When Recombinant Human Neuropilin-1 Fc Chimera (Catalog # 10445-N1) is immobilized at 0.25 μg/mL (100 μL/well), Recombinant Human VEGF 165 (Catalog # 293-VE) binds with an ED50 of 0.25-1.5 ng/mL.
2 µg/lane of Recombinant Human Neuropilin-1 Fc Chimera (Catalog # 10455-N1) was resolved by SDS-PAGE under reducing (R) and non-reducing (NR) conditions and visualized by Coomassie® Blue staining, showing bands at ...read more
Recombinant Human Neuropilin-1 Fc Chimera Protein, CF Summary
Details of Functionality
Measured by its binding ability in a functional ELISA. When Recombinant Human Neuripilin-1 Fc Chimera is immobilized at 1 µg/mL (100 µL/well), Recombinant Human VEGF 165
(Catalog #
293-VE)
binds with an ED50 of 0.25-1.5 ng/mL.
Source
Human embryonic kidney cell, HEK293-derived human Neuropilin-1 protein
Human Neuropilin-1 (Phe22-Lys852) Accession # NP_003864.4
>95%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining.
Endotoxin Note
<0.10 EU per 1 μg of the protein by the LAL method.
Applications/Dilutions
Dilutions
Bioactivity
Theoretical MW
120 kDa. 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.
SDS-PAGE
117-131 kDa, under reducing conditions
Publications
Read Publications using 10455-N1 in the following applications:
Neuropilin-1 (Npn-1, also known as neuropilin
and 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) human Npn-1 isoform 1 contains an 835 aa extracellular domain
(ECD) that shows 92-95% aa identity with mouse, rat, 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). C-terminally divergent splice variants with 704, 644, 609,
and 551 aa lack the MAM and TM domains and are demonstrated or presumed to be
soluble antagonists (1, 5-7). A 906 aa form lacks a TM segment,
but secretion has not been found (8). The sema domains of Class III secreted
semaphorins such as Sema3A bind Npn-1 a1a2 (9). Heparin, the heparin-binding
forms of VEGF (VEGF 165, 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 VEGF 165
binding (1). Sema3A signaling can be blocked by VEGF 165, which has
higher affinity for Npn-1 (12). Npn-1 is preferentially expressed in arteries
during development or those undergoing remodeling (1, 2). Npn-1 is also
expressed on dendritic cells and mediates DC-induced T cell proliferation (13).
Npn-1 is a marker of CD4+ Treg cells and a population of CD8+ T-cells
infiltrating solid tumors. Immunotherapies that block Npn-1 synergizes with
anti-PD-1 to enhance CD8+ proliferation and response (14). There is evidence
that Npn-1 with VEGF-A plays a role in stemness of breast cancer cell by
activating Wnt/b-catenin pathway (15).
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.
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.
Tao, Q. et al. (2003) Angiogenesis 6:39.
Gu, C. et al. (2002) J. Biol. Chem. 277:18069.
Mamluk, R. et al. (2002) J. Biol. Chem. 277:24818.
Yaron, A. et al. (2005) Neuron 45:513.
Narazaki, M. and G. Tosato (2006) Blood 107:3892.
Tordjman, R. et al. (2002) Nat. Immunol. 3:477.
Leclerc, M. et al. (2019) Nat Commun. 10:3345.
Zhang, L. et al. (2017) Cell Physiol. Biochem. 44:1251.
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FAQs for Neuropilin-1 (10455-N1). (Showing 1 - 2 of 2 FAQs).
If this product is used in an application or species as a part of a customer review, will that validate this product in the application/species?
If any of our primary antibodes are used in an untested application or species and it is shown to work through images from customer reviews or through publications, this validates the application/species for this product. Please check out our Innovator's Reward Program if you decide to test an antibody with a species or application that is not currently listed.
What research areas can Neuropilin-1 antibodies be used in?
Neuropilin-1 products can be applied in the following research areas: Adaptive Immunity, Angiogenesis, Breast Cancer, Cancer, Cardiovascular Biology, Neuroscience, and Virology Bacteria and Parasites.
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