AFfirm™ Synuclein alpha Mouse Monoclonal Antibody - #BF8041
Product Info
*The optimal dilutions should be determined by the end user.
*Tips:
WB: For western blot detection of denatured protein samples. IHC: For immunohistochemical detection of paraffin sections (IHC-p) or frozen sections (IHC-f) of tissue samples. IF/ICC: For immunofluorescence detection of cell samples. ELISA(peptide): For ELISA detection of antigenic peptide.
Fold/Unfold
Alpha synuclein; Alpha-synuclein; Alpha-synuclein, isoform NACP140; alphaSYN; MGC105443; MGC110988; MGC127560; MGC64356; NACP; Non A beta component of AD amyloid; Non A4 component of amyloid; Non A4 component of amyloid precursor; Non-A beta component of AD amyloid; Non-A-beta component of alzheimers disease amyloid , precursor of; Non-A4 component of amyloid precursor; Non-A4 component of amyloid, precursor of; OTTHUMP00000218549; OTTHUMP00000218551; OTTHUMP00000218552; OTTHUMP00000218553; OTTHUMP00000218554; PARK 1; PARK 4; PARK1; PARK4; Parkinson disease (autosomal dominant, Lewy body) 4; Parkinson disease familial 1; SNCA; Snca synuclein, alpha (non A4 component of amyloid precursor); SYN; Synuclein alpha; Synuclein alpha 140; Synuclein, alpha (non A4 component of amyloid precursor); SYUA_HUMAN;
Immunogens
A synthesized peptide derived from human Synuclein alpha, corresponding to a region within C-terminal amino acids.
Highly expressed in presynaptic terminals in the central nervous system. Expressed principally in brain.
- P37840 SYUA_HUMAN:
- Protein BLAST With
- NCBI/
- ExPASy/
- Uniprot
MDVFMKGLSKAKEGVVAAAEKTKQGVAEAAGKTKEGVLYVGSKTKEGVVHGVATVAEKTKEQVTNVGGAVVTGVTAVAQKTVEGAGSIAAATGFVKKDQLGKNEEGAPQEGILEDMPVDPDNEAYEMPSEEGYQDYEPEA
PTMs - P37840 As Substrate
| Site | PTM Type | Enzyme | Source |
|---|---|---|---|
| Ubiquitination | Uniprot | ||
| M1 | Acetylation | Uniprot | |
| K6 | Sumoylation | Uniprot | |
| K10 | Sumoylation | Uniprot | |
| K12 | Sumoylation | Uniprot | |
| K12 | Ubiquitination | Uniprot | |
| K21 | Acetylation | Uniprot | |
| K21 | Sumoylation | Uniprot | |
| K21 | Ubiquitination | Uniprot | |
| K23 | Sumoylation | Uniprot | |
| K23 | Ubiquitination | Uniprot | |
| K34 | Sumoylation | Uniprot | |
| Y39 | Phosphorylation | Uniprot | |
| S42 | Phosphorylation | Uniprot | |
| K45 | Sumoylation | Uniprot | |
| T54 | O-Glycosylation | Uniprot | |
| K58 | Acetylation | Uniprot | |
| K60 | Sumoylation | Uniprot | |
| K80 | Sumoylation | Uniprot | |
| S87 | O-Glycosylation | Uniprot | |
| S87 | Phosphorylation | P48729 (CSNK1A1) , P68400 (CSNK2A1) , Q13627 (DYRK1A) | Uniprot |
| K96 | Acetylation | Uniprot | |
| K96 | Sumoylation | Uniprot | |
| K102 | Sumoylation | Uniprot | |
| Y125 | Phosphorylation | P06241 (FYN) , Q14289 (PTK2B) , P12931 (SRC) , P43405 (SYK) | Uniprot |
| S129 | Phosphorylation | P68400 (CSNK2A1) , P49841 (GSK3B) , P53350 (PLK1) , Q5S007 (LRRK2) , P25098 (GRK2) , P34947 (GRK5) , P48729 (CSNK1A1) , Q9UQM7 (CAMK2A) , P43250 (GRK6) , Q9H4B4 (PLK3) , Q9NYY3 (PLK2) | Uniprot |
| Y133 | Phosphorylation | P43405 (SYK) | Uniprot |
| Y136 | Phosphorylation | P43405 (SYK) | Uniprot |
Research Backgrounds
Neuronal protein that plays several roles in synaptic activity such as regulation of synaptic vesicle trafficking and subsequent neurotransmitter release. Participates as a monomer in synaptic vesicle exocytosis by enhancing vesicle priming, fusion and dilation of exocytotic fusion pores. Mechanistically, acts by increasing local Ca(2+) release from microdomains which is essential for the enhancement of ATP-induced exocytosis. Acts also as a molecular chaperone in its multimeric membrane-bound state, assisting in the folding of synaptic fusion components called SNAREs (Soluble NSF Attachment Protein REceptors) at presynaptic plasma membrane in conjunction with cysteine string protein-alpha/DNAJC5. This chaperone activity is important to sustain normal SNARE-complex assembly during aging. Plays also a role in the regulation of the dopamine neurotransmission by associating with the dopamine transporter (DAT1) and thereby modulating its activity.
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.
Hallmark 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 (By similarity).
Acetylation at Met-1 seems to be important for proper folding and native oligomeric structure.
Cytoplasm. Membrane. Nucleus. Cell junction>Synapse. Secreted.
Note: Membrane-bound in dopaminergic neurons.
Highly expressed in presynaptic terminals in the central nervous system. Expressed principally in brain.
Soluble monomer. Homotetramer. A dynamic intracellular population of tetramers and monomers coexists normally and the tetramer plays an essential role in maintaining homeostasis. Interacts with UCHL1 (By similarity). Interacts with phospholipase D and histones. Interacts (via N-terminus) with synphilin-1/SNCAIP; this interaction promotes formation of SNCA inclusions in the cytoplasm. Interacts with CALM1. Interacts with STXBP1; this interaction controls SNCA self-replicating aggregation. Interacts with SNARE components VAMP2 and SNAP25; these interactions allows SNARE complex assembly and integrity. Interacts with RPH3A and RAB3A. Interacts with SERF1A; this interaction promotes the aggregation of SNCA.
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.
Belongs to the synuclein family.
Research Fields
· Human Diseases > Neurodegenerative diseases > Alzheimer's disease.
· Human Diseases > Neurodegenerative diseases > Parkinson's disease.
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