|Product Name||Anti-Neuropilin 1/NRP1 Picoband™ 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, IHC-P in Human;Rat.|
|Cite This Product||Anti-Neuropilin 1/NRP1 Picoband™ Antibody (Boster Biological Technology, Pleasanton CA, USA, Catalog # PB9300)|
|Contents/Buffer||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.|
Assay Dilutions Overview
Immunohistochemistry(Paraffin-embedded Section), 0.5-1μg/ml, Human, By Heat
Western blot, 0.1-0.5μg/ml, Human, Rat
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, and HRP Conjugated anti-Rabbit IgG Super Vision Assay Kit (SV0002-1) for IHC(P).
Images And Assay Conditions
Anti- Neuropillin-1 Picoband antibody, PB9300, Western blotting
All lanes: Anti Neuropillin-1 (PB9300) at 0.5ug/ml
Lane 1: U87 Whole Cell Lysate at 40ug
Lane 2: A549 Whole Cell Lysate at 40ug
Lane 3: Human Placenta Tissue Lysate at 50ug
Lane 4: Rat Cardiac Muscle Tissue Lysate at 50ug
Predicted bind size: 103KD
Observed bind size: 103KD
Anti- Neuropillin-1 Picoband antibody, PB9300, IHC(P)
IHC(P): Human Placenta Tissue
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||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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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.,