Recombinant Human Neuropilin 2 / NRP2 Protein (Fc tag)

Categories: [Proteins / Peptides]
Neuropilin-2 (NRP-2) which is related to NRP-1, is a type I? transmembrane glycoprotein and has the structure characteristic with five main extracellular domains: two complement binding (CUB) domains, two coagulation factor V/VIII homology domains, and a MAM (meprin, tyrosine phosphatase domain) region. NRP-2 is a receptor capable of binding two disparate ligands, classⅢ semaphorins (SEMA) and vascular endothelial growth factors (VEGF), and thus regulates two diverse systems by activating cellular signaling pathways via interacting with other cell surface receptors such as VEGF receptors and plexins. NRP-2 is well known for its role in facilitating axonal guidance during the development of the neuronal system, and additionally, it is also expressed in vascular endothelial cells and lymphatic endothelium where it affects proliferation, migration, angiogenesis, as well as formation of small lymphatic vessels and capillaries. Recent study has identified NRP-2 as a polysialylated protein expressed in human dendritic cells and modulates DC-T cell Interactions. Nearly all tumor cells express neuropilins and NRP-2 is predominantly expressed in neuronal tumors and melanomas. Furthermore, it is suggested that as the specific ligand for NRP-2, SEMA 3F inhibits tumor angiogenesis and metastasis.
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Properties

Data Sheet Click for Datasheet
Catalog Number TP06526
Size 20ug,50ug,100ug…
Host HEK293 Cells
Accession NP_003863.2
Molecular Weight 120.7 kDa
AP_Mol_Weight 119-129 kDa
Tag C-Fc
Sequences Met 1-Tyr855
Purity > 95% by HPLC
Concentration
Formulation PBS
Other Names Neuropilin-2;NP2;NPN2;PRO2714;VEGF165R2
Bioactivity Measured by its binding ability in a functional ELISA.2.Immobilized human VEGFC-His (Cat:10542-H08H) at 10μg/mL (100μL/well) can bind human NRP2-Fc (Cat:10695-H02H), the EC50 of human NRP2-Fc is 0.1-0.5μg/mL.
Storage Can be stored at +4°C short term (1-2 weeks). For long term storage, aliquot and store at -20°C or -70°C. Avoid repeated freezing and thawing cycles.
Postscript For research use only, not for use in diagnostic procedures.

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