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α-Synuclein (61–95) is a 35-amino-acid fragment corresponding to the central non-Aβ component (NAC) region of human α-synuclein. This hydrophobic region plays an important role in α-synuclein self-association and contains sequence elements that contribute to β-sheet-rich oligomer and fibril formation.
The historical term NAC arose from early studies of Alzheimer-associated amyloid material. Today, this sequence is more appropriately positioned within α-synuclein aggregation, Parkinson’s disease, Lewy body and protein-misfolding research. The NAC sequence corresponds to residues 61–95 of α-synuclein.
Product Information
| Property | Specification |
|---|---|
| Product Name | α-Synuclein (61–95), Human |
| Synonym | NAC Peptide |
| Sequence | EQVTNVGGAVVTGVTAVAQKTVEGAGSIAAATGFV |
| Length | 35 amino acids |
| Molecular Formula | C141H235N39O49 |
| Theoretical MW | ~3260.65 Da |
| Origin | Human α-synuclein residues 61–95 |
| Peptide Type | Aggregation-prone synuclein fragment |
| Research Focus | α-Synuclein aggregation, fibrillation, Parkinson’s disease, protein misfolding |
| Purity | From crude to 98% |
Why the NAC Region Is Experimentally Useful
Full-length α-synuclein contains 140 residues and exhibits complex conformational behavior. Studying the isolated NAC region allows researchers to focus on one of the principal aggregation-prone segments without introducing the complete protein.
Synthetic NAC peptide can be used in fibrillation studies, cross-seeding experiments, peptide–membrane interaction assays and structure–activity studies examining residues involved in self-association.
Sample Preparation Matters
Aggregation state can vary substantially with solvent history, concentration, ionic strength, temperature and incubation time.
For quantitative comparisons, We recommend keeping sample preparation consistent across peptide lots and analogs rather than treating nominal HPLC purity as the only experimental variable.
Custom NAC variants, labeled derivatives and residue substitutions can be evaluated through Custom Peptide Synthesis. Analytical identity and purity can be supported through Peptide Quality Control.
Frequently Asked Questions
What is the NAC region of α-synuclein?
The NAC region is a hydrophobic segment within human α-synuclein that contributes strongly to peptide self-association and fibril formation. The commonly studied NAC fragment corresponds to α-synuclein residues 61–95 and contains 35 amino acids.
Why is α-synuclein (61–95) used in aggregation research?
The isolated NAC sequence allows researchers to study one of the principal aggregation-prone regions of α-synuclein without using the full 140-amino-acid protein. It is useful for investigating fibril nucleation, amyloid assembly, cross-seeding, membrane interactions, and sequence-specific aggregation mechanisms.
Is NAC an amyloid-β peptide?
No. The historical name “non-Aβ component” came from its early identification in amyloid preparations, but NAC is derived from α-synuclein, not amyloid-β precursor protein. It should therefore be distinguished clearly from Aβ40, Aβ42, and other APP-derived amyloid peptides.
Is α-synuclein (61–95) mainly relevant to Alzheimer’s or Parkinson’s research?
Although the NAC terminology originated in Alzheimer-associated amyloid studies, current research relevance is much stronger in α-synuclein aggregation, Parkinson’s disease, Lewy body biology, and synucleinopathies.
Research Use Only.