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| Description | Biotin-β-amyloid (1-28) is the N-terminal 1-28 region of β-amyloid, biotinylated for capture by streptavidin on solid phases or conjugation to reporters. It is used to study Aβ aggregation kinetics, antibody recognition, protein binding and in vitro neurotoxicity models. |
| Peptide purity (HPLC) | ≥95% |
| Molecular formula | ~C151H229N43O45 (biotinylated) |
| Molecular weight (Da) | ~3495 (biotinylated) |
| Structure | Linear 28-mer (Aβ1-28, N-biotinylated) |
| Solubility | Readily soluble in water/PBS (pH 7.4) |
| Storage | Powder, −20°C, dry, light-protected |
Product Basic Information Table
| Product Standard English Name | Product Abbreviation / Alias | Function Tags (comma-separated) | Core Structure | Molecular Formula | Exact Mass (Da) | Average MW (Da) | Salt Form | Length (aa) |
| Biotin-beta-amyloid (1-28), N-terminally Biotin-Labeled Peptide | Biotin-Abeta(1-28); Biotin-amyloid beta-protein 1-28; N-terminally biotinylated beta-amyloid peptide; biotin-labeled Abeta fragment; streptavidin-binding Abeta probe | biotinylated peptide, beta-amyloid peptide, Abeta(1-28), Alzheimer's disease, Abeta aggregation, streptavidin binding, ELISA/SPR probe, affinity purification/pull-down | Linear 28-mer, sequence DAEFRHDSGYEVHHQKLVFFAEDVGSNK (residues 1-28 of human Abeta1-42; comprises the N-terminal hydrophilic domain plus the central LVFFA hydrophobic cluster); N-terminal alpha-amine forms an amide bond with biotin; free C-terminal carboxyl; no Cys/Met (no disulfide, no Met oxidation); contains 1 Tyr and 2 Phe (hydrophobic aromatic cluster drives aggregation); near-neutral, slightly negative net charge (~-1 at pH 7); amphipathic and aggregation-prone; biotinylation improves solubility and confers streptavidin binding | C155H223N43O48S | 3486.61 | 3488.80 | TFA/acetate exchangeable (per request); N-terminal biotin label | 28 |
Physicochemical Solubility & Storage Parameters
| Product Code | Appearance | Long-term Storage | Short-term Storage | Solution Stability | Solid Powder Stability |
| PEP-BAβ28-01 | White to off-white powder | Store at -20°C, sealed, desiccated, in single-use aliquots, ~2 years; AVOID REPEATED FREEZE-THAW. Abeta is amphipathic and highly aggregation-prone-must be aliquoted into single-use portions and stored at -20°C. Keep pH near neutral; avoid strongly acidic/basic conditions. | 2-8°C for ~1-2 weeks; working aliquots at -20°C, prepare fresh before use. | Biotinylation improves water solubility over unmodified Abeta. Pre-dissolve in a minimal volume of DMSO or dilute ammonia, then dilute into pH 7.4 PBS to working concentration. Abeta aggregates readily: prepare fresh and use promptly; for oligomer preparation, follow published low-pH/low-temperature protocols. Avoid repeated freeze-thaw (it accelerates aggregation and precipitation). The biotin group is stable and forms a high-affinity noncovalent complex with streptavidin (Kd ~ 1e-14 M). | solid stable ~2 years at -20°C, sealed and desiccated; recommended to flush with argon/nitrogen to minimize oxidation (no Met, but Tyr may slowly oxidize on prolonged air exposure). |
Functional Description
| Product Code | Frontend Short Summary | Detailed Biological Function Description | Applicable Research Areas (comma-separated) | Targets / Pathways |
| PEP-BAβ28-01 | N-terminally biotinylated beta-amyloid peptide Abeta(1-28), containing the Abeta N-terminal hydrophilic region and the central hydrophobic LVFFA aggregation core-used for Abeta aggregation/receptor-binding ELISA, SPR, streptavidin pull-down and Alzheimer's disease mechanism research. | Beta-amyloid (Abeta) is the principal component of senile plaques (SP) in Alzheimer's disease (AD) brain, generated by sequential beta- and gamma-secretase cleavage of the amyloid precursor protein (APP). Abeta(1-28) comprises the N-terminal charged/hydrophilic region (residues 1-16: Asp1, Glu3, Arg5, His6/13/14, Lys16-the main segment engaging ApoE, prion protein (PrP), RAGE, mGluR and other receptors/chaperones) together with residues 17-21, the central hydrophobic LVFFA core that nucleates beta-sheet aggregation. It lacks the strongly hydrophobic transmembrane region of residues 29-42, so it aggregates less than full-length Abeta(1-40/42) and is more soluble-an established model peptide for studying early Abeta aggregation and receptor recognition. N-terminal biotinylation enables, via the streptavidin system: (1) ELISA/SPR/BLI measurement of Abeta binding to candidate ligands (antibodies, ApoE fragments, small-molecule inhibitors, receptor ectodomains); (2) streptavidin-coated beads/plates for Abeta affinity pull-down of interactors from brain or cell lysates; (3) fluorescence/HRP streptavidin detection of Abeta deposits in tissue sections or on cell surfaces. Note: Abeta is amphipathic and highly aggregation-prone-store at -20°C in aliquots, avoid repeated freeze-thaw, keep pH neutral and prepare fresh. Biotinylation improves solubility and orients the N-terminus, making this reagent suitable for Abeta aggregation kinetics, receptor recognition and anti-Abeta drug screening in AD. | Alzheimer's disease (AD) mechanism, Abeta aggregation/fibrillization, Abeta-receptor interactions (ApoE/PrP/RAGE), biotin-streptavidin affinity purification/pull-down, ELISA/SPR/BLI binding assays, anti-Abeta drug screening, neurodegenerative disease model peptide | Abeta aggregation core (LVFFA motif); ApoE, prion protein PrP, RAGE and other Abeta receptors/chaperones; high-affinity binding to streptavidin/avidin |
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