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Molecular structure

2D reference
Sequence-derived 2D chemical structure of Alpha-Synuclein fragment (61–80), 20 amino-acid residues.
Linear reference chainView full size
Reference sequence20 residues
EQVTNVGGAVVTGVTAVAQK

Sequence-derived chemical connectivity. Free N terminus and C-terminal acid; no specific 3D fold is implied.

PL-SYN-023 Synuclein peptides & proteins

Alpha-Synuclein fragment (61–80)

$64.99

Human alpha-synuclein fragment (61–80), comprising 20 amino acids for comparative laboratory studies of protein conformation and sequence-dependent molecular association.

In stock

SKU: PL-SYN-023 Category:

Technical identity

Catalog ID
PL-SYN-023
Construct
Human alpha-synuclein residues 61–80
Reference sequence
EQVTNVGGAVVTGVTAVAQK
Calculated reference mass
1928.17 Da — calculated average mass of the unmodified free-acid chain; not a measured result. Tags, termini, modifications, counterions and disulfides change the actual mass.
Reference modifications
Unmodified reference chain

Reference identity: UniProt P37840. Calculated mass describes the reference chain and does not replace a measured lot result.

Documentation

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For qualified organizational in vitro research only. Purchasing access is available to approved research organizations.

Description

Alpha-Synuclein fragment (61–80) is a 20-amino-acid peptide fragment corresponding to human alpha-synuclein residues 61–80. Alpha-synuclein is encoded by the SNCA gene; the reference sequence is recorded as UniProt P37840. Sequence reference: UniProt P37840.

Research context

This chain includes the central non-amyloid-beta component (NAC) region at parent-sequence residues 61–80. The fragment’s 61–80 boundary defines which portions of the parent sequence are present. Comparisons with the 1–140 chain or overlapping fragments can investigate the contribution of those regions to conformation, molecular recognition, and self-association.

Alpha-synuclein is a neuronal protein associated with synaptic vesicle biology. Its molecular association and assembly into amyloid structures are central topics in Parkinson’s disease and synucleinopathy research. Studies distinguish the functions of the N-terminal, NAC, and C-terminal regions and examine how substitutions or truncations change their relationships within the protein. Research reference.

Research applications

  • Comparative characterization of full-length and truncated alpha-synuclein sequences.
  • Mapping regional contributions to protein association and conformational behavior.
  • Biophysical studies of alpha-synuclein-derived chains in defined in vitro systems.

Molecular identity

  • Catalog ID: PL-SYN-023
  • Product type: Peptide
  • Reference species: Human (Homo sapiens)
  • Sequence length: 20 amino acids
  • Reference region: Human alpha-synuclein residues 61–80
  • Calculated average molecular mass: 1,928.17 Da for the unmodified free-acid reference chain
  • Sequence modification: Unmodified reference sequence

Reference sequence

EQVTNVGGAVVTGVTAVAQK

For in vitro laboratory research only. Not for human or animal administration.

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