alpha Synuclein antibody (20-SG70)
Goat polyclonal alpha Synuclein antibody
|Synonyms||Polyclonal alpha Synuclein antibody, Anti-alpha Synuclein antibody, Synuclein antibody, aSynuclein antibody|
|Specificity||Human alpha synuclein|
|Cross Reactivity||To be determined by end-user|
|Immunogen||Alpha Synuclein antibody was raised in goat using a peptide; MPVDPDNEAYEMPSEE, as the immunogen.|
|Form & Buffer||Supplied as liquid neat serum without preservative.|
Usage & Assay Information
|Usage Recommendations||ELISA: >1:1,500, IHC-F: >1:5,000, IHC-P: >1:100|
Storage & Safety
|Storage||Store at 4 deg C for short term storage. Aliquot and store at -20 deg C for long term storage. Avoid repeated freeze/thaw cycles.|
Product Uses: Polyclonal SNCA antibody specific for human alpha Synuclein for use in ELISA and Immunohistochemistry.
Biological Significance: 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. Although the function of SNCA is not well understood, studies suggest that it plays an important role in maintaining a supply of synaptic vesicles in presynaptic terminals. It may also help regulate the release of dopamine, a type of neurotransmitter that is critical for controlling the start and stop of voluntary and involuntary movements. SNCA may serve to integrate presynaptic signaling and membrane trafficking. SNCA Induces fibrillization ofmicrotubule-associated protein tau and reduces neuronal responsiveness to various apoptotic stimuli, leading to a decreased caspase-3 activation.
Expression: SNCA is expressed principally in brain and also in low concentrations in all tissues. It is highly concentrated in presynaptic nerve terminals.
Tissue and Cell Localization: SNCA is abundant in the human brain. Smaller amounts are found in the heart, muscles, and other tissues. In the brain, alpha-synuclein is found mainly at the tips of nerve cells (neurons) in specialized structures called presynaptic terminals. Within these structures, alpha-synuclein interacts with phospholipids and proteins.
Implications in Disease: 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. SNCA defects have also been linked to REM sleep behavior disorder.
Sequence Information: Alpha-synuclein primary structure is usually divided in three distinct domains: Residues 1-60: An amphipathic N-terminal region dominated by four 11-residue repeats including the consensus sequence KTKEGV. This sequence has a structural alpha helix propensity similar to apolipoproteins-binding domains. Residues 61-95: A central hydrophobic region which includes the non-amyloid-β component (NAC) region, involved in protein aggregation. Residues 96-140: a highly acidic and proline-rich region which has no distinct structural propensity.
Post-Translational Modifications: SNCA is 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. Glycosylation occurs at Thr54. Acetylation at Met-1 seems to be important for proper folding and native oligomeric structure.
Database References: Entrez Gene: 6622 Human, Omim: 163890 Human, SwissProt: P37840 Human, Unigene: 21374 Human
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