Description
Key facts
Purity:>95% SDS-PAGE,
Endotoxin level:< 1 EU/µg,
Expression system:HEK 293 cells,
Tags:Tag free,
Applications:SDS-PAGE, FuncSSee reactivity dataSee the reactivity data table below for information on validated species and application combinations.,
Biologically active:Yes,
Biological activity:Measured by its binding ability in a functional ELISA. Immobilized ab221023 at 2 μg/mL (100 μL/well) can bind Biotinylated Human VEGF165 with a linear range of 5-40 ng/mL.,
Accession:O14786,
Animal free:No,
Carrier free:No,
Species:Human,
Reconstitution:Reconstitute at 200 µg/mL in water,
Storage buffer:pH: 7.4Constituents: L-Arginine, Sodium chloride, 5% Trehalose, 0.75% Glycine, 0.61% Tris
Properties and Storage Information:
Shipped at conditions-Blue Ice, Appropriate short-term storage conditions--20°C, Appropriate long-term storage conditions--20°C, Storage information-Avoid freeze / thaw cycle
Supplementary Information:
This supplementary information is collated from multiple sources and compiled automatically.
Neuropilin-1 also known as NRP1 is a transmembrane protein with a significant role in the nervous and vascular systems. It has a molecular mass of approximately 130 kDa. Neuropilin-1 expression occurs broadly in tissues including neurons endothelial cells and tumor cells. Its structure includes a large extracellular domain that binds various ligands mediating several cellular functions. Neuropilin-1 is sometimes targeted in experiments using methods like neuropilin-1 ELISA and PE immunofluorescence to study its distribution and function in different tissues.
Biological function summary
Neuropilin-1 serves as a co-receptor for both the Vascular Endothelial Growth Factor (VEGF) and Semaphorin family proteins. It plays an important role in processes such as angiogenesis axonal guidance and the immune system. Neuropilin-1 does not function alone; it forms complexes with neuropilin-2 and other receptors like Plexin and VEGFR enhancing signal transduction pathways for angiogenesis and neuronal development. This involvement allows cells to respond appropriately to their environment especially during organismal development and repair processes.
Pathways
Neuropilin-1 facilitates interactions within the VEGF and Semaphorin pathways. In the VEGF pathway Neuropilin-1 enhances binding and signaling efficiency with VEGF closely working alongside VEGFR to promote endothelial cell survival migration and new blood vessel formation. In the Semaphorin pathway Neuropilin-1 interacts with Plexins mediating neuronal pathfinding and axonal growth. These interactions highlight Neuropilin-1's adaptive capabilities in various physiological processes critical for system development.
Neuropilin-1 is linked to pathological conditions like cancer and cardiovascular diseases. Neuropilin-1 overexpression is frequently observed in tumors driving cancer progression through enhanced angiogenesis and tissue invasion closely interacting with proteins like VEGF-A. In cardiovascular disease Neuropilin-1 contributes to abnormal blood vessel formation and stability. By studying Neuropilin-1 and other biomarkers like CD304 FITC researchers aim to develop therapeutic strategies targeting its role in these diseases.
