Anti-Neuropilin 1/NRP1 Antibody Picoband® Fluoro647 Conjugated

This gene encodes one of two neuropilins, which contain specific protein domains which allow them to participate in several different types of signaling pathways that control cell migration. Neuropilins contain a large N-terminal extracellular domain, made up of complement-binding, coagulation factor V/VIII, and meprin domains. These proteins also contain a short membrane-spanning domain and a small cytoplasmic domain. Neuropilins bind many ligands and various types of co-receptors; they affect cell survival, migration, and attraction. Some of the ligands and co-receptors bound by neuropilins are vascular endothelial growth factor (VEGF) and semaphorin family members. Several alternatively spliced transcript variants that encode different protein isoforms have been described for this gene.

E.coli-derived human Neuropilin 1 recombinant protein (Position: K504-T827) . Human Neuropilin 1 shares 95% and 94% amino acid (aa) sequences identity with mouse and rat Neuropilin 1, respectively.

The expression of isoforms 1 and 2 does not seem to overlap. Isoform 1 is expressed by the blood vessels of different tissues. In the developing embryo it is found predominantly in the nervous system. In adult tissues, it is highly expressed in heart and placenta; moderately in lung, liver, skeletal muscle, kidney and pancreas; and low in adult brain. Isoform 2 is found in liver hepatocytes, kidney distal and proximal tubules.

Adaptive Immunity, Angiogenesis, Axonal Guidance Proteins, Cardiovascular, Growth and Development, Growth Factors, Immunology, Neurology Process, Neuroscience

The membrane-bound isoform 1 is a receptor involved in the development of the cardiovascular system, in angiogenesis, in the formation of certain neuronal circuits and in organogenesis outside the nervous system. It mediates the chemorepulsant activity of semaphorins. It binds to semaphorin 3A, The PLGF-2 isoform of PGF, The VEGF-165 isoform of VEGF and VEGF-B. Coexpression with KDR results in increased VEGF-165 binding to KDR as well as increased chemotaxis. It may regulate VEGF-induced angiogenesis.

1. Gagnon, M. L., Bielenberg, D. R., Gechtman, Z., Miao, H.-Q., Takashima, S., Soker, S., Klagsbrun, M. Identification of a natural soluble neuropilin-1 that binds vascular endothelial growth factor: in vivo expression and antitumor activity. Proc. Nat. Acad. Sci. 97: 2573-2578, 2000. 2. Gu, C., Rodriguez, E. R., Riemert, D. V., Shu, T., Fritzsch, B., Richards, L. J., Kolodkin, A. L., Ginty, D. D. Neuropilin-1 conveys semaphorin and VEGF signaling during neural and cardiovascular development. Dev. Cell 5: 45-57, 2003.