Synuclein, alpha (SNCA) (pTyr136) antibody

Details for Product No. ABIN401576
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Antigen
Synonyms snca, MGC64356, LOC619283, NACP, alphaSYN, PARK1, PARK4, PD1
Epitope
pTyr136
(51), (42), (39), (35), (34), (16), (12), (10), (8), (7), (7), (6), (6), (6), (5), (5), (4), (3), (3), (2), (2), (2), (2), (2), (2), (2), (2), (1), (1), (1), (1), (1), (1), (1), (1), (1), (1), (1), (1), (1), (1), (1), (1), (1), (1), (1)
Reactivity
Human, Mouse (Murine), Rat (Rattus)
(452), (207), (196), (80), (77), (66), (24), (12), (3), (1), (1), (1)
Host
Rabbit
(363), (87), (14), (11), (2), (1)
Clonality
Polyclonal
Conjugate
Un-conjugated
(15), (11), (11), (7), (7), (7), (7), (7), (7), (7), (7)
Application
Immunofluorescence (IF), Western Blotting (WB)
(340), (152), (90), (87), (84), (70), (28), (21), (19), (16), (14), (6), (3), (1), (1), (1)
Pubmed 4 references available
Quantity 0.1 mg
Shipping to United States (Change)
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Catalog No. ABIN401576
357.50 $
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Immunogen Peptide Sequence around the phosphorylation site of Tyr136 (Q-D-Yp-E-P) derived from Human Alpha-Synuclein
Specificity This antibody detects endogenous levels of Alpha-Synuclein only when phosphorylated at Tyrosine 136.
Purification Immunoaffinity 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
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
Application Notes Western Blot: 1/500approx. 1/1000. Immunofluorescence: 1/100approx. 1/200.
Other applications not tested.
Optimal dilutions are dependent on conditions and should be determined by the user.
Restrictions For Research Use only
Concentration 1.0 mg/mL
Buffer PBS (without Mg2+ and Ca2+), pH 7.4, 150 mM NaCl, 0.02 % Sodium Azide and 50 % Glycerol.
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
anti-Synuclein, alpha (SNCA) (pTyr136) antibody anti-Synuclein, alpha (SNCA) (pTyr136) antibody
anti-Synuclein, alpha (SNCA) (pTyr136) antibody (2) anti-Synuclein, alpha (SNCA) (pTyr136) antibody (Image 2)
Background publications 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).

Negro, Brunati, Donella-Deana et al.: "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).

Takahashi, Yamashita, Nagano et al.: "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).

Chen, Chang, Liao et al.: "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).

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