Biotin-Ahx-Amyloid β-Protein (1-40)

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Biotin-Ahx-Amyloid β-Protein (1-40)
Details
N-biotinylated, Ahx-spaced Aβ1-40 (DAEFRHDSGYEVHHQKLVFFAEDVGSNKGAIIGLMVGGVV), 40
residues; HPLC ≥95%.
Related Documents: COA/MS/HPLC
report; streptavidin-capture Aβ aggregation guide.
Category
Drug Peptides
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Description

Shanghai Sonyt Biotechnology Co., Ltd. is one of the leading manufacturers and suppliers of biotin-ahx-amyloid β-protein (1-40) in China, also supports custom service. Welcome to wholesale bulk high quality biotin-ahx-amyloid β-protein (1-40) from our factory. Contact us for more details.

 

Description Biotin-Ahx-Aβ(1-40) carries an N-terminal biotin via a flexible 6-aminohexanoic acid spacer that reduces steric interference with Aβ aggregation. It is efficiently captured on streptavidin plates/beads for aggregation-kinetics, oligomer-capture, antibody-recognition and inhibitor-screening assays.
CAS No.  1802086-72-1
Structure type Linear 40-mer (biotin-Ahx-Aβ1-40)
Solubility NaOH pre-dispersion then PBS pH adjust
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-Ahx-beta-Amyloid (1-40), human (biotin-Ahx spacer human amyloid-beta 1-40), CAS 1802086-72-1 Biotin-Ahx-Abeta(1-40); Biotinyl-eAhx-Abeta40; Biotin-LC-Abeta(1-40); N-terminally biotinylated + Ahx spacer human Abeta40; biotin-labeled amyloid probe biotinylated peptide, beta-amyloid peptide, Abeta(1-40), Alzheimer's disease, Abeta aggregation/fibrillization, HFIP monomerization, Ahx spacer, streptavidin capture, ELISA/SPR/pull-down probe Linear 40-mer human Abeta(1-40), sequence DAEFRHDSGYEVHHQKLVFFAEDVGSNKGAIIGLMVGGVV; the N-terminal alpha-amine is linked via an epsilon-aminocaproic acid (Ahx/LC flexible spacer), whose free amine forms an amide bond with biotin (biotin-Ahx-amide); free C-terminal Val40 carboxyl; contains Met35 (oxidation-prone), 1 Tyr and 3 Phe; no Cys; amphipathic, less aggregation-prone than Abeta(1-42) but more than Abeta(1-28); net charge ~ -1 at pH 7; the long Ahx spacer keeps biotin away from Abeta, minimizing steric hindrance so Abeta epitopes remain exposed after streptavidin immobilization; biotin binds streptavidin with high affinity (Kd ~ 1e-14 M) C210H320N56O61S2 4666.31 4669.32 Free acid; N-terminal biotin + Ahx spacer label; TFA/acetate available on request; CAS 1802086-72-1 40

 

Physicochemical Solubility & Storage Parameters

 

Product Code Appearance Long-term Storage Short-term Storage Solution Stability Solid Powder Stability
PEP-BioAb40-01 White to off-white powder Store at -20C, sealed, desiccated and light-protected, in single-use aliquots, ~1-2 years; AVOID REPEATED FREEZE-THAW. Abeta is amphipathic and aggregation-prone-must be aliquoted, kept under inert gas, near neutral pH, and prepared fresh; aggregation tendency: Abeta(1-42) > Abeta(1-40). 2-8C for ~1-2 weeks; working aliquots at -20C, prepare fresh. MUST BE HFIP-PRETREATED TO MONOMERIZE BEFORE USE: dissolve peptide in sterile hexafluoroisopropanol (HFIP) at room temperature to dissociate pre-aggregates, evaporate under N2/Ar, redissolve in anhydrous DMSO, then dilute into pH 7.4 buffer (e.g. PBS) to working concentration; do NOT dissolve lyophilized solid directly in water, which would introduce pre-aggregates. In solution Abeta readily aggregates/fibrillizes-prepare fresh, use promptly, and avoid repeated freeze-thaw and prolonged 37C incubation. The biotin group is stable and forms a high-affinity noncovalent complex with streptavidin (Kd ~ 1e-14 M); the Ahx spacer keeps the N-terminus and the LVFFA aggregation core well exposed after immobilization. solid stable ~1-2 years at -20C, sealed, desiccated and light-protected; Met35 may slowly oxidize to the sulfoxide on prolonged air exposure-flush with Ar/N2 and minimize air exposure.

