MABN826
Anti-phospho-α-Synuclein (Ser129) Antibody, clone 81A
clone 81A, from mouse
Synonim(y):
Alpha-synuclein, NACP, Non-A beta component of AD amyloid, Non-A4 component of amyloid precursor, Synuclein alpha-140
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About This Item
Kod UNSPSC:
12352203
eCl@ss:
32160702
NACRES:
NA.41
Polecane produkty
pochodzenie biologiczne
mouse
Poziom jakości
forma przeciwciała
purified antibody
rodzaj przeciwciała
primary antibodies
klon
81A, monoclonal
reaktywność gatunkowa
mouse, human
metody
electron microscopy: suitable
immunocytochemistry: suitable
immunofluorescence: suitable
immunohistochemistry: suitable (paraffin)
western blot: suitable
izotyp
IgG2aκ
numer dostępu NCBI
numer dostępu UniProt
Warunki transportu
dry ice
docelowa modyfikacja potranslacyjna
phosphorylation (pSer129)
informacje o genach
human ... SNCA(6622)
Opis ogólny
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.
Specyficzność
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.
Zastosowanie
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).
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
Neuroscience
Research Sub Category
Neurodegenerative Diseases
Neurodegenerative Diseases
Jakość
Identity Confirmation by Isotyping Test.
Isotyping Analysis: The identity of this monoclonal antibody is confirmed by isotyping test to be IgG2aκ.
Isotyping Analysis: The identity of this monoclonal antibody is confirmed by isotyping test to be IgG2aκ.
Opis wartości docelowych
14.46 kDa calculated.
Postać fizyczna
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.
Przechowywanie i stabilność
Stable for 1 year at 2-8°C from date of receipt.
Oświadczenie o zrzeczeniu się odpowiedzialności
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.
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Kod klasy składowania
12 - Non Combustible Liquids
Klasa zagrożenia wodnego (WGK)
WGK 1
Temperatura zapłonu (°F)
Not applicable
Temperatura zapłonu (°C)
Not applicable
Certyfikaty analizy (CoA)
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Dokumenty związane z niedawno zakupionymi produktami zostały zamieszczone w Bibliotece dokumentów.
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.
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
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
Lu-Lu Bu et al.
Frontiers in aging neuroscience, 12, 575481-575481 (2020-12-18)
Alpha-synuclein (α-Syn) is widely distributed and involved in the regulation of the nervous system. The phosphorylation of α-Syn at serine 129 (pSer129α-Syn) is known to be closely associated with α-Synucleinopathies, especially Parkinson's disease (PD). The present study aimed to explore
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