Recombinant Human Neuropilin-2 Fc Chimera Protein, CF Summary
Details of Functionality
Measured by its binding ability in a functional ELISA. Immobilized Recombinant Human (rh) Neuropilin‑2 Fc Chimera can bind rhVEGF165 with an apparent KD < 5 nM.
Source
Mouse myeloma cell line, NS0-derived human Neuropilin-2 protein
Human Neuropilin-2 (Gln23-Tyr855) Accession #Q7LBX6
>90%, 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
Binding Activity
Theoretical MW
120.5 kDa (monomer). 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
140 kDa, reducing conditions
Publications
Read Publications using 2215-N2 in the following applications:
Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
12 months from date of receipt, -20 to -70 °C as supplied.
1 month, 2 to 8 °C under sterile conditions after reconstitution.
3 months, -20 to -70 °C under sterile conditions after reconstitution.
Buffer
Lyophilized from a 0.2 μm filtered solution in PBS.
Purity
>90%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining.
Reconstitution Instructions
Reconstitute at 100 μg/mL in sterile PBS.
Notes
This product or the use of
this product is covered by U.S. Patents owned by The Regents of the University of California. This product is for research
use only and is not to be used for commercial purposes. Use of this product to
produce products for sale or for diagnostic, therapeutic or drug discovery
purposes is prohibited. In order to obtain a license to use this product for
such purposes, contact The Regents of the University of California. U.S. Patent # 6,054,293, 6,623,738, and
other U.S.
and international patents pending.
This product is produced by and ships from R&D Systems, Inc., a Bio-Techne brand.
Alternate Names for Recombinant Human Neuropilin-2 Fc Chimera Protein, CF
Neuropilin-2 (Npn-2) is a 120 kDa, type I transmembrane (TM) glycoprotein that is related to the semaphorin receptor now known as Neuropilin-1 (1). Npn-2 is a complex molecule with multiple splice forms. Five transmembrane forms are known, and one 62 kDa soluble form has been identified (2). Based on the originally reported precursor size of 909 amino acids (aa), the “standard” precursor in human will have a 20 aa signal sequence, an 842 aa extracellular region, a 25 aa TM segment, and a 42 aa cytoplasmic tail (1). The extracellular region contains two N-terminal CUB (C1r/Ugef/BMP-1) domains, two jellyroll-shaped coagulation factor V type C domains, and a juxtamembrane MAM (meprin/A-5 protein/tyrosine phosphatase μ) domain (1, 3). The CUB and factor V domain are involved in VEGF and semaphorin binding. The MAM domain appears necessary for signaling through plexin-1 (4). The five transmembrane isoforms all share the same CUB, factor V and MAM domains. Splicing begins at aa 809, seven amino acids after the end of the MAM domain, and it involves the end of the extracellular region, the TM segment, and the cytoplasmic domain (a total of 101 aa). Two of the four variants show a complete replacement of these 101 aa with a totally unrelated stretch of approximately 90 aa. This creates a new TM and cytoplasmic tail. These forms are called “Npn-2b” forms. Two other isoforms (plus the standard 909 aa form) retain the 101 aa stretch, and add either 17 or 22 aa to the end of the extracellular region. These forms are called “Npn-2a” forms. The isoform offered by R&D Systems is the “a” form with the 17 aa addition. This isoform shows 94% aa identity to the equivalent regions in mouse and rat Npn-2. The soluble form of Npn-2 is 555 aa in precursor length, and contains the two CUB domains plus the first 1½ factor V type C domains (1). Npn-2 binds Sema3B through F, and VEGF isoforms 165, 145, PlGF-2 and VEGF-C (5). It is known to form homodimers and heterodimers with Npn-1, and it forms receptor complexes with plexin-1 and VEGF R1 (4, 5). Npn-2 is found on a variety of cell types including neurons (motor, autonomic, sensory), vascular endothelial cells, Schwann cells and pancreatic acinar cells.
Chen, H. et al. (1997) Neuron 19:547.
Rossignol, M. et al. (2000) Genomics 70:211.
He, Z. and M. Tessier-lavigne (1997) Cell 90:739.
Nakamura, F. and Y. Goshima (2002) Adv. Exp. Med. Biol. 515:55.
Neufeld, G. et al. (2002) Adv. Exp. Med. Biol. 515:81.
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