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

Molecular structure

2D reference
Sequence-derived 2D chemical structure of APP770 fragment (751–770), 20 amino-acid residues.
Linear reference chainView full size
Reference sequence20 residues
KMQQNGYENPTYKFFEQMQN

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

PL-APP-014 APP-related materials

APP770 fragment (751–770)

$199.99

Human APP770 fragment spanning residues 751–770, comprising 20 amino acids for laboratory studies of APP-derived sequences, fragment boundaries, and regional molecular interactions.

In stock

SKU: PL-APP-014 Category:

Technical identity

Catalog ID
PL-APP-014
Construct
Human APP canonical 770-residue isoform, residues 751–770
Reference sequence
KMQQNGYENPTYKFFEQMQN
Calculated reference mass
2525.79 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

For specification, analytical-record or handling questions, contact our team with the product name or catalog ID.

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

Description

APP770 fragment (751–770) is a 20-amino-acid peptide fragment corresponding to residues 751–770 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 maps to the C-terminal intracellular portion of APP770. The 751–770 sequence defines a particular part of the APP tail for comparisons with longer C-terminal chains and overlapping fragments in region-specific molecular interaction studies. It retains the YENPTY motif at APP770 residues 757–762, a region involved in interactions with intracellular adaptor proteins.

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-014
  • Product type: Peptide
  • Reference species: Human (Homo sapiens)
  • Sequence length: 20 amino acids
  • Reference region: Human APP canonical 770-residue isoform, residues 751–770
  • Calculated average molecular mass: 2,525.79 Da for the unmodified free-acid reference chain
  • Sequence modification: Unmodified reference sequence

Reference sequence

KMQQNGYENPTYKFFEQMQN

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