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| Description | Cyclization constrains the APP 96-110 epitope into a rigid native-like conformation, improving stability for epitope mimicry, antibody/protein binding and conformation-function studies. |
Product Basic Information Table
| Product Standard English Name | Product Abbreviation / Alias | Function Tags (comma-separated) | Core Structure (Sequence) | Molecular Formula | Exact Mass (Da) | Average MW (Da) | Salt Form | Length (aa) |
| β-Amyloid precursor protein (96-110), cyclized, human (human APP residues 96–110, 15-mer, Ac-NWCKGRRKQCKTHPH-NH₂, Cys3–Cys10 intramolecular disulfide cyclization) | APP(96-110) cyclized; Amyloid Precursor Protein 96-110; Ac-NWCKGRRKQCKTHPH-NH₂; APP GFLD cyclic peptide; β-APP (96-110) | β-amyloid precursor protein (APP), APP(96-110), cyclic peptide, disulfide-stabilized conformation, N-acetylation/C-amidation, KKRR basic cluster, heparan sulfate binding, cell adhesion, APP processing, protease resistance | Cyclized 15-mer: Ac-Asn-Trp-Cys-Lys-Arg-Gly-Arg-Lys-Gln-Cys-Lys-Thr-His-Pro-His-NH₂; N-acetylated (Ac-) and C-amidated (-NH₂); an intramolecular disulfide bond (-S-S-) between Cys3 and Cys10 cyclizes the peptide; contains a strong basic cluster (KKRR, around residues 4–7) that is a heparin/heparan sulfate proteoglycan (HSPG) binding motif; two histidines (His13/His15) and Pro14 confer a turn conformation; the disulfide locks the conformation, markedly increasing resistance to proteolysis and biological stability | C81H128N32O19S2 | 1916.95 | 1918.22 | TFA salt / Free base (cyclized disulfide, N-acetylated, C-amidated); CAS 289634-54-4 | 15 |
Physicochemical Solubility & Storage Parameters
| Product Code | Appearance | Long-term Storage | Short-term Storage | Solution Stability | Solid Powder Stability |
| PEP-APP96110-01 | White powder | Store at −20°C, sealed, desiccated, protected from light; aliquot to avoid repeated freeze-thaw, ~2 years. Cyclic disulfide peptides should be protected from prolonged oxidizing/reducing environments; keep sealed and dark to prevent disulfide exchange and oxidation. | 2–8°C for ~2 weeks; working aliquots at −80°C; avoid prolonged room-temperature exposure; prepare fresh when possible. | Good water solubility due to the KKRR basic cluster; readily dissolved in water or PBS buffer; the cyclic conformation keeps it stable in aqueous phase and resistant to aggregation. Dissolve in water or buffer (pH 5–7) at 0.1–1 mM; in solution keep at 4°C for ≤1 week or aliquot at −80°C; avoid repeated freeze-thaw; avoid strong reducing agents (e.g. DTT, β-mercaptoethanol) that would break the Cys3–Cys10 disulfide cyclization. | solid stable for ~2 years at −20°C, sealed, desiccated, protected from light; hygroscopic, store dry and dark; the disulfide bond is sensitive to both reducing and oxidizing environments, avoid repeated opening to air. |
Functional Description
| Product Code | Frontend Short Summary | Detailed Biological Function Description | Applicable Research Areas (comma-separated) | Targets / Receptors |
| PEP-APP96110-01 | Human APP(96-110) cyclized synthetic peptide, N-acetylated and C-amidated, with an intramolecular Cys3–Cys10 disulfide bond and a KKRR heparin-binding basic cluster; conformationally locked and protease-resistant; used for studies of the APP growth factor-like domain (GFLD), heparan sulfate binding, cell adhesion and APP processing; white powder with good water solubility, store at −20°C in aliquots. | β-Amyloid precursor protein (APP) is a type I transmembrane glycoprotein whose extracellular region contains a growth factor-like domain (GFLD) stabilized by two disulfide bonds and involved in neuronal cell adhesion, neurite outgrowth and synapse formation. APP(96-110) corresponds to a highly conserved basic loop within the APP GFLD; the sequence NWCKGRRKQCKTHPH is highly conserved across human, mouse and other species. Oxidizing Cys3 and Cys10 into an intramolecular disulfide cyclizes the peptide into a small loop of ~8 residues, mimicking the native disulfide-stabilized β-hairpin/loop conformation of the GFLD. N-acetylation and C-amidation eliminate terminal charges, further enhancing peptide stability and resistance to proteolysis. This loop region is rich in Lys/Arg (forming a KKRR-like basic cluster near K2R3K5) and is the key site by which APP binds heparin and heparan sulfate proteoglycans (HSPGs); APP mediates cell–matrix adhesion, neurite extension and cell-surface signaling through GFLD–HSPG interactions. In addition, the cyclic APP(96-110) peptide can serve as: (1) a mimotope of the APP GFLD conformational epitope for structure–function studies; (2) a positive ligand for heparin/HSPG binding assays investigating APP–extracellular matrix interactions; (3) an immunogen or epitope-mapping tool for anti-APP GFLD antibodies; (4) a tool peptide for APP processing (α/β/γ-secretase cleavage) and APP metabolism studies; and (5) a functional peptide in cell adhesion, neurite outgrowth and synapse formation assays. Because cyclization locks the conformation, this peptide is more resistant to trypsin, chymotrypsin and other serum proteases than linear analogues, giving a longer half-life and more homogeneous conformation in cell culture and in vitro assays-particularly suited for structural biology (NMR/crystallography) and biophysical binding experiments (ITC, SPR). | Alzheimer's disease (AD), APP biology, APP growth factor-like domain (GFLD), heparin/heparan sulfate (HSPG) binding, cell adhesion/neurite outgrowth, synapse formation, anti-APP antibody epitope mapping, structural biology (NMR/crystallography), APP processing and metabolism | Heparin/heparan sulfate proteoglycans (HSPGs); APP GFLD domain; cell-surface adhesion molecules; disulfide-stabilized β-hairpin conformational epitope |
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