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 CD4+ Mouse Splenocytes by Flow Cytometry.
CD4+ mouse splenocytes were stained with Rabbit Anti-Human/Mouse FoxP3 Alexa Fluor® 488‑conjugated Monoclonal Antibody (Catalog # IC8214G) and either (A) Rat Anti-Mouse Neuropilin‑1 Alexa Fluor® 647‑conjugated Monoclonal Antibody (Catalog # FAB5994R) or (B) Rat IgG2A Alexa Fluor 647 Isotype Control (Catalog # IC006R). To facilitate intracellular staining of FoxP3, cells were fixed and permeabilized with FlowX FoxP3 Fixation & Permeabilization Buffer Kit (Catalog # FC012). Splenocytes were gated on CD4.View our protocol for Staining Membrane-associated Proteins.
Preparation and Storage
The product is shipped with polar packs. Upon receipt, store it immediately at the temperature recommended below.
Stability & Storage
Protect from light. Do not freeze.
12 months from date of receipt, 2 to 8 °C as supplied.
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.
He, Z. and M. Tessier-Lavigne (1997) Cell 90:739.
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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