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AB17041

Human Alpha-synuclein peptide

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Human Alpha-synuclein peptide is a Synthetic blocking peptide. >90% and suitable for BL.

View Alternative Names

NACP, PARK1, SNCA, Alpha-synuclein, Non-A beta component of AD amyloid, Non-A4 component of amyloid precursor

1 Images
ELISA - Human Alpha-synuclein peptide (AB17041)
  • ELISA

Unknown

ELISA - Human Alpha-synuclein peptide (AB17041)

ab10789 gave a positive result in ELISA against the immunising peptide (ab17030, blue line). It gave a negative result in ELISA against the non-modified equivalent peptide (ab17041, red line). This indicates that it is specific for the modified peptide. Not yet tested in other applications.

Key facts

Purity

>90% HPLC

Tags

Tag free

Applications

BL

applications

Biologically active

No

Accession

P37840

Animal free

No

Carrier free

No

Species

Human

Storage buffer

Constituents: HEPES, 0.87% Sodium chloride, 0.0584% EDTA, 0.001% Sorbitan monolaurate, ethoxylated

storage-buffer

Reactivity data

{ "title": "Reactivity Data", "filters": { "stats": ["", "Reactivity", "Dilution Info", "Notes"] }, "values": { "BL": { "reactivity":"TESTED_AND_REACTS", "dilution-info":"", "notes":"<p>This peptide can be used with studies using <a href='/en-us/products/primary-antibodies/alpha-synuclein-phospho-y125-antibody-ab10789'>ab10789</a> and <a href='/en-us/products/unavailable/human-alpha-synuclein-phospho-y125-peptide-ab17030'>ab17030</a>.</p>" } } }

Product details

- First try to dissolve a small amount of peptide in either water or buffer. The more charged residues on a peptide, the more soluble it is in aqueous solutions.
- If the peptide doesn't dissolve try an organic solvent e.g. DMSO, then dilute using water or buffer.
- Consider that any solvent used must be compatible with your assay. If a peptide does not dissolve and you need to recover it, lyophilise to remove the solvent.
- Gentle warming and sonication can effectively aid peptide solubilisation. If the solution is cloudy or has gelled the peptide may be in suspension rather than solubilised.
- Peptides containing cysteine are easily oxidised, so should be prepared in solution just prior to use.

Sequence info

[{"sequence":null,"proteinLength":null,"predictedMolecularWeight":null,"actualMolecularWeight":null,"aminoAcidEnd":0,"aminoAcidStart":0,"nature":"Synthetic","expressionSystem":null,"accessionNumber":"P37840","tags":[]}]

Properties and storage information

Shipped at conditions
Blue Ice
Appropriate short-term storage conditions
-20°C
Appropriate long-term storage conditions
-20°C
Aliquoting information
Upon delivery aliquot
Storage information
Avoid freeze / thaw cycle
False

Specifications

Form

Liquid

General info

Function

Neuronal protein that plays several roles in synaptic activity such as regulation of synaptic vesicle trafficking and subsequent neurotransmitter release (PubMed : 20798282, PubMed : 26442590, PubMed : 28288128, PubMed : 30404828). 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 Ca(2+) release from microdomains which is essential for the enhancement of ATP-induced exocytosis (PubMed : 30404828). 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 (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).

Sequence similarities

Belongs to the synuclein family.

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.

Product protocols

Target data

Neuronal protein that plays several roles in synaptic activity such as regulation of synaptic vesicle trafficking and subsequent neurotransmitter release (PubMed : 20798282, PubMed : 26442590, PubMed : 28288128, PubMed : 30404828). 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 Ca(2+) release from microdomains which is essential for the enhancement of ATP-induced exocytosis (PubMed : 30404828). 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 (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).
See full target information SNCA

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