SNCA antibody (Synuclein, alpha) (pSer129)

Details for Product anti-SNCA Antibody No. ABIN319236, Supplier: Log in to see
Antigen
  • snca
  • MGC64356
  • LOC619283
  • NACP
  • alphaSYN
  • PARK1
  • PARK4
  • PD1
  • synuclein, alpha
  • alpha-synuclein
  • synuclein, alpha (non A4 component of amyloid precursor)
  • snca
  • LOC619283
  • LOC100359228
  • Snca
  • SNCA
Alternatives
anti-Human SNCA antibody for Immunohistochemistry (Frozen Sections)
Epitope
pSer129
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Reactivity
Human, Mouse (Murine), Rat (Rattus)
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Host
Rabbit
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Clonality
Polyclonal
Conjugate
This SNCA antibody is un-conjugated
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Application
Immunofluorescence (IF), Immunohistochemistry (Paraffin-embedded Sections) (IHC (p)), Western Blotting (WB)
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Options
Supplier
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Supplier Product No.
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Immunogen Synthetic phosphopeptide derived from Human alpha-Synuclein around the phosphorylation site of Serine 129 (M-P-SP-E-E).
Specificity This antibody AP08013PU detects endogenous levels of alpha-Synuclein only when phosphorylated at Serine 129.
Purification Immunoaffinity Chromatography: The antibody was affinity-purified from rabbit antiserum by affinity-chromatography using epitope-specific phosphopeptide. The antibody against non-phosphopeptide was removed by chromatography using non-phosphopeptide corresponding to the phosphorylation site.
Alternative Name alpha-Synuclein / SNCA (SNCA Antibody Abstract)
Background Alpha Synuclein is implicated in the regulation of dopamine release and transport. It is a soluble protein, expressed principally in the brain but also expressed in low concentrations in all tissues examined (except liver). In the nervous system, alpha Synuclein is primarily located at presynaptic terminals and is found membrane bound in dopaminergic neurons. It can form filamentous aggregates that are the major non amyloid component of intracellular inclusions in several neurodegenerative diseases (synucleinopathies), including Parkinson's Disease. Alpha Synuclein induces fibrillization of microtubule associated protein tau and reduces neuronal responsiveness to various apoptotic stimuli, leading to a decreased caspase 3 activation. Alpha synuclein is a protein phosphorylated predominantly on serine residues.Synonyms: NACP, Non-A beta component of AD amyloid, Non-A4 component of amyloid precursor, PARK1
Gene ID 6622
NCBI Accession NP_000336
UniProt P37840
Research Area Neurology
Pathways Synaptic Membrane, Regulation of G-Protein Coupled Receptor Protein Signaling, Positive Regulation of Endopeptidase Activity, Regulation of Carbohydrate Metabolic Process, Platelet-derived growth Factor Receptor Signaling, Negative Regulation of Transporter Activity, Regulation of long-term Neuronal Synaptic Plasticity
Application Notes Western blot (1/500-1/1000).
Other applications not tested.
Optimal dilutions are dependent on conditions and should be determined by the user.
Restrictions For Research Use only
Format Liquid
Concentration 1.0 mg/mL
Buffer PBS (without Mg2+ and Ca2+), pH 7.4, 150 mM NaCl containing 0.02 % Sodium Azide as preservative and 50 % Glycerol as stabilizer.
Preservative Sodium azide
Precaution of Use This product contains sodium azide: a POISONOUS AND HAZARDOUS SUBSTANCE which should be handled by trained staff only.
Handling Advice Avoid repeated freezing and thawing.
Storage -20 °C
Storage Comment Store the antibody (in aliquots) at-20 °C.
Supplier Images
 image for anti-Synuclein, alpha (SNCA) (pSer129) antibody (ABIN319236) anti-Synuclein, alpha (SNCA) (pSer129) antibody
Background publications Chen, Chang, Liao, Chao: "Humidity effect on the decay of second-order nonlinearity in thermally poled fused silica." in: Optics express, Vol. 14, Issue 25, pp. 12334-40, 2009 (PubMed).

Takahashi, Yamashita, Nagano, Nakamura, Ohmori, Avraham, Avraham, Yasuda, Matsumoto: "Identification and characterization of a novel Pyk2/related adhesion focal tyrosine kinase-associated protein that inhibits alpha-synuclein phosphorylation." in: The Journal of biological chemistry, Vol. 278, Issue 43, pp. 42225-33, 2003 (PubMed).

Negro, Brunati, Donella-Deana, Massimino, Pinna: "Multiple phosphorylation of alpha-synuclein by protein tyrosine kinase Syk prevents eosin-induced aggregation." in: FASEB journal : official publication of the Federation of American Societies for Experimental Biology, Vol. 16, Issue 2, pp. 210-2, 2002 (PubMed).

Goldberg, Lansbury: "Is there a cause-and-effect relationship between alpha-synuclein fibrillization and Parkinson's disease?" in: Nature cell biology, Vol. 2, Issue 7, pp. E115-9, 2000 (PubMed).

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