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MABN826

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Anti-phospho-α-Synuclein (Ser129) Antibody, clone 81A

clone 81A, from mouse

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Synonym(s):
Alpha-synuclein, NACP, Non-A beta component of AD amyloid, Non-A4 component of amyloid precursor, Synuclein alpha-140
eCl@ss:
32160702
NACRES:
NA.41

biological source

mouse

Quality Level

antibody form

purified antibody

antibody product type

primary antibodies

clone

81A, monoclonal

species reactivity

mouse, human

technique(s)

electron microscopy: suitable
immunocytochemistry: suitable
immunofluorescence: suitable
immunohistochemistry: suitable (paraffin)
western blot: suitable

isotype

IgG2aκ

NCBI accession no.

UniProt accession no.

shipped in

dry ice

target post-translational modification

phosphorylation (pSer129)

Gene Information

human ... SNCA(6622)

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AB5038

Anti-Synuclein α Antibody

species reactivity

mouse, human

species reactivity

human

species reactivity

rat, human

species reactivity

rat, human, mouse

Gene Information

human ... SNCA(6622)

Gene Information

human ... SNCA(6622)

Gene Information

human ... SNCA(6622)

Gene Information

human ... SNCA(6622)

antibody form

purified antibody

antibody form

purified immunoglobulin

antibody form

serum

antibody form

purified immunoglobulin

biological source

mouse

biological source

mouse

biological source

rabbit

biological source

mouse

UniProt accession no.

P37840

UniProt accession no.

P37840

UniProt accession no.

P37840

UniProt accession no.

P37840

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General description

Alpha-synuclein (UniProt P37840; also known as NACP, Non-A beta component of AD amyloid, Non-A4 component of amyloid precursor, Synuclein alpha-140) is encoded by the SNCA (also known as NACP, PARK1, PARK4) gene (Gene ID 6622) in human. Pathological aggregates are common features of many neurodegenerative diseases, such as tau neurofibrillary tangles (NFTs) in Alzheimer’s disease (AD) and frontotemporal degeneration, and α-synuclein (α-syn) Lewy bodies (LBs) in Parkinson’s disease (PD) and dementia with LB (DLB). Alpha-synuclein is a phospholipid-binding protein concentrated in presynaptic terminals where it promotes SNARE complex formation and modulates synaptic functions. Alpha-synuclein is the major component of pathologic inclusions that characterize PD, DLB, and multiple system atrophy (MSA). Both casein kinase-1 (CK-1) and CK-2 can catalyze the phosphorylation of alpha-synuclein on Ser129, and Ser129-phosphorylated alpha-synuclein is found in alpha-synuclein inclusions.

Specificity

Clone 81A detected CK1- and CK2-catalyzed alpha-synuclein Ser129 phosphorylation, but not CK1-catalyzed alpha-synuclein Ser87 phosphorylation, nor non-phosphorylated alpha-synuclein (Waxman, E.A., et al. (2008). J. Neuropathol. Exp. Neurol. 67(5):402-416).

Immunogen

Epitope: pSer129
KLH-conjugated linear peptide corresponding a human α-synuclein sequence with the phosphorylated Ser129.

