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Molecular structure

2D reference
Sequence-derived 2D chemical structure of APP770 fragment (649–671), 23 amino-acid residues.
Linear reference chainView full size
Reference sequence23 residues
GLTTRPGSGLTNIKTEEISEVKM

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

PL-APP-008 APP-related materials

APP770 fragment (649–671)

$89.99

Human APP770 fragment spanning residues 649–671, comprising 23 amino acids for laboratory studies of APP-derived sequences, fragment boundaries, and regional molecular interactions.

In stock

SKU: PL-APP-008 Category:

Technical identity

Catalog ID
PL-APP-008
Construct
Human APP canonical 770-residue isoform, residues 649–671
Reference sequence
GLTTRPGSGLTNIKTEEISEVKM
Calculated reference mass
2461.81 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 P05067. 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

APP770 fragment (649–671) is a 23-amino-acid peptide fragment corresponding to residues 649–671 of human amyloid precursor protein isoform APP770. Numbering follows the 770-residue reference sequence in UniProt P05067, allowing this fragment to be aligned directly with other APP-derived materials. Sequence reference: UniProt P05067.

Research context

This sequence lies immediately upstream of the Aβ region, which begins at APP770 residue 672. The 649–671 boundaries define an extracellular, cleavage-site-adjacent APP segment for sequence mapping and comparisons with neighboring fragments. Its sequence retains the amino-acid order of that specific region of the parent protein.

APP is a membrane protein whose proteolytic processing produces multiple extracellular and C-terminal fragments, including amyloid-beta peptides. APP research examines how local sequence, cleavage boundaries, and interactions within the C-terminal tail relate to protein processing and signaling. Individual fragments provide defined sequences for studying selected parts of this broader molecular system. Research reference.

Research applications

  • Mapping defined APP770 sequence regions and fragment boundaries.
  • Comparative characterization of overlapping APP-derived chains.
  • Investigating region-specific molecular recognition and protein-interaction sequences.

Molecular identity

  • Catalog ID: PL-APP-008
  • Product type: Peptide
  • Reference species: Human (Homo sapiens)
  • Sequence length: 23 amino acids
  • Reference region: Human APP canonical 770-residue isoform, residues 649–671
  • Calculated average molecular mass: 2,461.81 Da for the unmodified free-acid reference chain
  • Sequence modification: Unmodified reference sequence

Reference sequence

GLTTRPGSGLTNIKTEEISEVKM

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

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