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Molecular structure

2D reference
Sequence-derived 2D chemical structure of Human IAPP reference fragment (8–37), free-acid chain, 30 amino-acid residues.
Linear reference chainView full size
Reference sequence30 residues
ATQRLANFLVHSSNNFGAILSSTNVGSNTY

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

PL-AMY-005 Amylin / IAPP peptides

Human IAPP reference fragment (8–37), free-acid chain

$54.99

Human IAPP/amylin sequence fragment (8–37), comprising 30 amino acids in the linear free-acid reference form for sequence-focused laboratory research.

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SKU: PL-AMY-005 Category:

Technical identity

Catalog ID
PL-AMY-005
Construct
Mature human IAPP-relative residues 8–37; precursor P10997 residues 41–70
Reference sequence
ATQRLANFLVHSSNNFGAILSSTNVGSNTY
Calculated reference mass
3184.47 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
Linear free-acid reference design. Native IAPP has a disulfide and C-terminal amidation; those features are not asserted for this planned entry. Actual chemical form requires supplier confirmation.

Reference identity: UniProt P10997. 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

Human IAPP reference fragment (8–37), free-acid chain is a 30-amino-acid peptide corresponding to residues 8–37 of the mature human islet amyloid polypeptide (IAPP) sequence, also called amylin. These positions map to residues 41–70 of the IAPP precursor, UniProt P10997. Sequence reference: UniProt P10997.

Research context

The 8–37 boundaries isolate a specific part of the 37-residue mature IAPP sequence. The fragment begins with alanine and ends with tyrosine, defining the terminal residues used for comparisons with longer and overlapping IAPP-derived peptides. It contains the NFGAIL segment at mature IAPP residues 22–27, a sequence examined in studies of amyloid-core assembly. The reference form shown on this page has a free N terminus and a C-terminal carboxylic acid, with cysteines represented as unlinked thiols where present. Native mature amylin has a C-terminal amide and a disulfide bond between cysteines 2 and 7; this entry identifies the linear free-acid chain.

IAPP is a peptide associated with pancreatic islet biology and islet amyloid research. Studies of IAPP-derived fragments examine how particular sequence regions contribute to peptide association and amyloid assembly. Defined linear chains also allow analytical comparisons that keep amino-acid sequence, terminal chemistry, and native post-translational features distinct. Research reference.

Research applications

  • Comparing IAPP-derived peptide lengths and terminal boundaries.
  • Investigating sequence contributions to peptide association and assembly.
  • Analytical characterization of linear free-acid IAPP reference chains.

Molecular identity

  • Catalog ID: PL-AMY-005
  • Product type: Peptide
  • Reference species: Human (Homo sapiens)
  • Sequence length: 30 amino acids
  • Reference region: Mature human IAPP-relative residues 8–37; precursor P10997 residues 41–70
  • Calculated average molecular mass: 3,184.47 Da for the unmodified free-acid reference chain
  • Sequence modification: Unmodified reference sequence
  • Reference chemistry: Linear chain; free N terminus and C-terminal acid

Reference sequence

ATQRLANFLVHSSNNFGAILSSTNVGSNTY

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

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