Description | This recombinant anti-SNCA antibody (clone pC) recognizes α-synuclein (α-syn). pC showed binding only with α-syn fibrils and not with A-beta 42, tau or IAPP proteins, confirming its specificity towards α-syn fibrils. This antibody could inhibit the α-syn aggregation, α-syn seed-induced toxicity in a cell model of PD, and reduced the production of insoluble α-syn phosphorylated at Ser-129 (pS129-α-syn). |
Clonality | Monoclonal |
Host Species | Human |
Target Species | Human |
Function | Neuronal protein that plays several roles in synaptic activity such as regulation of synaptic vesicle trafficking and subsequent neurotransmitter release (PubMed: 28288128, PubMed: 30404828, PubMed: 20798282, PubMed: 26442590). Participates as a monomer in synaptic vesicle exocytosis by enhancing vesicle priming, fusion and dilation of exocytotic fusion pores (PubMed: 28288128, PubMed: 30404828). Mechanistically, acts by increasing local Ca2+ release from microdomains which is essential for the enhancement of ATP-induced exocytosis (PubMed: 30404828). 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 (PubMed: 20798282). This chaperone activity is important to sustain normal SNARE-complex assembly during aging (PubMed: 20798282). Also plays a role in the regulation of the dopamine neurotransmission by associating with the dopamine transporter (DAT1) and thereby modulating its activity (PubMed: 26442590). |
Isotype | Human IgG |
Expression Species | HEK293F or CHO cell line |
Conjugation | Unconjugated |
Purity | >95% |
Endotoxin | <1 EU/mg |
Form | Liquid |
Purification | Protein A purified |
Sterility | 0.2 μM filtered |
Formulation | PBS, pH 7.4 |
Preservation | No preservatives |
Stabilizer | No stabilizers |
Storage | Store at 4°C within a week. For longer storage, aliquot and store at -20°C. |
Application | ELISA; DB; WB; IHC |
Application Notes | The result of Dot Blot showed that pC (5 µg/mL) could bind with 250 ng α-syn fibrils. The result of Western Blot showed the inhibition of α-syn aggregation and the significant decrease of insoluble pS129-α-syn caused by this antibody. The result of Immunohistochemistry showed that pC could detect disease specific cytoplasmic granules in human post-mortem brain tissues. |
ELISA | Enzyme-Linked Immunosorbent Assay Protocol |
WB | Western Blot Protocol |
FC | Flow Cytometry Protocol |
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. 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. Acetylation at Met-1 seems to be important for proper folding and native oligomeric structure. |