 

Functional Description

 

Product Code Frontend Short Summary Detailed Biological Function Description Applicable Research Areas (comma-separated) Targets / Pathways
PEP-BioAb40-01 N-terminally Ahx (LC)-spaced biotinylated human Abeta(1-40) (CAS 1802086-72-1), containing the complete N-terminal hydrophilic region and the LVFFA aggregation core; HFIP-monomerized before use; for streptavidin-captured Abeta40 aggregation/receptor-binding ELISA, SPR, oligomer pull-down and AD biomarker research. Beta-amyloid (Abeta) is the principal component of senile plaques (SP) in Alzheimer's disease (AD) brain, generated by sequential cleavage of the amyloid precursor protein (APP) by beta-secretase (BACE1) and gamma-secretase. Abeta(1-40) is the most abundant secretase product, and the cerebrospinal-fluid/plasma Abeta40/Abeta42 ratio is a key AD biomarker. Abeta(1-40) comprises the N-terminal charged region (residues 1-16, engaging ApoE, PrP(C), RAGE, mGluR5) and the central hydrophobic core LVFFA (residues 17-21, the beta-sheet nucleation motif), ending at Val40 (lacking the Ile41-Ala42 of Abeta42); it therefore aggregates and fibrillizes less than Abeta(1-42) and is more soluble-an established isoform for studying early Abeta aggregation, receptor recognition and the biology of the Abeta40/42 ratio. This product tethers biotin at the N-terminus via an Ahx (epsilon-aminocaproic acid/LC) flexible spacer: (1) the long Ahx spacer keeps biotin away from the Abeta backbone, avoiding steric shielding of the N-terminal epitope and LVFFA core after streptavidin immobilization; (2) the biotin-streptavidin system allows immobilization or capture of Abeta. Typical applications: (1) ELISA/SPR/BLI measurement of Abeta40 binding to anti-Abeta antibodies, ApoE fragments, small-molecule aggregation inhibitors and receptor ectodomains; (2) streptavidin-bead/plate pull-down of Abeta interactors or capture of Abeta oligomers; (3) competitive assays of Abeta40 immunoreactivity in CSF/plasma; (4) biotinylated tracing in Abeta40 aggregation/fibrillization kinetics (ThT fluorescence) and inhibitor screening. Note: Abeta is highly amphipathic and aggregation-prone; IT MUST BE HFIP-PRETREATED TO OBTAIN A UNIFORM MONOMER (HFIP to dissociate pre-aggregates -> N2 blow-down -> DMSO redissolution -> buffer dilution); prepare fresh in solution, keep pH neutral, avoid repeated freeze-thaw; Met35 is oxidation-sensitive. Alzheimer's disease (AD) mechanism, Abeta(1-40) aggregation/fibrillization, HFIP monomerization, Abeta40/Abeta42 biomarker ratio, Abeta-receptor interactions (ApoE/PrP/RAGE), biotin-streptavidin pull-down, ELISA/SPR/BLI binding assays, anti-Abeta aggregation inhibitor screening Abeta aggregation core (LVFFA motif); ApoE, PrP(C), RAGE, mGluR5 and other Abeta receptors/chaperones; high-affinity binding to streptavidin/avidin (Kd ~ 1e-14 M)

 

 

 

 

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