Goat Polyclonal Neuropilin 1 antibody - conjugated to Biotin. Suitable for ELISA, WB, sELISA and reacts with Human samples. Immunogen corresponding to Recombinant Full Length Protein corresponding to Human NRP1.
pH: 7.2
Constituents: PBS
| ELISA | WB | sELISA | |
|---|---|---|---|
| Human | Expected | Expected | Expected |
| Species | Dilution info | Notes |
|---|---|---|
Species Human | Dilution info - | Notes Allows the detection of at least 0.2 - 0.4 ng/well of recombinant human Neuropilin 1. |
| Species | Dilution info | Notes |
|---|---|---|
Species Human | Dilution info - | Notes The detection limit for recombinant human Neuropilin 1 is 1.5 - 3.0 ng/lane, under either reducing or non-reducing conditions. |
| Species | Dilution info | Notes |
|---|---|---|
Species Human | Dilution info - | Notes When used as detection antibody paired with recommended antibody, allows the detection of at least 0.2 - 0.4 ng/well of recombinant human Neuropilin 1. |
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Cell-surface receptor involved in the development of the cardiovascular system, in angiogenesis, in the formation of certain neuronal circuits and in organogenesis outside the nervous system. Mediates the chemorepulsant activity of semaphorins (PubMed:10688880, PubMed:9288753, PubMed:9529250). Recognizes a C-end rule (CendR) motif R/KXXR/K on its ligands which causes cellular internalization and vascular leakage (PubMed:19805273). It binds to semaphorin 3A, the PLGF-2 isoform of PGF, the VEGF165 isoform of VEGFA and VEGFB (PubMed:10688880, PubMed:19805273, PubMed:9288753, PubMed:9529250). Coexpression with KDR results in increased VEGF165 binding to KDR as well as increased chemotaxis. Regulates VEGF-induced angiogenesis. Binding to VEGFA initiates a signaling pathway needed for motor neuron axon guidance and cell body migration, including for the caudal migration of facial motor neurons from rhombomere 4 to rhombomere 6 during embryonic development (By similarity). Regulates mitochondrial iron transport via interaction with ABCB8/MITOSUR (PubMed:30623799). (Microbial infection) Acts as a host factor for human coronavirus SARS-CoV-2 infection. Recognizes and binds to CendR motif RRAR on SARS-CoV-2 spike protein S1 which enhances SARS-CoV-2 infection. Isoform 2. Binds VEGF-165 and may inhibit its binding to cells (PubMed:10748121, PubMed:26503042). May induce apoptosis by sequestering VEGF-165 (PubMed:10748121). May bind as well various members of the semaphorin family. Its expression has an averse effect on blood vessel number and integrity.
CD304, NRP, VEGF165R, NRP1, Neuropilin-1, Vascular endothelial cell growth factor 165 receptor
Goat Polyclonal Neuropilin 1 antibody - conjugated to Biotin. Suitable for ELISA, WB, sELISA and reacts with Human samples. Immunogen corresponding to Recombinant Full Length Protein corresponding to Human NRP1.
pH: 7.2
Constituents: PBS
ab83435 is sterile filtered.This antibody was purified by affinity chromatography and then biotinylated.
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.
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.
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.
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