- Other Names
- NRP1, NRP-1, NPN1, NP1, NRP, VEGF165R, Vascular endothelial growth factor-165 receptor, BDCA4, Blood Dendritic cell antigen 4
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Neuropilin-1 (NRP1) is a type I transmembrane receptor that functions to mediate angiogenesis and neurogenesis, binding members of the vascular endothelial growth factor (VEGF) family and class III semaphorins (Sema III). Due to lack of catalytic activity of its cytoplasmic domain, NRP1 is considered to exert signaling functions via recruitment of or complex formation with other receptors, including plexins for the downstream effects of semaphorins on growth-cone collapse and axonal guidance via recruitment of monomeric GTPases of the Rho family, and VEGF receptor 2 (VEGFR2) for the VEGF-induced endothelial cell proliferation, migration, and vascular remodeling via PI3K/Akt signal transduction pathway. Highly expressed in endothelial cells with KDR/FLK-1 (VEGFR2), NRP1 promotes the anchoring of 165–amino acid isoform of vascular endothelial growth factor A (VEGF-A165) with KDR as well as VEGF165-regulated chemotaxis, playing central roles in embryonic and neural vascularization as well as tumor development and progression, especially in breast, lung, prostate, pancreatic and colon carcinomas. Alternative splicing produces several isoforms whose size ranges from 551 to 704 amino acid residues, though only two soluble ones—namely, s12NRP1 (NRP1 isoform b) and sIVNRP1 (NRP1 isoform c)—are known to exist in protein form and found in protein databases. While NRP gene knockout is strongly implicated in broad categories of neuronal and cardiovascular dysfunctions, its overexpression predicates embryonic lethality by inducing capillary overgrowth, hemorrhage in the head, neck and heart, as well as uncontrolled sprouting and nerve fiber defasciculation. Also facilitating T-cell maturation and activation in the immune system, NRP1 and plexin A1 are upregulated in response to IFNγ activation of microglia exerting neuroprotective effects against potential damage by triggering microglial apoptosis through Sema3A. NRP1’s role in wound healing has also been identified in mouse models with cerebral ischemia, the mRNA expression of NRP1 elevated in response to the injury and remaining so for at least a month. With its localization to ischemic neurons and brain vessel endothelial cells, NRP1 mediates both neuronal growth and angiogenesis.Product Details
- Human Neuropilin-1, amino acids Phe22-Lys644 (Accession # NP_001019799) with a C-terminal 8x His tag was expressed in CHO cells.
- Molecular Mass
- The 636 amino acid recombinant protein has a predicted molecular mass of approximately 71.3 kD. The DTT-reduced and non-reduced proteins migrate at approximately 80 kD by SDS-PAGE. The predicted N-terminal amino acid is Phe.
- > 95%, as determined by Coomassie stained SDS-PAGE.
- 0.22 µm filtered protein solution is in PBS, pH 7.2.
- Endotoxin Level
- Less than 1.0 EU per µg protein as determined by the LAL method.
- 10 and 25 µg sizes are bottled at 200 µg/mL. 100 µg and larger sizes are lot-specific and bottled at the concentration indicated on the vial (please contact technical support for concentration, or use our Lookup tool if you have a lot number.)
- Storage & Handling
- Unopened vial can be stored between 2°C and 8°C for up to 2 weeks, at -20°C for up to six months, or at -70°C or colder until the expiration date. For maximum results, quick spin vial prior to opening. The protein can be aliquoted and stored at -20°C or colder. Stock solutions can also be prepared at 50 - 100 µg/mL in appropriate sterile buffer, carrier protein such as 0.2 - 1% BSA or HSA can be added when preparing the stock solution. Aliquots can be stored between 2°C and 8°C for up to one week and stored at -20°C or colder for up to 3 months. Avoid repeated freeze/thaw cycles.
- When human NRP-1 is immobilized at 1.0 µg/mL, biotinylated human VEGF-165 binds in a dose dependent manner with EC50 of 30-120 ng/mL.
- Application Notes
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.
BioLegend carrier-free recombinant proteins provided in liquid format are shipped on blue-ice. Our comparison testing data indicates that when handled and stored as recommended, the liquid format has equal or better stability and shelf-life compared to commercially available lyophilized proteins after reconstitution. Our liquid proteins are verified in-house to maintain activity after shipping on blue ice and are backed by our 100% satisfaction guarantee. If you have any concerns, contact us at firstname.lastname@example.org.
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.
- 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.
- Endothelial cells, Neurons
- VEGF-165, VEGF-B167, PLGF-2, Semaphorins
- Measured by the ability of immobilized protein to bind VEGF-165
- Biology Area
- Angiogenesis, Cell Adhesion, Cell Biology, Immunology, Innate Immunity, Neuroscience, Synaptic Biology
- Molecular Family
- Adhesion Molecules, CD Molecules
- Antigen References
1. He Z and Tessier-Lavigne M. 1997. Cell. 739-51.
2. Soker S, et al. 1998. Cell. 735-45.
3. Tordjman R, et al. 2002. Nat. Immunol. 477-82.
4. Neufeld G, et al. 2002. Adv. Exp. Med. Biol. 81-90.
5. Bielenberg DR, et al. 2006. Exp. Cell Res. 584-93.
6. Pellet-Many C, et al. 2008. Biochem. J. 211-26.
7. Shibuya M. 2011. Genes Cancer. 1097-105.
- Gene ID
- 8829 View all products for this Gene ID
- View information about Neuropilin-1 on UniProt.org
- Does specific activity of a recombinant protein vary between lots?
Specific activity will vary for each lot and for the type of experiment that is done to validate it, but all passed lots will have activity within the established ED50 range for the product and we guarantee that our products will have lot-to-lot consistency. Please conduct an experiment-specific validation to find the optimal ED50 for your system.
- Have your recombinants been tested for stability?
Our testing shows that the recombinant proteins are able to withstand room temperature for a week without losing activity. In addition the recombinant proteins were also found to withstand four cycles of freeze and thaw without losing activity.
- How do you convert activity as an ED50 in ng/ml to a specific activity in Units/mg?
- Use formula Specific activity (Units/mg) = 10e6/ ED50 (ng/mL)
- How does the activity of your recombinant proteins compare to competitors?
We quality control each and every lot of recombinant protein. Not only do we check its bioactivity, but we also compare it against other commercially available recombinant proteins. We make sure each recombinant protein’s activity is at least as good as or better than the competition’s. In order to provide you with the best possible product, we ensure that our testing process is rigorous and thorough. If you’re curious and eager to make the switch to BioLegend recombinants, contact your sales representative today!
- What is the specific activity or ED50 of my recombinant protein?
The specific activity range of the protein is indicated on the product datasheets. Because the exact activity values on a per unit basis can largely fluctuate depending on a number of factors, including the nature of the assay, cell density, age of cells/passage number, culture media used, and end user technique, the specific activity is best defined as a range and we guarantee the specific activity of all our lots will be within the range indicated on the datasheet. Please note this only applies to recombinants labeled for use in bioassays. ELISA standard recombinant proteins are not recommended for bioassay usage as they are not tested for these applications.