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IN VITRO LABORATORY RESEARCH ONLYQualified research organizations · No human or animal administration

Molecular structure

2D reference
Sequence-derived 2D chemical structure of APP770 fragment (660–680), 21 amino-acid residues.
Linear reference chainView full size
Reference sequence21 residues
NIKTEEISEVKMDAEFRHDSG

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

PL-APP-010 APP-related materials

APP770 fragment (660–680)

$54.99

Human APP770 fragment spanning residues 660–680, comprising 21 amino acids for laboratory studies of APP-derived sequences, fragment boundaries, and regional molecular interactions.

In stock

SKU: PL-APP-010 Category:

Technical identity

Catalog ID
PL-APP-010
Construct
Human APP canonical 770-residue isoform, residues 660–680
Reference sequence
NIKTEEISEVKMDAEFRHDSG
Calculated reference mass
2435.65 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 (660–680) is a 21-amino-acid peptide fragment corresponding to residues 660–680 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 fragment crosses the boundary at APP770 residue 672, the N-terminal start of the Aβ sequence. It combines residues upstream of that boundary with an N-terminal portion of Aβ, providing a defined local sequence for research on APP processing regions and molecular recognition.

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-010
  • Product type: Peptide
  • Reference species: Human (Homo sapiens)
  • Sequence length: 21 amino acids
  • Reference region: Human APP canonical 770-residue isoform, residues 660–680
  • Calculated average molecular mass: 2,435.65 Da for the unmodified free-acid reference chain
  • Sequence modification: Unmodified reference sequence

Reference sequence

NIKTEEISEVKMDAEFRHDSG

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

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