Application

Detect phospho-α-Synuclein using this Anti-phospho-α-Synuclein (Ser129) Antibody, clone 81A validated for use in Electron Microscopy, Immunocytochemistry, Immunofluorescence, Immunohistochemistry (Paraffin), Western Blotting.
Immunohistochemistry Analysis: A 1:250-1,000 dilution from a representative lot detected α-synuclein pSer129 immunoreactivity associated with pathologic inclusions in M83 transgenic mouse brain and human PD brian.
Immunocytochemistry Analysis: A representative lot detected Ser129-phosphorylated α-synuclein in Lewy bodies-/LB- and Lewy-neurite-/LN-like inclusions in cultured embryonic hippocampal neurons from wild-type mice and mice carrying human mutant P301S tau transgene, but not Snca-/- mice, upon exposure to preformed α-synuclein fibrils (pffs) from C-terminally truncated, Myc-tagged α-synuclein (Guo, J.L., and Giasson, B.I. (2013). Cell. 154(1):103-117).
Electron Microscopy Analysis: A representative lot detected phosphorylated α-synuclein in close physical associations of tau in filamentous structures within neuronal processes of human P301S mutant tau transgenic mouse embryo hippocampal neurons exposed to α-synuclein fibrils formed by repeated rounds of self-seeding using C-terminally truncated, Myc-tagged α-synuclein (Guo, J.L., and Giasson, B.I. (2013). Cell. 154(1):103-117).
Western Blotting Analysis: A representative lot detected phosphorylation of the Triton-insoluble α-synuclein formed in cultured mouse embryonic hippocampal neurons upon exposure to preformed α-synuclein fibrils (pffs) from C-terminally truncated, Myc-tagged α-synuclein (Guo, J.L., and Giasson, B.I. (2013). Cell. 154(1):103-117).
Western Blotting Analysis: A representative lot detected Ser129 phosphorylation of Triton-insoluble, but not Triton-soluble, α-synuclein in the cingulate cortex extracts from DLB (dementia with Lewy bodies) patients and the cerebella extracts from patients with multiple systems atrophy (MSA) (Waxman, E.A., et al. (2008). J. Neuropathol. Exp. Neurol. 67(5):402-416).
Western Blotting Analysis: A representative lot detected CK1- and CK2-catalyzed alpha-synuclein Ser129 phosphorylation, but not CK1-catalyzed α-synuclein Ser87 phosphorylation, nor non-phosphorylated α-synuclein (Waxman, E.A., et al. (2008). J. Neuropathol. Exp. Neurol. 67(5):402-416).
Immunohistochemistry Analysis: A representative lot detected pathologic inclusions-associated α-synuclein Ser129 phosphorylation in paraffin-embedded brain tissue sections from patients with PD (Parkinson′s disease), DLB (dementia with Lewy bodies) and MSA (multiple systems atrophy), while clone 81A detected no α-synuclein Ser129 phosphorylation associated with neurofibrillary tangles in the hippocampus of a patient with Alzheimer′s disease (Waxman, E.A., et al. (2008). J. Neuropathol. Exp. Neurol. 67(5):402-416).
Immunofluorescence Analysis: A representative lot detected pathologic inclusions-associated α-synuclein Ser129 phosphorylation by fluorescent immunohistochemistry in paraffin-embedded cingulate cortex sections from a patient with LB variant of Alzheimer′s disease (LBVAD) and in the cerebellum sections from a patient with multiple systems atrophy (MSA) (Waxman, E.A., et al. (2008). J. Neuropathol. Exp. Neurol. 67(5):402-416).

Note: Incubating the transferred membrane with a combination of 4% paraformaldehyde and 0.01 ~ 0.1% glutaraldehyde is reported to produce an approximately 10-fold increase in the detection sensitivity of α-synuclein Ser129 phosphorylation by Western blotting. If not fixed, α-synuclein monomers can detach from the transferred membrane during incubation (Sasaki, A., et al. (2015). Sci. Rep. 5:14211).
Research Category
Neuroscience
Research Sub Category
Neurodegenerative Diseases

Quality

Identity Confirmation by Isotyping Test.

Isotyping Analysis: The identity of this monoclonal antibody is confirmed by isotyping test to be IgG2aκ.

Target description

14.46 kDa calculated.

Physical form

Format: Purified
Protein G Purified
Purified mouse monoclonal IgG2aκ in buffer containing 0.1 M Tris-Glycine (pH 7.4), 150 mM NaCl with 0.05% sodium azide.

Storage and Stability

Stable for 1 year at 2-8°C from date of receipt.

Disclaimer

Unless otherwise stated in our catalog or other company documentation accompanying the product(s), our products are intended for research use only and are not to be used for any other purpose, which includes but is not limited to, unauthorized commercial uses, in vitro diagnostic uses, ex vivo or in vivo therapeutic uses or any type of consumption or application to humans or animals.

Storage Class

12 - Non Combustible Liquids

wgk_germany

WGK 1

flash_point_f

Not applicable

flash_point_c

Not applicable


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Alberto Delaidelli et al.
Acta neuropathologica communications, 9(1), 105-105 (2021-06-08)
Circumstantial evidence points to a pathological role of alpha-synuclein (aSyn; gene symbol SNCA), conferred by aSyn misfolding and aggregation, in Parkinson disease (PD) and related synucleinopathies. Several findings in experimental models implicate perturbations in the tissue homeostatic mechanisms triggered by
Sonja Fixemer et al.
Acta neuropathologica communications, 10(1), 36-36 (2022-03-18)
The cellular alterations of the hippocampus lead to memory decline, a shared symptom between Alzheimer's disease (AD) and dementia with Lewy Bodies (DLB) patients. However, the subregional deterioration pattern of the hippocampus differs between AD and DLB with the CA1
Marta Jorge-Oliva et al.
Alzheimer's research & therapy, 14(1), 187-187 (2022-12-15)
Granulovacuolar degeneration bodies (GVBs) are intracellular vesicular structures that commonly accompany pathological tau accumulations in neurons of patients with tauopathies. Recently, we developed the first model for GVBs in primary neurons, that requires exogenous tau seeds to elicit tau aggregation.
null
Nelson Ferreira et al.
Brain communications, 3(2), fcab104-fcab104 (2021-06-18)
Neuropathological observations in neurodegenerative synucleinopathies, including Parkinson disease, implicate a pathological role of α-synuclein accumulation in extranigral sites during the prodromal phase of the disease. In a transgenic mouse model of peripheral-to-central neuroinvasion and propagation of α-synuclein pathology (via hindlimb

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