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Biotin anti-α-Synuclein Phospho (Ser129) Antibody

Pricing & Availability
Clone
P-syn/81A (See other available formats)
Regulatory Status
RUO
Other Names
Synuclein alpha-140, non-A4 component of amyloid, alpha-synuclein, isoform NACP140, non-A beta component of AD amyloid Parkinson disease (autosomal dominant, Lewy body) 4
Isotype
Mouse IgG2a, κ
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Product Citations
publications
P-synslash81A_Biotin_a-synuclein_Phospho_Ser129_Antibody_IHC_010517_resized
IHC staining of α-synuclein deposits with biotin anti-α-Synuclein Phospho (Ser129) antibody (clone P-Syn/81A) on formalin-fixed, paraffin-embedded Parkinson's disease brain tissue. Following antigen retrieval using 70% formic acid, the tissue was incubated with the primary antibody at 5 µg/mL overnight at 4°C. HRP Streptavidin and DAB 2 Component with Stabilizer was used for the detection system followed by hematoxylin counterstaining, according to the protocol provided.
  • P-synslash81A_Biotin_a-synuclein_Phospho_Ser129_Antibody_IHC_010517_resized
    IHC staining of α-synuclein deposits with biotin anti-α-Synuclein Phospho (Ser129) antibody (clone P-Syn/81A) on formalin-fixed, paraffin-embedded Parkinson's disease brain tissue. Following antigen retrieval using 70% formic acid, the tissue was incubated with the primary antibody at 5 µg/mL overnight at 4°C. HRP Streptavidin and DAB 2 Component with Stabilizer was used for the detection system followed by hematoxylin counterstaining, according to the protocol provided.
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825704 100 µg 287€
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Description

α-synuclein is expressed principally in the nervous system, but it is also produced in other tissues, including  the skin. In the brain, the protein is primarily neuronal, but it is also present in glia. Neuronal α-synuclein is concentrated in presynapt   ic nerve terminals, interacts with plasma membrane phospholipids, and is also present in nuclei and mitochondria. At least three isoforms of α-synuclein are produced through alternative splicing. The most common isoform is a 140 amino acid-long transcript. Other isoforms includes, a-synuclein-126, lacking residues 41-54; and α-synuclein-112, which lacks residues 103-130. α-synuclein’s physiological role is poorly understood, but the protein has been implicated in regulating dopamine release and transport, synaptic vesicle clustering, and functioning as a SNARE-complex chaperone. α-synuclein fibrils are a major component of the intracellular Lewy bodies that are associated with Parkinson's disease, Lewy body dementia, and multiple system atrophy. α-synuclein is phosphorylated at low levels under normal physiological conditions whereas the majority of the protein is phosphorylated in Lewy bodies at S129.

Product Details
Technical Data Sheet (pdf)

Product Details

Verified Reactivity
Human
Antibody Type
Monoclonal
Host Species
Mouse
Immunogen
This monoclonal antibody was raised against a synthetic peptide corresponding to amino acids 124 - 134 of α-synuclein, phosphorylated at Serine 129, and conjugated to KLH via a C-terminal Cysteine.
Formulation
Phosphate-buffered solution, pH 7.2, containing 0.09% sodium azide.
Preparation
The antibody was purified by affinity chromatography and conjugated with biotin under optimal conditions.
Concentration
0.5 mg/mL
Storage & Handling
The antibody solution should be stored undiluted between 2°C and 8°C. Do not freeze.
Application

IHC-P - Quality tested
Recommended Usage

Each lot of this antibody is quality control tested by formalin-fixed paraffin-embedded immunohistochemical staining. For immunohistochemistry, a concentration range of 1.0 - 2.0 µg/ml is suggested. It is recommended that the reagent be titrated for optimal performance for each application.

Application Notes

This antibody is effective in immunohistochemistry (IHC-P). Additional reported applications (for the relevant formats) include: Western blotting, immunohistochemisty on frozen tissue sections (IHC-F), and immunocytochemistry.

P-syn/81A is a mAb that is specific to alpha synuclein that has been phosphorylated on serine 129.

Application References
  1. Waxman EA, Giasson BI. 2008. J. Neuropathol. Exp. Neurol. 67(5):402-16. (IHC-P, WB)
  2. Lim Y, et al. 2011. J. Neurosci. 31:10076. (IHC-P)
  3. Volpicelli-Daley LA, et al. 2014. Mol. Biol. Cell. 25:4010. (ICC) PubMed
  4. Adamowicz DH, et al. 2017. J. Neurosci. 37(7):1675-1684. (IHC-P, IHC-F) PubMed
RRID
AB_2650683 (BioLegend Cat. No. 825704)

Antigen Details

Structure
α-synuclein’s canonical isoform consists of 140 amino acids, which consist of four 11-residue repeats containing the consensus sequence KTKEGV. α-synuclein has an apparent molecular mass of 14 kD.
Distribution

Tissue distribution: primarily nervous system, but lower expression in other tissues such as skin.
Cellular distribution: cytoskeleton, cytosol, lysosome, mitochondria, nucleus, plasma membrane, and extracellular.

Function
The function of α-synuclein in the healthy brain is currently unknown.
Biology Area
Cell Biology, Neurodegeneration, Neuroscience, Protein Misfolding and Aggregation
Molecular Family
α-Synuclein, Phospho-Proteins
Antigen References

1. Mor DE, et al. 2016. Neurobiol Dis. 88:66. PubMed
2. Jucker M, Walker LC. 2013. Nature. 501(7465):45.
3. Bartels T, et al. 2011. Nature. 477(7362): 107. PubMed
4. Devine MJ, et al. 2011. Mov Disord. 26:2160. PubMed

Gene ID
6622 View all products for this Gene ID
UniProt
View information about alpha-Synuclein Phospho Ser129 on UniProt.org

Related FAQs

How many biotin molecules are per antibody structure?
We don't routinely measure the number of biotins with our antibody products but the number of biotin molecules range from 3-6 molecules per antibody.
Go To Top Version: 2    Revision Date: 08/29/2022

For Research Use Only. Not for diagnostic or therapeutic use.

 

This product is supplied subject to the terms and conditions, including the limited license, located at www.biolegend.com/terms) ("Terms") and may be used only as provided in the Terms. Without limiting the foregoing, BioLegend products may not be used for any Commercial Purpose as defined in the Terms, resold in any form, used in manufacturing, or reverse engineered, sequenced, or otherwise studied or used to learn its design or composition without express written approval of BioLegend. Regardless of the information given in this document, user is solely responsible for determining any license requirements necessary for user’s intended use and assumes all risk and liability arising from use of the product. BioLegend is not responsible for patent infringement or any other risks or liabilities whatsoever resulting from the use of its products.

 

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This data display is provided for general comparisons between formats.
Your actual data may vary due to variations in samples, target cells, instruments and their settings, staining conditions, and other factors.
If you need assistance with selecting the best format contact our expert technical support team.

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