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AB42906

Anti-Alpha-synuclein (phospho S129) antibody

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(1 Review)

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(2 Publications)

Rabbit Polyclonal Alpha-synuclein phospho S129 antibody. Suitable for WB and reacts with Rat samples. Cited in 2 publications. Immunogen corresponding to Synthetic Peptide within Rat Snca phospho S129.

View Alternative Names

Alpha-synuclein, Snca

1 Images
Western blot - Anti-Alpha-synuclein (phospho S129) antibody (AB42906)
  • WB

Unknown

Western blot - Anti-Alpha-synuclein (phospho S129) antibody (AB42906)

Western blot of rat cortex lysate showing specific labelling of the ~15kDa alpha Synuclein protein phosphorylated at serine 129, using ab42906 at a 1/1000 dilution. Immunolabeling is blocked by the phosphopeptide (peptide) used as immunogen.

All lanes:

Western blot - Anti-Alpha-synuclein (phospho S129) antibody (ab42906) at 1/1000 dilution

Lane 1:

Rat cortex lysate at 20 µg

Lane 2:

Rat cortex lysate with immunogenic peptide 1ng

Predicted band size: 14 kDa

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Key facts

Host species

Rabbit

Clonality

Polyclonal

Isotype

IgG

Carrier free

No

Reacts with

Rat

Applications

WB

applications

Immunogen

Synthetic Peptide within Rat Snca phospho S129. The exact immunogen used to generate this antibody is proprietary information.

P37377

Specificity

This antibody is specific for the 15 kDa alpha Synuclein protein phosphorylated at serine 129. Immunolabelling is blocked by the phosphopeptide used as an antigen but not by the corresponding dephosphopeptide.

Reactivity data

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Properties and storage information

Form
Liquid
Purification technique
Affinity purification Immunogen
Purification notes
Prepared from rabbit serum by affinity purification via sequential chromatography on phosph- and dephosphopeptide affinity columns.
Storage buffer
pH: 7.5 Constituents: 50% Glycerol (glycerin, glycerine), 0.87% Sodium chloride, 0.238% HEPES, 0.01% BSA
Shipped at conditions
Blue Ice
Appropriate short-term storage conditions
+4°C
Appropriate long-term storage conditions
-20°C
Aliquoting information
Upon delivery aliquot
Storage information
Avoid freeze / thaw cycle

Supplementary information

This supplementary information is collated from multiple sources and compiled automatically.

Alpha-synuclein often referred to by alternate names such as SNCA is a protein of around 14 kDa mass. It mainly expresses in the brain particularly in presynaptic nerve terminals. This protein functions mechanically by stabilizing synaptic vesicles and maintaining synaptic function. It exists both in soluble monomer forms and as aggregates in protein filaments. Antibodies like 4D6 and EP1536Y target monomer forms of protein for more detailed studies.
Biological function summary

The alpha-synuclein protein plays critical roles in neuronal activity. It contributes to neurotransmitter release regulation by acting in the formation and plasticity of the presynaptic neuronal network. Alpha-synuclein doesn't usually form parts of large protein complexes but it may associate transiently with membranes and vesicular structures. The protein's monomer form has also been observed in alpha lines and related neuronal processes operating alongside various cellular functions.

Pathways

Synaptic vesicle trafficking and dopamine neurotransmitter release are significant areas involving the alpha-synuclein protein. In these pathways alpha-synuclein interacts with other proteins like synaptophysin and protein monomer monomerizations are intrinsic to these processes. Altered function or aggregation of alpha-synuclein disrupts these pathways influencing broader neurological functions.

Alterations or accumulations of alpha-synuclein are strongly linked to Parkinson's disease and Lewy body dementia. In these conditions alpha-synuclein forms abnormal protein filaments known as Lewy bodies within neurons. These formations disrupt cellular processes and neuron health. Synucleinopathies such as these show connections with proteins like parkin and DJ-1 which also have key roles in these neurodegenerative diseases.

Product protocols

For this product, it's our understanding that no specific protocols are required. You can visit:

Target data

Neuronal protein that plays several roles in synaptic activity such as regulation of synaptic vesicle trafficking and subsequent neurotransmitter release (By similarity). Participates as a monomer in synaptic vesicle exocytosis by enhancing vesicle priming, fusion and dilation of exocytotic fusion pores (By similarity). Mechanistically, acts by increasing local Ca(2+) release from microdomains which is essential for the enhancement of ATP-induced exocytosis (By similarity). Acts also as a molecular chaperone in its multimeric membrane-bound state, assisting in the folding of synaptic fusion components called SNAREs (Soluble NSF Attachment Protein REceptors) at presynaptic plasma membrane in conjunction with cysteine string protein-alpha/DNAJC5 (By similarity). This chaperone activity is important to sustain normal SNARE-complex assembly during aging (By similarity). Also plays a role in the regulation of the dopamine neurotransmission by associating with the dopamine transporter (DAT1) and thereby modulating its activity (By similarity).
See full target information Snca phospho S129

Publications (2)

Recent publications for all applications. Explore the full list and refine your search

Scientific reports 7:16386 PubMed29180624

2017

Alpha-synuclein facilitates to form short unconventional microtubules that have a unique function in the axonal transport.

Applications

Unspecified application

Species

Unspecified reactive species

Shiori Toba,Mingyue Jin,Masami Yamada,Kanako Kumamoto,Sakiko Matsumoto,Takuo Yasunaga,Yuko Fukunaga,Atsuo Miyazawa,Sakiko Fujita,Kyoko Itoh,Shinji Fushiki,Hiroaki Kojima,Hideki Wanibuchi,Yoshiyuki Arai,Takeharu Nagai,Shinji Hirotsune

Journal of neurochemistry 122:812-22 PubMed22639889

2012

Potential role of α-synuclein in neurodegeneration: studies in a rat animal model.

Applications

Unspecified application

Species

Unspecified reactive species

George Stoica,Gina Lungu,Nicole L Bjorklund,Giulio Taglialatela,Xing Zhang,Veronica Chiu,Herbert H Hill,James O Schenk,Ian Murray
View all publications

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