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| Description | Aβ43 adds Thr43 beyond Aβ42, making it more hydrophobic, aggregation-prone and neurotoxic; enriched in plaques and Down-syndrome brain. TFA salt for aggregation/toxicity 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 (1-43) (human) TFA (full-length human amyloid-β residues 1–43, 43-mer, DAEFRHDSGYEVHHQKLVFFAEDVGSNKGAIIGLMVGGVVIAT; one extra Thr43 at the C-terminus versus Aβ(1-42)) | Aβ(1-43) human TFA; Amyloid β-Protein (1-43); Aβ43; DAEFRHDSGYEVHHQKLVFFAEDVGSNKGAIIGLMVGGVVIAT; β-Amyloid (1-43) TFA | β-amyloid peptide, Aβ(1-43), full-length variant, Alzheimer's disease, extra Thr43, strong aggregation, strong neurotoxicity, C-terminal extension, core senile-plaque component | Linear 43-mer; free N-terminal Asp and free C-terminal Thr carboxylic acid (-COOH); full-length human Aβ variant with one additional Thr43 at the C-terminus versus Aβ(1-42); contains the N-terminal charged/metal-binding region (1–16), central hydrophobic core LVFFA (17–21), the E22/D23 charged cluster (22–23) and the strongly hydrophobic C-terminal segment (29–43, GAIIGLMVGGVVIAT); aggregation propensity and neurotoxicity are stronger than those of Aβ(1-42) | C207H318N56O62S (free acid) | 4726.28 | 4729.17 | TFA salt (Trifluoroacetate) | 43 |
Physicochemical Solubility & Storage Parameters
| Product Code | Appearance | Long-term Storage | Short-term Storage | Solution Stability | Solid Powder Stability |
| PEP-AB143T-01 | White to off-white powder | Store at −20°C, sealed, desiccated, protected from light; aliquot to avoid repeated freeze-thaw, ~1–2 years. This full-length Aβ variant contains the complete hydrophobic core and an extended C-terminal hydrophobic region, and aggregates/fibrillizes even more readily than Aβ(1-42); immediate HFIP pre-treatment and aliquoting upon receipt are recommended. | 2–8°C for ≤1 week; working aliquots must be stored at −20°C (preferably −80°C); avoid room-temperature exposure; ship on dry ice. | Strongly hydrophobic full-length peptide with poor water solubility; spontaneously forms oligomers/fibrils faster and is more neurotoxic than Aβ(1-42). Handle by standard protocol: resuspend powder in hexafluoroisopropanol (HFIP) at 1–2 mM, sonicate/vortex to disrupt pre-aggregates, dry under nitrogen, reconstitute in DMSO or alkaline buffer (e.g., NaOH/ammonia), then dilute into PBS/buffer. In solution keep at 4°C for ≤24 h, aliquot and store at −20°C; avoid repeated freeze-thaw. | solid stable for ~1–2 years at −20°C, sealed, desiccated, protected from light; contains oxidizable Met35, so store dry, protected from light, under inert gas; HFIP pre-treatment and immediate aliquoting upon receipt to disrupt pre-aggregates. |
Functional Description
| Product Code | Frontend Short Summary | Detailed Biological Function Description | Applicable Research Areas (comma-separated) | Targets / Receptors |
| PEP-AB143T-01 | Full-length human Aβ(1-43) TFA salt 43-mer (DAEFRHDSGYEVHHQKLVFFAEDVGSNKGAIIGLMVGGVVIAT), carrying one extra C-terminal Thr43 versus Aβ(1-42); more aggregation-prone and more neurotoxic; used for full-length Aβ aggregation mechanisms and a potent neurotoxicity model in AD; white powder requiring HFIP pre-treatment and −20°C aliquot storage. | Amyloid-β (Aβ) is generated by sequential β- and γ-secretase cleavage of APP; the exact C-terminus varies with the γ-secretase cleavage site, yielding mainly Aβ(1-40) and Aβ(1-42) as well as rarer, more hydrophobic and more pathogenic species such as Aβ(1-43). Aβ(1-43) carries an additional threonine (Thr43) at the C-terminus beyond Aβ(1-42), further extending the C-terminal hydrophobic stretch; in vitro and in transgenic mouse models it exhibits stronger self-aggregation, faster fibrillation kinetics, higher β-sheet content and greater neurotoxicity than Aβ(1-42). Although less abundant than Aβ(1-42) in human senile plaques, Aβ(1-43) is regarded as a potent "seeding" aggregate nucleus that promotes co-aggregation and plaque spreading of other Aβ species; elevated Aβ(1-43)/Aβ(1-42) ratios are associated with disease progression in Down syndrome (DS) and some forms of familial early-onset AD. This full-length peptide retains the N-terminal metal-binding region (His6/13/14), central hydrophobic core LVFFA (17–21), the E22/D23 charge-sensitive region and the extended C-terminal hydrophobic segment. It is used to: compare aggregation kinetics and neurotoxicity among Aβ(1-40/42/43); investigate how C-terminal extension affects fibril structure and membrane insertion; screen potent anti-aggregation/anti-fibrillation drugs; and establish AD cell/animal models that more closely mimic pathological, strongly aggregating Aβ. | Alzheimer's disease (AD), full-length Aβ variant, Aβ(1-43) vs Aβ(1-42) aggregation differences, potent neurotoxicity model, oligomer/fibril formation, anti-aggregation/anti-fibrillation drug screening, Down syndrome (DS) Aβ metabolism, senile-plaque seeding effect | Full-length Aβ self-aggregation (monomer → oligomer → fibril); N-terminal histidines mediate Cu/Zn metal binding; the extended C-terminal Thr43 enhances hydrophobic packing, fibril stability and neurotoxicity; binds receptors such as RAGE, PrP^c and mGluR5 |
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