Neuropilin-1 Protein, Human, Recombinant (His Tag): Product Information
> 95 % as determined by SDS-PAGE
< 1.0 EU per μg of the protein as determined by the LAL method
1. Using the Octet RED System, the affinity constant (Kd) of NRP1-his bound to biotinylated human VEGF165 was 25nM. 2. Measured by its binding ability in a functional ELISA. Immobilized NRP1-His (Cat:10011-H08H） at 10 μg/mL (100 μL/well) can bind VEGF165/Biotin (Cat:11066-HNAH), the EC50 of VEGF165/Biotin (Cat:11066-HNAH) is 18-40 ng/mL.
A DNA sequence encoding the human NRP1 isoform b (NP_001019799.1) (Met 1-Lys 644) was fused with a polyhistidine tag at the C-terminus.
The secreted recombinant human NRP1 consists of 634 amino acids and has a calculated molecular mass of 71.3 kDa. As a result of glycosylation, rh NRP1 migrates as an approximately 88 kDa band in SDS-PAGE under reducing conditions.
Lyophilized from sterile PBS, pH 7.4 Please contact us for any concerns or special requirements. Normally 5 % - 8 % trehalose, mannitol and 0.01% Tween80 are added as protectants before lyophilization.
Please refer to the specific buffer information in the hard copy of CoA.
In general, recombinant proteins are provided as lyophilized powder which are shipped at ambient temperature. Bulk packages of recombinant proteins are provided as frozen liquid. They are shipped out with blue ice unless customers require otherwise.
Stability & Storage
Samples are stable for up to twelve months from date of receipt at -20℃ to -80℃ Store it under sterile conditions at -20℃ to -80℃. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.
A hardcopy of COA with reconstitution instruction is sent along with the products. Please refer to it for detailed information.
Measured by its binding ability in a functional ELISA. Immobilized NRP1-His (Cat:10011-H08H） at 10 μg/mL (100 μL/well) can bind VEGF165/Biotin (Cat:11066-HNAH), the EC50 of VEGF165/Biotin (Cat:11066-HNAH) is 18-40 ng/mL.
Neuropilin is a type I transmembrane protein and the molecular mass is 12 kDa. Two homologues, Neuropilin-1 and Neuropilin-2, are identified. The primary structure of Neuropilin-1 and Neuropilin-2 is well conserved and is divided into four domains, CUB (a1/a2) domain, FV/FVIII (b1/b2) domain, MAM (c) domain, and (d) domain that contains a transmembrane and a short cytoplasmic region. Neuropilin-1 (NRP1) acts as a receptor for two different extracellular ligands, class 3 semaphorins and specific isoforms of vascular endothelial growth factor. The functions of NRP1 and NRP2 have been extensively studied in neurons where they act in axon guidance and in endothelial cells where they promote angiogenesis and cell migration. Neuropilin-1 is likely to mediate contacts between the dendritic cells and the T lymphocytes via homotypic interactions and is essential for the initiation of the primary immune response. NRP1 is a co-receptor for VEGF receptor-2 (VEGFR2) that enhances the binding of VEGF165 to VEGFR2 and VEGF165-mediated chemotaxis. NRP1 expression is regulated in EC by tumor necrosis factor-alpha, the transcription factors dHAND and Ets-1, and vascular injury. NRP1 upregulation is positively correlated with the progression of various tumors. Overexpression of NRPI in rat tumor cells results in enlarged tumors and substantially enhanced tumor angiogenesis. On the other hand, soluble NRP1 (sNRP1) is an antagonist of tumor angiogenesis.
Nakamura F, et al. (2002) Structural and functional relation of neuropilins. Adv Exp Med Biol. 515: 55-69.
Romeo PH, et al. (2002) Neuropilin-1 in the immune system. Adv Exp Med Biol. 515: 49-54.
Klagsbrun M, et al. (2002) The role of neuropilin in vascular and tumor biology. Adv Exp Med Biol. 515: 33-48.
Staton CA, et al. (2007) Neuropilins in physiological and pathological angiogenesis. J Pathol. 212(3): 237-48.
Bagri A, et al. (2009) Neuropilins in tumor biology. Clin Cancer Res. 15(6): 1860-4.
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