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| Description | Rat/mouse Aβ1-42 with human-rodent differences at 5/10/13 (Gly5/Phe10/Arg13) and markedly lower aggregation; used in rodent AD models for aggregation, metabolism and comparison. |
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 (1-42), rat/mouse, CAS:166090-74-0 | Rat/mouse Aβ(1-42); Rodent Aβ42; r/mAβ(1-42) | Alzheimer disease,rodent Aβ,rat/mouse control,aggregation,fibrillation,neurotoxicity,human-rodent difference,AD animal model | DAEFGHDSGFEVRHQKLVFFAEDVGSNKGAIIGLMVGGVVIA | C199H307N53O59S1 | 4415.24 | 4418.02 | Free acid | 42 |
Physicochemical Solubility & Storage Parameters
| Product Code | Appearance | Long-term Storage | Short-term Storage | Solution Stability | Solid Stability |
| PEP-AB142RM-01 | White to off-white powder. | -20 °C, dry, light-protected, sealed; aliquot recommended. | 2–8 °C, short-term (≤1 week); use within the day after reconstitution. | Aggregates/fibrillates in aqueous solution, but R5G/Y10F/H13R mutations lower aggregation propensity vs human Aβ(1-42); HFIP disaggregation pretreatment recommended, keep on ice and use same day. | powder stable ≥2 years at -20 °C dry & light-protected. |
Functional Description
| Product Code | Short Summary (listing) | Detailed Biological Function | Research Areas | Targets/Receptors |
| PEP-AB142RM-01 | Standard rat/mouse Aβ(1-42) (R5G/Y10F/H13R); reference for rodent AD models and human-rodent Aβ comparison. | Rodent (rat/mouse/guinea pig) endogenous Aβ(1-42) differs from human Aβ at three N-terminal positions: R5G, Y10F, H13R. These changes reduce N-terminal charge/aromatic interactions and markedly lower in vitro aggregation and plaque-forming capacity, which partly explains why wild-type mice rarely develop dense amyloid plaques. This peptide is used as (1) endogenous control in rodent AD models (APP-transgenic/intracerebral injection); (2) comparator for human-rodent differences in aggregation kinetics, oligomer formation and neurotoxicity; (3) cross-reactivity/species-specificity testing of N-terminal-targeting anti-Aβ antibodies; (4) mechanistic explanation of relative resistance of rodents to AD-like pathology. | Alzheimer disease,rodent animal model,human-rodent Aβ difference,aggregation kinetics,antibody cross-reactivity,neurotoxicity control | Rodent Aβ oligomers/fibrils; N-terminal epitope of anti-Aβ antibodies; microglia; RAGE |
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