S5566
Anti-α-Synuclein antibody, Mouse monoclonal
clone Syn211, purified from hybridoma cell culture
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Synonym(s):
Anti-SNCA
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biological source
mouse
Quality Level
conjugate
unconjugated
antibody form
purified immunoglobulin
antibody product type
primary antibodies
clone
Syn211, monoclonal
form
buffered aqueous solution
mol wt
antigen 19 kDa
species reactivity
zebra finch, human
should not react with
rat, mouse
packaging
antibody small pack of 25 μL
concentration
~1 mg/mL
technique(s)
immunohistochemistry: suitable
immunoprecipitation (IP): suitable
western blot: 0.25 μg/mL using recombinant human α·-synuclein.
isotype
IgG1
UniProt accession no.
shipped in
dry ice
storage temp.
−20°C
target post-translational modification
unmodified
Gene Information
human ... SNCA(6622)
Related Categories
General description
The SNCA (synuclein α) gene codes for a 140-amino acid protein α-synuclein, that is mapped to human chromosome 4q21-23.
The SNCA (synuclein α) gene is mapped to human chromosome 4q22.1. The gene encodes a small synaptic protein called α-synuclein.
Immunogen
recombinant human α synuclein.
Application
Anti-α-Synuclein antibody, Mouse monoclonal has been used in western blotting and ELISA.
Applications in which this antibody has been used successfully, and the associated peer-reviewed papers, are given below.
Flow cytometry/Cell sorting (1 paper)
Immunocytochemistry (1 paper)
Flow cytometry/Cell sorting (1 paper)
Immunocytochemistry (1 paper)
Biochem/physiol Actions
Accumulation of α-synuclein in oligodendrocytes results in the loss of myelin and causes neurodegeneration, leading to multiple system atrophy. Synuclein-α is known to induce oligodendrocyte maturation. The encoded protein is considered to be an important aggregate of Lewy bodies, contributing to the pathogenesis of Parkinson disease.
Synuclein-α is known to induce oligodendrocyte maturation. Accumulation of α-synuclein in oligodendrocytes results in the loss of myelin and causes neurodegeneration, leading to multiple system atrophy. Mutations in the SNCA gene results in Parkinson′s disease.
Physical form
Solution in 0.01 M phosphate buffered saline pH 7.4, containing 1 % bovine serum albumin and 15 mM sodium azide.
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.
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Description
Pricing
WGK
WGK 3
Flash Point(F)
Not applicable
Flash Point(C)
Not applicable
Regulatory Information
常规特殊物品
含少量动物源组分生物产品
Certificates of Analysis (COA)
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Sabrina Büttner et al.
The EMBO journal, 32(23), 3041-3054 (2013-10-17)
Malfunctioning of the protein α-synuclein is critically involved in the demise of dopaminergic neurons relevant to Parkinson's disease. Nonetheless, the precise mechanisms explaining this pathogenic neuronal cell death remain elusive. Endonuclease G (EndoG) is a mitochondrially localized nuclease that triggers
α-synuclein in blood and brain from familial Parkinson disease with SNCA locus triplication.
Miller DW, et al.
Neurology, 62(10), 1835-1838 (2004)
Kavita Prasad et al.
Brain pathology (Zurich, Switzerland), 22(6), 811-825 (2012-03-29)
The role of Lewy bodies, Lewy neurites and α-synuclein (αSYN) in the pathophysiology and diagnosis of Parkinson's disease (PD) is unclear. We used postmortem human tissue, a panel of antibodies (Abs) and confocal microscopy to examine the three-dimensional neurochemical anatomy
Regional deficiencies in chaperone-mediated autophagy underlie α-synuclein aggregation and neurodegeneration
Malkus KA, et al.
Neurobiology of Disease, 46(3), 732-744 (2012)
Anna E Cartier et al.
PloS one, 7(4), e34713-e34713 (2012-04-20)
Parkinson's disease (PD) is a progressive neurodegenerative disorder caused by genetic and environmental factors. Abnormal accumulation and aggregation of alpha-synuclein (a-syn) within neurons, and mutations in the a-syn and UCH-L1 genes have been shown to play a role in the
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