alpha-Synuclein [p Ser129] Antibody - Azide and BSA Free

Novus Biologicals, part of Bio-Techne | Catalog # NBP3-05429

Novus Biologicals, part of Bio-Techne
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NBP3-05429
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Key Product Details

Species Reactivity

Human, Mouse, Rat

Applications

Western Blot

Label

Unconjugated

Antibody Source

Polyclonal Rabbit IgG

Format

Azide and BSA Free

Concentration

Please see the vial label for concentration. If unlisted please contact technical services.

View all alpha-Synuclein Antibodies »

Product Specifications

Immunogen

A synthetic phosphorylated peptide around S129 of human alpha-Synuclein (NP_000336.1). MPSEE

Modification

p Ser129

Clonality

Polyclonal

Host

Rabbit

Isotype

IgG

Scientific Data Images for alpha-Synuclein [p Ser129] Antibody - Azide and BSA Free

Western Blot: alpha-Synuclein [p Ser129] AntibodyAzide and BSA Free [NBP3-05429]

Western Blot: alpha-Synuclein [p Ser129] AntibodyAzide and BSA Free [NBP3-05429]

Western Blot: alpha-Synuclein [p Ser129] Antibody [NBP3-05429] - Western blot analysis of extracts from mouse brain tissue, using alpha-Synuclein antibody (NBP3-05429). Secondary antibody: HRP Goat Anti-Rabbit IgG (H+L) at 1:10000 dilution. Lysates/proteins: 25ug per lane. Blocking buffer: 3% BSA.

Applications for alpha-Synuclein [p Ser129] Antibody - Azide and BSA Free

Application
Recommended Usage

Western Blot

1:500-1:2000

Formulation, Preparation, and Storage

Purification

Affinity purified

Formulation

PBS with 50% glycerol, pH7.3.

Format

Azide and BSA Free

Preservative

0.01% Thimerosal

Concentration

Please see the vial label for concentration. If unlisted please contact technical services.

Shipping

The product is shipped with polar packs. Upon receipt, store it immediately at the temperature recommended below.

Stability & Storage

Store at -20C. Avoid freeze-thaw cycles.

Background: alpha-Synuclein

Alpha-synuclein, a member of the synuclein family, is a protein that was first identified in 1988 whose name is derived from its localization to both the synapse and nucleus (1-3). Specifically, it is expressed primarily in the brain, including Lewy Bodies (1-6). Alpha-synuclein is encoded by the SNCA gene, located on chromosome 4p21, and is processed as a 140 amino acid (aa) protein with a theoretical molecular weight of 14 kDa (1,2,4). Structurally alpha-synuclein consists of a N-terminal binding domain (1-60 aa), a central domain core region called the non-amyloid-beta component (NAC) (61-95 aa), and a C-terminal domain (96-140 aa) (1-3). The N-terminal region contains aa repeats with a KTKEGV consensus sequence that gives the protein its alpha-helical structure that associates with lipid membranes (1-4). The hydrophobic NAC region is responsible for alpha-synuclein aggregation and fibril formation (1-4). The acidic C-terminal tail is largely unstructured but can be targeted for post-translational modifications (1-4). The function of alpha-synuclein is not entirely understood, but it is shown to have a role in suppression of apoptosis, acting as a molecular chaperone, regulating glucose, and modulating calmodulin activity (1,3).

A number of studies have revealed that alpha-synuclein aggregation is a hallmark feature in a number of neurodegenerative diseases, referred to as synucleinopathies (2-4). Alpha-synuclein protein aggregates are a large component of Lewy bodies that are present in Parkinson's disease (PD), Lewy body dementia (LBD), and multiple system atrophy (1-6). Research has shown phosphorylation of alpha-synuclein at Ser129 moves the protein from the nucleus to the cytoplasm and promotes fibril formation associated with synucleinopathies (1,2,5). Recent studies also suggest that alpha-synuclein accumulation can prevent mitochondrial import machinery causing mitochondrial dysfunction that is often observed in neurodegeneration (5). It is thought that preventing alpha-synuclein aggregation may prevent PD, thus alpha-synuclein is a target for many potential therapeutic interventions aimed at decreasing aggregate formation or increasing clearance (1,2,4-6).

References

1. Villar-Pique, A., Lopes da Fonseca, T., & Outeiro, T. F. (2016). Structure, function and toxicity of alpha-synuclein: the Bermuda triangle in synucleinopathies. Journal of neurochemistry. https://doi.org/10.1111/jnc.13249

2. Emamzadeh F. N. (2016). Alpha-synuclein structure, functions, and interactions. Journal of research in medical sciences : the official journal of Isfahan University of Medical Sciences. https://doi.org/10.4103/1735-1995.181989

3. Burre J. (2015). The Synaptic Function of alpha-Synuclein. Journal of Parkinson's disease. https://doi.org/10.3233/JPD-150642

4. Lashuel, H. A., Overk, C. R., Oueslati, A., & Masliah, E. (2013). The many faces of alpha-synuclein: from structure and toxicity to therapeutic target. Nature reviews. Neuroscience. https://doi.org/10.1038/nrn3406

5. Rocha, E. M., De Miranda, B., & Sanders, L. H. (2018). Alpha-synuclein: Pathology, mitochondrial dysfunction and neuroinflammation in Parkinson's disease. Neurobiology of disease. https://doi.org/10.1016/j.nbd.2017.04.004

6. O'Leary, E. I., & Lee, J. C. (2019). Interplay between alpha-synuclein amyloid formation and membrane structure. Biochimica et biophysica acta. Proteins and proteomics. https://doi.org/10.1016/j.bbapap.2018.09.012

Alternate Names

NACP, PARK1, PARK4, SNCA, Synuclein-alpha

Gene Symbol

SNCA

Additional alpha-Synuclein Products

Product Documents for alpha-Synuclein [p Ser129] Antibody - Azide and BSA Free

Product Datasheets

Certificate of Analysis

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Product Specific Notices for alpha-Synuclein [p Ser129] Antibody - Azide and BSA Free

This product is for research use only and is not approved for use in humans or in clinical diagnosis. Primary Antibodies are guaranteed for 1 year from date of receipt.

⚠ WARNING: This product can expose you to chemicals including Methotrexate, which is known to the State of California to cause reproductive toxicity with developmental effects. For more information, go to www.P65Warnings.ca.gov

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