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| Description | Mouse/rat Aβ1-38 with species-differing positions 5/10/13; used in rodent AD models for aggregation, metabolism and species-specific comparisons. |
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) |
| beta-Amyloid (1-38), mouse, rat (endogenous rodent amyloid-beta residues 1–38, 38-mer; three natural N-terminal substitutions relative to human Aβ: R5G, Y10F, H13R; C-terminus ends at Gly38) | Aβ(1-38) mouse/rat; Mouse/rat Aβ(1-38); Rodent Aβ38; murine/rat beta-amyloid (1-38); rodent AD-model control peptide | mouse/rat Aβ(1-38), rodent AD model, human vs mouse Aβ comparison, R5G/Y10F/H13R natural variation, N-terminal charge/histidine distribution difference, Aβ38 C-truncated, transgenic mouse background peptide, HFIP pre-treatment, aggregation differs from human | Linear 38-mer, sequence DAEFGHDSGFEVRHQKLVFFAEDVGSNKGAIIGLMVGG (rodent Aβ Asp1 to Gly38). Three natural N-terminal substitutions relative to human Aβ(1-42): Arg5→Gly (R5G), Tyr10→Phe (Y10F), His13→Arg (H13R); the C-terminus ends at Gly38, lacking the Val39-Val40/Ile41-Ala42 hydrophobic tail of Aβ40/Aβ42. R5G removes a positive charge and H13R replaces the pH-sensitive, metal-coordinating histidine with a strongly basic arginine, making the rodent N-terminal charge and histidine-mediated metal coordination markedly different from human-an important sequence basis for why wild-type rodents have much lower brain Aβ aggregation propensity than humans. | C180H273N49O55S | 4032.98 | 4035.51 | TFA salt; CAS 186359-66-0 | 38 |
Physicochemical Solubility & Storage Parameters
| Product Code | Appearance | Long-term Storage | Short-term Storage | Solution Stability | Solid Powder Stability |
| PEP-AB138MR-01 | White powder | Store at −20°C, sealed, desiccated, protected from light; aliquot to avoid repeated freeze-thaw, ~2 years. | Keep briefly at 2–8°C; keep working solutions on ice; ship on dry ice or ample blue ice. | Although the C-terminus is truncated at Gly38 and lacks the strongly hydrophobic tail of Aβ40/Aβ42 (lower aggregation than Aβ42), the LVFFA (17–21) core is retained, giving moderate aggregation propensity; **routine HFIP de-aggregation is still recommended**: dissolve in HFIP ~1 mM, sonicate on ice, aliquot and Speed-Vac to a monomer film. The rodent N-terminal R5G/H13R changes N-terminal charge and histidine distribution, so aqueous solubility/aggregation differ slightly from human Aβ(1-38); reconstitute in dilute NaOH (~pH 10) then neutralize to the desired pH, on ice and fresh. Keep in solution at 4°C for ≤ a few days, or aliquot and store at −20°C/−80°C; avoid repeated freeze-thaw. | solid stable ~2 years at −20°C, sealed, desiccated, protected from light; hygroscopic, keep dry/dark/sealed; contains oxidizable Met35. |
Functional Description
| Product Code | Frontend Short Summary | Detailed Biological Function Description | Applicable Research Areas (comma-separated) | Targets / Receptors |
| PEP-AB138MR-01 | Endogenous mouse/rat Aβ(1-38), 38-mer, carrying three natural N-terminal substitutions (R5G/Y10F/H13R) that differ from human, C-terminus ending at Gly38. Used as a rodent AD-model control, for human-vs-rodent Aβ aggregation comparisons, and as the background peptide in transgenic mouse studies. HFIP de-aggregation recommended; prepare fresh. TFA-salt powder; store at −20°C dry and dark. | Aβ naturally produced in wild-type mouse and rat brains differs from human Aβ by three conserved N-terminal substitutions (R5G, Y10F, H13R); this sequence difference is thought to be a key reason why wild-type rodents rarely develop cerebral amyloid plaques even at advanced age-R5G lowers the N-terminal positive charge, H13R alters histidine-mediated Cu²⁺/Zn²⁺ coordination and pH-sensitive conformation, and Y10F changes N-terminal aromatic interactions. Aβ(1-38) itself is a C-terminally truncated gamma-secretase cleavage product of APP (ending at Gly38, shorter than Aβ40's Val40 and Aβ42's Ala42), present at appreciable levels in CSF and brain, with aggregation propensity between Aβ40 and shorter fragments. This product is the rodent-sequence Aβ(1-38), used mainly to: (1) serve as the 'endogenous background peptide' in APP/PS1, 5xFAD and APP NL-G-F transgenic AD mouse models, distinguishing the aggregation/toxicity contributions of the transgenic human Aβ from the endogenous rodent Aβ; (2) compare nucleation rate, fibril morphology and neurotoxicity of human Aβ(1-38/40/42) versus rodent Aβ(1-38) in parallel in vitro (ThT, fibril EM/AFM, neuronal toxicity), quantifying the contribution of the three N-terminal substitutions; (3) evaluate cross-reactivity of anti-Aβ antibodies, especially those recognizing N-terminal conformational or species-specific epitopes; and (4) serve as a control peptide for in vivo intracerebral/intrahippocampal injection in rodents. Because rodent Aβ aggregates less readily than human, extend incubation time or increase concentration and run in parallel with human peptide from the same batch. | Alzheimer's disease (AD), transgenic mouse models, human vs rodent Aβ differences, R5G/Y10F/H13R natural variation, Aβ38 C-truncated, ThT aggregation comparison, anti-Aβ antibody species cross-reactivity, rodent intracerebral injection control | Aβ self-aggregation / beta-sheet fibrils; N-terminal histidine/arginine participate in Cu²⁺/Zn²⁺ coordination; no specific receptor target |
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