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| Description | From Glu22 (mutation hotspot) to Met35, covering the second half of the central region to the hydrophobic start; TFA salt for conformational switching and elongation studies. |
Product Basic Information Table
| Standard English Name | Abbreviations/Aliases | Functional Tags | Structural Core | Molecular Formula | Exact MW (Da) | Average MW (Da) | Salt Form | Length (aa) |
| β-Amyloid (22-35) human TFA (human Aβ mid-domain 22-35 14-mer fragment, TFA salt; sequence EDVGSNKGAIIGLM, contains Asp23 near the Dutch/Iowa mutation hotspots and oxidizable Met35) | Aβ(22-35); EDVGSNKGAIIGLM; mid-domain fragment; Dutch/Iowa mutation region | β-amyloid peptide, mid-domain 22-35, Asp23 (Dutch/Iowa mutation site), GSNKGAIIGLM, Met35, familial AD mutation model, cerebral amyloid angiopathy (CAA) | Linear 14-mer EDVGSNKGAIIGLM, spanning Glu22-Asp23-Val24-Gly25-Ser26-Asn27-Lys28-Gly29-Ala30-Ile31-Ile32-Gly33-Leu34-Met35; Asp23 lies near the Dutch (E22Q) / Iowa (D23N) mutation hotspots; Gly29-Ala30-Ile31-Ile32-Gly33-Leu34 is the hydrophobic mid-segment; C-terminal contains oxidizable Met35 | C59H102N16O21S1 | 1402.71 | 1403.61 | TFA salt / powder | 14 |
Physicochemical Solubility & Storage Parameters
| Product Code | Appearance | Long-term Storage | Short-term Storage | Solution Stability | Solid Stability |
| PEP-AB2235-01 | White to off-white powder | Store at −20°C, sealed, desiccated, protected from light; aliquot into single-use portions to avoid repeated freeze-thaw, ~2 years; contains oxidizable Met35, storage under argon/nitrogen preferred. | 2–8°C for ~1 week; working aliquots at −80°C; avoid room-temperature exposure; ship on dry ice/blue ice. | Contains charged residues; intermediate water solubility; the hydrophobic GAIIGLM mid-segment has strong aggregation tendency; first dissolve in a small amount of DMSO at 1–2 mM, then dilute with PBS/buffer; keep solutions at 4°C for ≤24 h or aliquot and store at −80°C; Met35 is readily oxidized-prepare fresh and keep under argon. | solid stable for ~2 years at −20°C, sealed, desiccated and protected from light; highly hygroscopic and aggregation-prone, store dry under inert gas, protected from light; contains oxidizable Met35, keep dark, dry and at −20°C. |
Functional Description
| Product Code | Short Summary (listing) | Detailed Biological Function | Research Areas | Targets/Receptors |
| PEP-AB2235-01 | Human Aβ mid-domain 22-35 14-mer (TFA salt), sequence EDVGSNKGAIIGLM. Covers the region adjacent to familial AD mutation hotspots Dutch (E22Q)/Iowa (D23N), the hydrophobic GAIIGLM mid-segment, and the oxidizable C-terminal Met35. Used to study how mid-domain familial mutations affect aggregation rate and neurotoxicity, Met35 oxidation, and cerebral amyloid angiopathy (CAA). Intermediate water solubility; DMSO cosolvent recommended. | Aβ(22-35) (EDVGSNKGAIIGLM) spans the Aβ mid-domain, connecting the N-terminal hydrophilic segment (1-16), the central hydrophobic core KLVFF (17-20) and the strongly hydrophobic C-terminal transmembrane segment (29-42). Its key biological significance lies in covering several mutation hotspots associated with early-onset familial Alzheimer's disease (EOFAD) and cerebral amyloid angiopathy (CAA): Glu22 and Asp23 are the loci or immediate neighbors of the Dutch (E22Q), Iowa (D23N), Arctic (E22G), Italian (E22K) and Flemish (A21G) mutations. These familial mutations markedly alter the charge distribution and conformation of the Aβ mid-segment: the Dutch mutation (E22Q) removes the Glu22 negative charge, making Aβ more prone to deposit in cerebrovascular walls causing CAA; the Iowa mutation (D23N) removes the Asp23 negative charge, markedly accelerating Aβ aggregation and enhancing neurotoxicity; the Arctic mutation (E22G) increases flexibility and promotes fibril secondary nucleation. Aβ(22-35) retains these mutation sites, the hydrophobic Gly29-Ala30-Ile31-Ile32-Gly33-Leu34 mid-segment, and the C-terminal oxidizable Met35; it retains partial aggregation propensity and is an ideal short-peptide model for studying how mid-domain familial mutations affect Aβ aggregation rate, fibril structure and neurotoxicity. Main applications include: (1) in vitro models of how Dutch/Iowa/Arctic/Italian/Flemish familial mutations affect Aβ aggregation kinetics and CAA-like deposition; (2) the effect of the Met35 redox state on mid-domain conformation and aggregation; (3) studies of mid-domain charge distribution and pH sensitivity (protonation of Asp23 near physiological pH modulates aggregation); (4) screening of mid-domain-targeted aggregation inhibitors/antibodies; and (5) structural and toxicity studies of Aβ fragments relevant to vascular AD and cerebral amyloid angiopathy (CAA). Supplied as TFA-salt powder with intermediate water solubility due to charged residues; first dissolve in a small amount of DMSO, then dilute with buffer. | Alzheimer's disease (AD), familial Aβ mutations (Dutch/Iowa/Arctic/Italian/Flemish), Met35 oxidation, mid-domain aggregation, cerebral amyloid angiopathy (CAA), pH-sensitive aggregation, mid-domain-targeted inhibitors | Aβ mid-domain (22-35); familial mutation sites (E22Q/D23N/E22G/E22K/A21G etc.); Met35 redox site; GAIIGLM hydrophobic mid-segment |
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