|Reactivity||Human, Mouse, Rat|
|Product Name||Anti-Neuropilin 1/NRP1 Antibody|
|Storage & Handling||At -20°C for one year. After reconstitution, 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.|
|Description||Rabbit IgG polyclonal antibody for Neuropilin-1(NRP1) detection. Tested with WB in Human;Mouse;Rat.|
|Cite This Product||Anti-Neuropilin 1/NRP1 Antibody (Boster Biological Technology, Pleasanton CA, USA, Catalog # PA1752)|
|Contents/Buffer||Each vial contains 5mg BSA, 0.9mg NaCl, 0.2mg Na2HPO4, 0.05mg Thimerosal, 0.05mg NaN3.|
|Immunogen||A synthetic peptide corresponding to a sequence in the middle region of human Neuropilin 1(211-230aa LEIWDGFPDVGPHIGRYCGQ), different from the related rat and mouse sequences by one amino acid.|
|Reactivity||Human, Mouse, Rat|
Assay Dilutions Overview
Western blot, 0.1-0.5μg/ml, Human, Rat, Mouse
Boster's Secondary Antibodies And IHC, WB Kits
The following reagents are used to generate the images below.Boster recommends Enhanced Chemiluminescent Kit with anti-Rabbit IgG (EK1002) for Western blot.
Images And Assay Conditions
Anti-Neuropilin 1 antibody, PA1752, Western blotting
Lane 1: HELA Cell Lysate
Lane 2: MM231 Cell Lysate
Protein Target Info (Source: Uniprot.org)
|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.|
|Alternative Names||Neuropilin-1;Vascular endothelial cell growth factor 165 receptor;CD304;NRP1;NRP, VEGF165R;|
|Subcellular Localization||Cell membrane; Single-pass type I membrane protein.|
|Molecular Weight||103134 MW|
*if product is indicated to react with multiple species, protein info is based on the human gene.
|Protein Function||The membrane-bound isoform 1 is a 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. It mediates the chemorepulsant activity of semaphorins. It binds to semaphorin 3A, The PLGF-2 isoform of PGF, The VEGF-165 isoform of VEGF and VEGF-B. Coexpression with KDR results in increased VEGF-165 binding to KDR as well as increased chemotaxis. It may regulate VEGF-induced angiogenesis.|
|Research Areas||Adaptive Immunity, Angiogenesis, Axonal Guidance Proteins, Cardiovascular, Growth And Development, Growth Factors, Immunology, Neurology Process, Neuroscience
*You can search these to find other products in these research areas.
|Background||NRP1(Neuropilin 1) also known as NP1, NRP, BDCA4 or VEGF165R, is a membrane-bound coreceptor to a tyrosine kinase receptor for both vascular endothelial growth factor(VEGF) and semaphorin(see SEMA3A) family members. NRP1 plays versatile roles in angiogenesis, axon guidance, cell survival, migration, and invasion. By somatic cell hybrid analysis, the NRP1 gene was mapped to chromosome 10.They localized the NRP1 gene to 10p12 using radiation hybrid mapping. Sulfation of the glucosamine-O-6 and iduronic acid-O-2 groups of heparin potentiated PGF2 binding to NRP1. NRP1 also bound PGF1 with lower affinity. NRP1-mediated interactions are a necessary element in the initiation of the primary immune response and offer another example, like that of agrin, of a molecule shared by neurologic and immunologic synapses. After T-cell contact with DC, T-cell NRP1 colocalized with CD3 in the immunologic synapse and, sometimes, also at the opposite pole of the T cell. Soluble NRP1 interacts in a homophilic fashion with NRP1 on both DC and T cells, and this binding can be inhibited by blocking antibodies to NRP1. Furthermore, selective NRP1 inhibition in this model suppressed neovascular formation substantially.|
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1. Post-translational modification:phosphorylation, methylation, glycosylation etc. These modifications prevent SDS molecules from binding to the target protein and thus make the band size appear larger than expected
2. Post-translational cleavage: this can cause smaller bands and or multiple bands
3. Alternative splicing: the same gene can have alternative splicing patterns generating different size proteins, all with reactivities to the antibody.
4. Amino Acid R chain charge: SDS binds to positive charges. The different size and charge of the Amino Acid side chains can affect the amount of SDS binding and thus affect the observed band size.
5. Multimers: Multimers are usually broken up in reducing conditions. However if the interactions between the multimers are strong, the band may appear higher.,