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anti-SNCA antibody :: Synuclein, alpha Monoclonal Antibody

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Catalog # MBS312186
Unit / Price
  0.2 mL  /  $1,070 +1 FREE 8GB USB
anti-SNCA antibody
Product Name

Synuclein, alpha (SNCA), Monoclonal Antibody

Also Known As

MAb to Synuclein Alpha

Product Synonym Names
Monoclonal Antibody to Human Synuclein alpha
Research Use Only
For Research Use Only. Not for use in diagnostic procedures.
Chromosome Location
Chromosome: 4; NC_000004.11 (90645250..90759447, complement). Location: 4q21
OMIM
127750
3D Structure
ModBase 3D Structure for P37840
Clonality
Monoclonal
Isotype
IgG1
Clone Number
4D6
Host
Host: Mouse
Source: Tissue Culture Supernatant
Specificity
Synuclein, alpha
Reacts well with alpha-synuclein in Western blots and frozen and formalin-fixed/paraffin-embedded tissue sections. Recognizes human alpha-synuclein. Synuclein-alpha is the major component of Lewy bodies and Lewy neuritis in sporadic PD
Purity/Purification
Protein A chromatography
Form/Format
Purified, Liquid
Concentration
1mg/ml (lot specific)
Immunogen
Purified E. coli produced human alpha-synuclein
Affinity Constant
Not determined
Buffer
PBS
Preservative
No
Dry Ice Shipment
Extra charge fee may add to your shipping cost as dry ice is required to ship this product.
Important Note
Centrifuge before opening to ensure complete recovery of vial contents.
Preparation and Storage
Store at -20 degree C. Aliquot to avoid multiple freeze/thaw cycles.
ISO Certification
Manufactured in an ISO 9001:2008 Certified Laboratory.
Other Notes
Small volumes of anti-SNCA antibody vial(s) may occasionally become entrapped in the seal of the product vial during shipment and storage. If necessary, briefly centrifuge the vial on a tabletop centrifuge to dislodge any liquid in the container`s cap. Certain products may require to ship with dry ice and additional dry ice fee may apply.
Applications Tested/Suitable for anti-SNCA antibody
EIA/ELISA, Immunohistochemistry - Formalin/Paraffin, Western Blot
NCBI/Uniprot data below describe general gene information for SNCA. It may not necessarily be applicable to this product.
NCBI GI #
NCBI GeneID
UniProt Primary Accession #
UniProt Secondary Accession #
UniProt Related Accession #
Molecular Weight
14,460 Da[Similar Products]
NCBI Official Full Name
synuclein alpha
NCBI Official Synonym Full Names
synuclein, alpha (non A4 component of amyloid precursor)
NCBI Official Symbol
NCBI Official Synonym Symbols
PD1; NACP; PARK1; PARK4; MGC110988
  [Similar Products]
NCBI Protein Information
alpha-synuclein; OTTHUMP00000161559; OTTHUMP00000161560; OTTHUMP00000161561; OTTHUMP00000218549; OTTHUMP00000218550; OTTHUMP00000218551; OTTHUMP00000218552; OTTHUMP00000218553; non-A4 component of amyloid; alpha-synuclein, isoform NACP140; non A-beta component of AD amyloid; non-A beta component of AD amyloid; Parkinson disease (autosomal dominant, Lewy body) 4
UniProt Protein Name
Alpha-synuclein
UniProt Synonym Protein Names
Non-A beta component of AD amyloid; Non-A4 component of amyloid precursor
Protein Family
UniProt Gene Name
UniProt Synonym Gene Names
NACP; PARK1  [Similar Products]
UniProt Entry Name
SYUA_HUMAN
NCBI Summary for SNCA
Alpha-synuclein is a member of the synuclein family, which also includes beta- and gamma-synuclein. Synucleins are abundantly expressed in the brain and alpha- and beta-synuclein inhibit phospholipase D2 selectively. SNCA may serve to integrate presynaptic signaling and membrane trafficking. Defects in SNCA have been implicated in the pathogenesis of Parkinson disease. SNCA peptides are a major component of amyloid plaques in the brains of patients with Alzheimer's disease. Four alternatively spliced transcripts encoding two different isoforms have been identified for this gene. [provided by RefSeq]
UniProt Comments for SNCA
Function: May be involved in the regulation of dopamine release and transport. Induces fibrillization of microtubule-associated protein tau. Reduces neuronal responsiveness to various apoptotic stimuli, leading to a decreased caspase-3 activation.

