|Product Name||Anti-Nogo A/RTN4 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 Reticulon-4(RTN4) detection. Tested with WB, IHC-P in Human;Mouse;Rat.|
|Cite This Product||Anti-Nogo A/RTN4 Antibody (Boster Biological Technology, Pleasanton CA, USA, Catalog # PA1060)|
|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 at the C-terminus of human Nogo A(1170-1192aa NKNVKDAMAKIQAKIPGLKRKAE), different from the related rat sequence by two amino acids, and from the related mouse sequence by one amino acid.|
|Reactivity||Human, Mouse, Rat|
Assay Dilutions Overview
Immunohistochemistry(Paraffin-embedded Section), 0.5-1μg/ml, Rat, Human, Mouse, By Heat
Western blot, 0.1-0.5μg/ml, Mouse, Rat, Human
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-Nogo A antibody, PA1060, Western blotting
Lane 1: Rat Brain Tissue Lysate
Lane 2: Rat Brain Tissue Lysate
Lane 3: Mouse Brain Tissue Lysate
Lane 4: Mouse Brain Tissue Lysate
Anti-Nogo A antibody, PA1060, IHC(P)
IHC(P): Rat Brain Tissue
Protein Target Info (Source: Uniprot.org)
|Tissue Specificity||Isoform 1 is specifically expressed in brain and testis and weakly in heart and skeletal muscle. Isoform 2 is widely expressed except for the liver. Isoform 3 is expressed in brain, skeletal muscle and adipocytes. Isoform 4 is testis- specific.|
|Alternative Names||Reticulon-4;Foocen;Neurite outgrowth inhibitor;Nogo protein;Neuroendocrine-specific protein;NSP;Neuroendocrine-specific protein C homolog;RTN-x;Reticulon-5;RTN4;KIAA0886, NOGO;My043, SP1507;|
|Subcellular Localization||Endoplasmic reticulum membrane; Multi-pass membrane protein. Anchored to the membrane of the endoplasmic reticulum through 2 putative transmembrane domains.|
|Molecular Weight||129931 MW|
*if product is indicated to react with multiple species, protein info is based on the human gene.
|Protein Function||Developmental neurite growth regulatory factor with a role as a negative regulator of axon-axon adhesion and growth, and as a facilitator of neurite branching. Regulates neurite fasciculation, branching and extension in the developing nervous system. Involved in down-regulation of growth, stabilization of wiring and restriction of plasticity in the adult CNS. Regulates the radial migration of cortical neurons via an RTN4R-LINGO1 containing receptor complex (By similarity). Isoform 2 reduces the anti-apoptotic activity of Bcl-xl and Bcl-2. This is likely consecutive to their change in subcellular location, from the mitochondria to the endoplasmic reticulum, after binding and sequestration. Isoform 2 and isoform 3 inhibit BACE1 activity and amyloid precursor protein processing. .|
|Research Areas||Neurology Process, Neuroscience
*You can search these to find other products in these research areas.
|Background||Human neurite outgrowth inhibitor(NOGO) cDNAs encodes 3 splice variants: NOGOA, NOGOB and NOGOC. The longest cDNA, designated NOGOA, has an open reading frame of 1192 amino acids. It is a potent inhibitor of neurite growth and an IN-1 antigen produced by oligodendrocytes, and may allow the generation of new reagents to enhance CNS regeneration and plasticity. Nogo-A, a member of the Reticulon family, is expressed by oligodendrocytes and associates primarily with the endoplasmic reticulum. The acidic amino terminus of Nogo-A is detected at the cytosolic face of cellular membranes and may contribute to inhibition of axon regeneration at sites of oligodendrocyte injury. A multivalent form of the N terminus of Nogo-A affects the morphology of both neurons and other cell types.|
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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.,