|Product Name||Anti-NSE/ENO2 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 Gamma-enolase(ENO2) detection. Tested with WB, IHC-P in Human;Mouse;Rat.|
|Cite This Product||Anti-NSE/ENO2 Antibody (Boster Biological Technology, Pleasanton CA, USA, Catalog # PA1061)|
|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 NSE(420-434aa EARFAGHNFRNPSVL), identical to the related mouse and rat sequences.|
|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, Rat, Human, 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, and HRP Conjugated anti-Rabbit IgG Super Vision Assay Kit (SV0002-1) for IHC(P).
Images And Assay Conditions
Anti-NSE antibody, PA1061, Western blotting
WB: Rat Brain Tissue Lysate
Figure 2. IHC analysis of NSE using anti-NSE antibody (PA1061).
NSE was detected in paraffin-embedded section of rat brain tissue. Heat mediated antigen retrieval was performed in citrate buffer (pH6, epitope retrieval solution) for 20 mins. The tissue section was blocked with 10% goat serum. The tissue section was then incubated with 1μg/ml rabbit anti-NSE Antibody (PA1061) overnight at 4°C. Biotinylated goat anti-rabbit IgG was used as secondary antibody and incubated for 30 minutes at 37°C. The tissue section was developed using Strepavidin-Biotin-Complex (SABC)(Catalog # SA1022) with DAB as the chromogen.
Protein Target Info (Source: Uniprot.org)
|Tissue Specificity||The alpha/alpha homodimer is expressed in embryo and in most adult tissues. The alpha/beta heterodimer and the beta/beta homodimer are found in striated muscle, and the alpha/gamma heterodimer and the gamma/gamma homodimer in neurons.|
|Alternative Names||Gamma-enolase;220.127.116.11;2-phospho-D-glycerate hydro-lyase;Enolase 2;Neural enolase;Neuron-specific enolase;NSE;ENO2;|
|Subcellular Localization||Cytoplasm . Cell membrane . Can translocate to the plasma membrane in either the homodimeric (alpha/alpha) or heterodimeric (alpha/gamma) form. .|
|Molecular Weight||47269 MW|
*if product is indicated to react with multiple species, protein info is based on the human gene.
|Protein Function||Has neurotrophic and neuroprotective properties on a broad spectrum of central nervous system (CNS) neurons. Binds, in a calcium-dependent manner, to cultured neocortical neurons and promotes cell survival (By similarity). .|
|Research Areas||Cancer, Cancer Metabolism, Carbohydrate Metabolism, Energy Metabolism, Energy Transfer Pathways, Epigenetics And Nuclear Signaling, Metabolic Signaling Pathway, Metabolic Signaling Pathways, Metabolism, Metabolism Of Carbohydrates, Pathways And Processes, Signal Transduction, Transcription, Tumor Biomarkers
*You can search these to find other products in these research areas.
|Background||NSE(neuron specific enolase), also known as Enolase 2(ENO2), is found in elevated concentrations in plasma in certain neoplasias. The enolases catalyze the interconversion of 2-phosphoglycerate to phosphoenolpyruvate in the glycolytic pathway. ENO2 gene contains 12 exons distributed over 9,213 nucleotides. Human neurone-specific enolase is mapped to chromosome 12p13.|
Other Recommended Resources
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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.,