Neuropilin-1 (E8L6E) Rabbit mAb #54568
- WB
- IP
- F
Supporting Data
| REACTIVITY | H |
| SENSITIVITY | Endogenous |
| MW (kDa) | 120-140 |
| Source/Isotype | Rabbit IgG |
Application Key:
- WB-Western Blotting
- IP-Immunoprecipitation
- F-Flow Cytometry
Species Cross-Reactivity Key:
- H-Human
Product Information
Product Usage Information
| Application | Dilution |
|---|---|
| Western Blotting | 1:1000 |
| Immunoprecipitation | 1:100 |
| Flow Cytometry (Fixed/Permeabilized) | 1:50 - 1:200 |
Storage
Protocol
Specificity / Sensitivity
Neuropilin-1 (E8L6E) Rabbit mAb recognizes endogenous levels of total neuropilin-1 protein. This antibody also cross-reacts with an unidentified protein of 52 kDa in some cell lines.
Species Reactivity:
Human
Source / Purification
Monoclonal antibody is produced by immunizing animals with a synthetic peptide corresponding to residues surrounding Leu914 of human neuropilin-1 protein.
Background
Class 3 secreted semaphorin (Sema3A) is a chemorepellent that acts upon a wide variety of axons. As such, it induces a dramatic redistribution and depolymerization of actin filaments that results in growth cone collapse. Plexins are single-pass, transmembrane signaling proteins encompassing Plexin A1, A2, A3, and A4. Plexins form a complex with neuropilin-1 and -2 and the cell adhesion protein L1 to form a functional semaphorin receptor (1,2). The GTPase Rnd1 binds to the cytoplasmic domain of Plexin A1 to trigger cytoskeletal collapse. In contrast, the GTPase RhoD blocks Rnd1-mediated Plexin A1 activation and repulsion of sympathetic axons by Sema3A (3).
Neuropilin-1, a single-pass transmembrane glycoprotein, was originally identified as a semaphorin receptor mediating axon growth cone collapse. In addition, neuropilin-1 is involved in axonal fasciculation, neuronal migration, dendritic guidance, and repair of the adult nervous system (4). Neuropilin-1 is also an isoform-specific VEGF receptor on tumor and endothelial cells. Loss of neuropilin-1 function causes vascular remodeling and branching defects, which is compounded by additional loss of neuropilin-2 function (4,5).
- Pasterkamp, R.J. and Kolodkin, A.L. (2003) Curr Opin Neurobiol 13, 79-89.
- Takahashi, T. and Strittmatter, S.M. (2001) Neuron 29, 429-39.
- Zanata, S.M. et al. (2002) J Neurosci 22, 471-7.
- He, Z. et al. (2002) Sci STKE 2002, re1.
- Kawasaki, T. et al. (1999) Development 126, 4895-902.
- Takashima, S. et al. (2002) Proc Natl Acad Sci U S A 99, 3657-62.
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