Human SNCA protein (Recombinant-Active) (N-His) (STJP012580)
SPECIFICATIONS
HostE.coli
ConjugationUnconjugated
ImmunogenHomo sapiens (Human)
General Information
| Short Description | Recombinant-Active-Human SNCA-N-His protein was developed from e.coli and has a target region of N-His. For use in research applications. |
| Applications | ELISA/WB |
| Host | E.coli |
| Note | STRICTLY FOR FURTHER SCIENTIFIC RESEARCH USE ONLY (RUO). MUST NOT BE USED IN DIAGNOSTIC OR THERAPEUTIC APPLICATIONS. |
Product Properties
| Conjugation | Unconjugated |
| Dilution Range | Reconstitute in sterile water for a stock solution. |
| Formulation | Lyophilized from a 0.22 Mu m filtered solution in 20mM PB, 150mM NaCl, pH 7.4. |
| Storage Instruction | Use a manual defrost freezer and avoid repeated freeze thaw cycles. Store at 2 to 8ยฐC for one week. Store at-20 to-80ยฐC for twelve months from the date of receipt. |
| Endotoxin | < 1 EU/ยตg as determined by LAL test. |
Target Information
| Gene Symbol | SNCA |
| Gene ID | 6622 |
| Uniprot ID | SYUA_HUMAN |
| Immunogen | Homo sapiens (Human) |
| Immunogen Region | Met1-Ala140 |
Additional Info
| Post Translational Modifications | 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. |
| Function | 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. Also acts 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. Also plays a role in the regulation of the dopamine neurotransmission by associating with the dopamine transporter (DAT1) and thereby modulating its activity. |
| Protein Name | Alpha-SynucleinNon-A Beta Component Of Ad AmyloidNon-A4 Component Of Amyloid PrecursorNacp |
| Database Links | Reactome: R-HSA-977225Reactome: R-HSA-9833482 |
| Cellular Localisation | CytoplasmMembraneNucleusSynapseSecretedCell ProjectionAxonMembrane-Bound In Dopaminergic NeuronsExpressed And Colocalized With Septin4 In Dopaminergic Axon TerminalsEspecially At The Varicosities |
| Alternative Protein Names | Alpha-Synuclein proteinNon-A Beta Component Of Ad Amyloid proteinNon-A4 Component Of Amyloid Precursor proteinNacp proteinSNCA proteinNACP proteinPARK1 protein |
Information sourced from Uniprot.org