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Molecular structure

2D reference
Sequence-derived 2D chemical structure of APP770 fragment (711–730), 20 amino-acid residues.
Linear reference chainView full size
Reference sequence20 residues
VIATVIVITLVMLKKKQYTS

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

PL-APP-012 APP-related materials

APP770 fragment (711–730)

$89.99

Human APP770 fragment spanning residues 711–730, comprising 20 amino acids for laboratory studies of APP-derived sequences, fragment boundaries, and regional molecular interactions.

In stock

SKU: PL-APP-012 Category:

Technical identity

Catalog ID
PL-APP-012
Construct
Human APP canonical 770-residue isoform, residues 711–730
Reference sequence
VIATVIVITLVMLKKKQYTS
Calculated reference mass
2248.84 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 (711–730) is a 20-amino-acid peptide fragment corresponding to residues 711–730 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 covers a C-terminal region of APP770 associated with the transition between the Aβ-containing membrane region and the intracellular tail. Its 711–730 boundaries identify the precise portion retained for comparisons with shorter fragments and other APP C-terminal sequences.

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-012
  • Product type: Peptide
  • Reference species: Human (Homo sapiens)
  • Sequence length: 20 amino acids
  • Reference region: Human APP canonical 770-residue isoform, residues 711–730
  • Calculated average molecular mass: 2,248.84 Da for the unmodified free-acid reference chain
  • Sequence modification: Unmodified reference sequence

Reference sequence

VIATVIVITLVMLKKKQYTS

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

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