.
Entrez accession #EDL11827
Gagnon, M.L. et al. (2000) Proc. Natl. Acad. Sci. USA 97:2573.
Cackowski, F.C. et al. (2004) Genomics 84:82.
Rossignol, M. et al. (2000) Genomics 70:211.
Gu, C. et al. (2002) J. Biol. Chem. 277:18069.
Mamluk, R. et al. (2002) J. Biol. Chem. 277:24818.
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The data collected includes not only links to publications in PubMed,
but also provides information about sample types, species, and experimental conditions.
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