Recombinant Mouse Neuropilin-2 Fc Chimera Protein, CF

Recombinant Mouse Neuropilin-2 Fc Chimera Protein, CF Summary

Product Specifications

Product Datasheets

Carrier Free

CF stands for Carrier Free (CF). We typically add Bovine Serum Albumin (BSA) as a carrier protein to our recombinant proteins. Adding a carrier protein enhances protein stability, increases shelf-life, and allows the recombinant protein to be stored at a more dilute concentration. The carrier free version does not contain BSA.

In general, we advise purchasing the recombinant protein with BSA for use in cell or tissue culture, or as an ELISA standard. In contrast, the carrier free protein is recommended for applications, in which the presence of BSA could interfere.

Background: Neuropilin-2

Neuropilin‑2 (Nrp2) is a transmembrane glycoprotein that plays an important role in neuronal axon guidance and development of the vascular system (1). Neuropilin‑2 is differentially expressed in the developing nervous system (2). It binds to Semaphorins 3B, 3C, and 3F, leading to neuronal growth cone collapse (2‑4). This action is important for repulsive axon guidance and accurate axon projection to target fields (4‑7). Neuropilin-2 interacts with a range of proteins that regulate cell growth and morphology. It associates with TGF-beta RI and enhances the ability of TGF‑beta to induce epithelial mesenchymal transition during tumorigenesis (8). It associates with Integrin  alpha 6 beta 1 and promotes alpha 6 beta 1 mediated adhesion to Laminin (9). Neuropilin‑2 additionally binds the heparin‑binding PlGF‑2, HGF, VEGF₁₄₅, and VEGF₁₆₅ (10, 11) and associates with VEGF R1, VEGF R2, and VEGF R3 (12, 13). The presence of Neuropilin‑2 on vascular endothelial cells potentiates the angiogenic signaling effects of HGF and VEGF₁₆₅ (11). Semaphorin 3F, however, can block the contribution of Neuropilin‑2 to angiogenesis (13). In the vascular system, Neuropilin-2 is predominantly expressed on lymphatic vessel and capillary endothelial cells where it cooperates with VEGF R3 to induce lymphatic sprouting (14, 15). Neuropilin‑2 is lost from sympathetic nerve fibers in rheumatoid arthritis (RA) synovium, while a soluble form is elevated in RA synovial fluid (16). Neuropilin‑2 is expressed as an approximately 120 kDa molecule that associates into homo‑oligomers or hetero‑oligomers with Neuropilin‑1 (3, 4). It can be polysialylated during dendritic cell maturation to reach sizes as large as 200 kDa (17). Mature mouse Neuropilin‑2 consists of an 844 amino acid (aa) extracellular domain (ECD) with two CUB domains, two complement factor 5/8‑like domains, one MAM domain, and a Ser-Thr rich region, followed by a 25 aa transmembrane segment and a 42 aa cytoplasmic domain (2). Within the ECD, mouse Neuropilin‑2 shares 94% and 97% aa sequence identity with human and rat Neuropilin‑2, respectively. Alternative splicing of mouse Neuropilin‑2 generates additional isoforms with short deletions in the Ser‑Thr rich region or substitutions of the Ser‑Thr rich region, transmembrane segment, and cytoplasmic domain (2, 18).

Related Research Areas

• Semaphorins, Plexin Receptors, and Related Molecules
• VEGF Family
• VEGF Receptors and Regulators on Endothelial Cells