Subunit structure: Soluble monomer which can form filamentous aggregates. Interacts with UCHL1

By similarity. Interacts with phospholipase D and histones. Ref.15 Ref.16

Subcellular location: Cytoplasm. Membrane. Nucleus. Cell junction › synapse. Note: Membrane-bound in dopaminergic neurons. Ref.16

Tissue specificity: Expressed principally in brain but is also expressed in low concentrations in all tissues examined except in liver. Concentrated in presynaptic nerve terminals.

Domain: The 'non A-beta component of Alzheimer disease amyloid plaque' domain (NAC domain) is involved in fibrils formation. The middle hydrophobic region forms the core of the filaments. The C-terminus may regulate aggregation and determine the diameter of the filaments. Ref.21

Post-translational modification: Phosphorylated, predominantly on serine residues. Phosphorylation by CK1 appears to occur on residues distinct from the residue phosphorylated by other kinases. Phosphorylation of Ser-129 is selective and extensive in synucleinopathy lesions. In vitro, phosphorylation at Ser-129 promoted insoluble fibril formation. Phosphorylated on Tyr-125 by a PTK2B-dependent pathway upon osmotic stress. Ref.13 Ref.14 Ref.19Hallmark lesions of neurodegenerative synucleinopathies contain alpha-synuclein that is modified by nitration of tyrosine residues and possibly by dityrosine cross-linking to generated stable oligomers.Ubiquitinated. The predominant conjugate is the diubiquitinated form

Involvement in disease: Note=Genetic alterations of SNCA resulting in aberrant polymerization into fibrils, are associated with several neurodegenerative diseases (synucleinopathies). SNCA fibrillar aggregates represent the major non A-beta component of Alzheimer disease amyloid plaque, and a major component of Lewy body inclusions. They are also found within Lewy body (LB)-like intraneuronal inclusions, glial inclusions and axonal spheroids in neurodegeneration with brain iron accumulation type 1.Defects in SNCA are the cause of Parkinson disease type 1 (PARK1) [

MIM:168601]. A complex neurodegenerative disorder characterized by bradykinesia, resting tremor, muscular rigidity and postural instability. Additional features are characteristic postural abnormalities, dysautonomia, dystonic cramps, and dementia. The pathology of Parkinson disease involves the loss of dopaminergic neurons in the substantia nigra and the presence of Lewy bodies (intraneuronal accumulations of aggregated proteins), in surviving neurons in various areas of the brain. The disease is progressive and usually manifests after the age of 50 years, although early-onset cases (before 50 years) are known. The majority of the cases are sporadic suggesting a multifactorial etiology based on environmental and genetic factors. However, some patients present with a positive family history for the disease. Familial forms of the disease usually begin at earlier ages and are associated with atypical clinical features. Ref.24 Ref.25 Ref.26Defects in SNCA are the cause of Parkinson disease type 4 (PARK4) [

MIM:605543]. A complex neurodegenerative disorder with manifestations ranging from typical Parkinson disease to dementia with Lewy bodies. Clinical features include parkinsonian symptoms (tremor, rigidity, postural instability and bradykinesia), dementia, diffuse Lewy body pathology, autonomic dysfunction, hallucinations and paranoia.Defects in SNCA are the cause of dementia Lewy body (DLB) [

MIM:127750]. A neurodegenerative disorder clinically characterized by mental impairment leading to dementia, parkinsonism, often with fluctuating cognitive function, visual hallucinations, falls, syncopal episodes, and sensitivity to neuroleptic medication. Brainstem or cortical intraneuronal accumulations of aggregated proteins (Lewy bodies) are the only essential pathologic features. Patients may also have hippocampal and neocortical senile plaques, sometimes in sufficient number to fulfill the diagnostic criteria for Alzheimer disease.

Sequence similarities: Belongs to the synuclein family.
Product References and Citations for anti-SNCA antibody
• Lucking, C.B., et al., (2000), "Alpha-synuclein and Parkinson's disease", Cell Mol. Life Sci., 57(13-14): 1894-1908.
• Trojanowski, J.Q., et al., (2000), "Fatal attractions of proteins. A comprehensive hypothetical mechanism under

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