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Anti-Neuropilin-1 Antibody
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- BACKGROUND
Application 
| WB, IHC-P |
|---|---|
| Primary Accession | O14786 |
| Host | Rabbit |
| Reactivity | Human, Rat |
| Clonality | Polyclonal |
| Format | Lyophilized |
| Description | Rabbit IgG polyclonal antibody for Neuropilin-1(NRP1) detection. Tested with WB, IHC-P in Human;Rat. |
| Reconstitution | Add 0.2ml of distilled water will yield a concentration of 500ug/ml. |
| Gene ID | 8829 |
|---|---|
| Other Names | Neuropilin-1, Vascular endothelial cell growth factor 165 receptor, CD304, NRP1, NRP, VEGF165R |
| Calculated MW | 103134 MW KDa |
| Application Details | Immunohistochemistry(Paraffin-embedded Section), 0.5-1 µg/ml, Human, By Heat Western blot, 0.1-0.5 µg/ml, Human, Rat |
| Subcellular Localization | Cell membrane; Single-pass type I membrane protein. |
| Tissue Specificity | The expression of isoforms 1 and 2 does not seem to overlap. Isoform 1 is expressed by the blood vessels of different tissues. In the developing embryo it is found predominantly in the nervous system. In adult tissues, it is highly expressed in heart and placenta; moderately in lung, liver, skeletal muscle, kidney and pancreas; and low in adult brain. Isoform 2 is found in liver hepatocytes, kidney distal and proximal tubules. |
| Protein Name | Neuropilin-1 |
| Contents | Each vial contains 5mg BSA, 0.9mg NaCl, 0.2mg Na2HPO4, 0.05mg NaN3. |
| Immunogen | E.coli-derived human Neuropilin 1 recombinant protein (Position: K504-T827). Human Neuropilin 1 shares 95% and 94% amino acid (aa) sequences identity with mouse and rat Neuropilin 1, respectively. |
| Purification | Immunogen affinity purified. |
| Cross Reactivity | No cross reactivity with other proteins |
| Storage | At -20˚C for one year. After r˚Constitution, at 4˚C for one month. It˚Can also be aliquotted and stored frozen at -20˚C for a longer time.Avoid repeated freezing and thawing. |
| Sequence Similarities | Belongs to the neuropilin family. |
| Name | NRP1 (HGNC:8004) |
|---|---|
| Synonyms | NRP, VEGF165R |
| Function | 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). |
| Cellular Location | [Isoform 2]: Secreted |
| Tissue Location | [Isoform 1]: The expression of isoforms 1 and 2 does not seem to overlap. Expressed in olfactory epithelium (at protein level) (PubMed:33082293). Expressed in fibroblasts (at protein level) (PubMed:36213313). Expressed by the blood vessels of different tissues In the developing embryo it is found predominantly in the nervous system. In adult tissues, it is highly expressed in heart and placenta; moderately in lung, liver, skeletal muscle, kidney and pancreas; and low in adult brain (PubMed:10688880, PubMed:9529250). Expressed in the central nervous system, including olfactory related regions such as the olfactory tubercles and paraolfactory gyri (PubMed:33082293) |
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Provided below are standard protocols that you may find useful for product applications.
Background
This gene encodes one of two neuropilins, which contain specific protein domains which allow them to participate in several different types of signaling pathways that control cell migration. Neuropilins contain a large N-terminal extracellular domain, made up of complement-binding, coagulation factor V/VIII, and meprin domains. These proteins also contain a short membrane-spanning domain and a small cytoplasmic domain. Neuropilins bind many ligands and various types of co-receptors; they affect cell survival, migration, and attraction. Some of the ligands and co-receptors bound by neuropilins are vascular endothelial growth factor (VEGF) and semaphorin family members. Several alternatively spliced transcript variants that encode different protein isoforms have been described for this gene.
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