Shanghai Sonyt Biotechnology Co., Ltd. is one of the leading manufacturers and suppliers of β-amyloid (42-1) human tfa in China, also supports custom service. Welcome to wholesale bulk high quality β-amyloid (42-1) human tfa from our factory. Contact us for more details.
| Description | Aβ1-42 reversed end-to-end, same composition but opposite backbone direction; cannot form native intermolecular β-sheets; a sequence-direction negative control for Aβ42 aggregation/toxicity. |
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 (42-1), human TFA (reverse sequence of Aβ 1-42) (human reverse-sequence 42-mer of Aβ 1-42, TFA salt; sequence AIVVGGVMLGIIAGKNSGVDEAFFVLKQHHVEYGSDHRFEAD) | Reverse Aβ(1-42); Aβ(42-1); scrambled-order Aβ control; reversed-sequence Aβ(1-42) negative control | β-amyloid peptide, reverse-sequence negative control, non-aggregating, AD assay control peptide, aggregation-inhibition baseline, ThT fluorescence negative control, random-coil control | Linear 42-mer; complete reverse of human Aβ(1-42) from residue 42 (Ala) back to residue 1 (Asp): AIVVGGVMLGIIAGKNSGVDEAFFVLKQHHVEYGSDHRFEAD; identical residue composition and chiral amino acids to human Aβ(1-42), but primary order fully reversed; the amphipathic β-sheet register is destroyed and the peptide behaves as a random coil in aqueous solution | C203H311N55O60S1 | 4511.27 | 4514.10 | TFA salt / powder | 42 |
Physicochemical Solubility & Storage Parameters
| Product Code | Appearance | Long-term Storage | Short-term Storage | Solution Stability | Solid Stability |
| PEP-AB42REV-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. | 2–8°C for ~1 week; working aliquots at −80°C; avoid prolonged room-temperature exposure; ship on dry ice/blue ice. | The reverse-sequence disordered peptide does not form oligomers or fibrils; water-soluble and can be dissolved directly in water or buffer; no HFIP pretreatment required; solutions stable for several days at 4°C, or aliquot and store long-term at −80°C. | solid stable for ~2 years at −20°C, sealed, desiccated and protected from light; not hygroscopic/aggregation-prone; storage under argon/nitrogen preferred. |
Functional Description
| Product Code | Short Summary (listing) | Detailed Biological Function | Research Areas | Targets/Receptors |
| PEP-AB42REV-01 | Human Aβ(1-42) fully reversed-sequence synthetic peptide (42-mer, TFA salt). Residue composition and chiral amino acids are identical to native Aβ(1-42), but the primary order is inverted; disruption of the amphipathic β-sheet register makes the peptide a random coil in aqueous solution, with no oligomer/fibril formation and no neurotoxicity. The classic negative/baseline control for Aβ aggregation, aggregation-inhibitor screening, ThT/CD spectroscopy and cytotoxicity assays. Good water solubility; dissolves directly in water or buffer. | Amyloid-β (Aβ) self-assembles into β-sheet oligomers and fibrils that deposit as senile plaques in Alzheimer's disease (AD). The high aggregation propensity of Aβ(1-42) arises from the directional amphipathic arrangement along the chain: the N-terminal hydrophilic/charged region (DAEFRHDSGYEVHHQK), the central hydrophobic core KLVFF (17-20), the central charged cluster AEDVGSN (21-27), and the strongly hydrophobic C-terminal transmembrane segment KGAIIGLMVGGVVIA (28-42), which cooperatively drive intermolecular antiparallel/parallel β-sheet stacking. Aβ(42-1) is the control peptide obtained by fully reversing the sequence from C- to N-terminus; its residue composition, chirality, total charge and molecular weight are nearly identical to native Aβ(1-42), but the amphipathic directionality along the chain is destroyed: the strongly hydrophobic C-terminal segment is moved to the N-terminus, the hydrophilic N-terminal charged region is moved to the C-terminus, and the central hydrophobic core KLVFF is reversed to FFVLK. This primary-sequence inversion destroys the hydrophobic-hydrophilic periodicity required for intermolecular β-sheet recognition, so the reverse peptide behaves as a random coil in aqueous solution, gives very low ThT fluorescence, shows a far-UV CD minimum near ~200 nm, does not form oligomers or fibrils, and does not induce neuronal toxicity. Aβ(42-1) is therefore widely used as: (1) the negative/blank baseline in Aβ aggregation kinetics; (2) the benchmark peptide to exclude non-specific hydrophobic/charge interference in aggregation-inhibitor screens; (3) the negative control for ThT fluorescence, ANS hydrophobic probe, and CD/FTIR spectroscopy; (4) the control in cytotoxicity assays to distinguish sequence-specific Aβ toxicity from generic physicochemical interference; and (5) the control peptide for assessing drug-Aβ binding specificity by SPR/ITC. This product is supplied as TFA-salt powder with good water solubility; it can be dissolved directly in water or buffer without HFIP pretreatment. | Alzheimer's disease (AD), Aβ aggregation mechanism, aggregation-inhibitor screening, ThT/CD/FTIR spectroscopy baseline, cytotoxicity negative control, random-coil control peptide, drug-Aβ binding specificity | No specific receptor; serves as negative/baseline control in Aβ aggregation and toxicity assays |
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