β-Amyloid (1-40), FAM-labeled 

β-Amyloid (1-40), FAM-labeled is a FAM fluorescently-labelled β-Amyloid (1-40) peptide (λ_ex= 492 nm and λ_em= 518 nm)^[1].

λ_ex= 492 nm; λ_em= 518 nm

Apical-to-basolateral exchange across endothelial monolayer of fluorescent Aβ42 (FAM-labeled Human β-Amyloid (1-42) and Fluor^™488-labeled β-Amyloid (1-42)) or scramble Aβ42 (FAM-labeled scrambled β-Amyloid (1-42)) (1-100 μM) is monitored in transendothelial electrical resistance (TEER) during cell monolayer’s formation over time (over 120 min in presence or absence of Aβ24). Human β-Amyloid (1-24) (1 μM) results in H-Aβ42 retention, thus reducing its efflux through the BBB and therefore preventing an efficient mechanism of Aβ42 clearance^[1].
The in vitro BBB model is used to investigate the passage of FAM-labeled or 488-conjugated H-Aβ42 across the endothelial cell monolayer. The addition of fluorescently labeled H-Aβ42 (FAM-labeled Human β-Amyloid (1-42) or Fluor^™ 488-labeled β-Amyloid (1-42)) to the apical side of cell inserts results in effective BBB crossing, FAM-labeled scrambled β-Amyloid (1-42) is not efficiently transcytosed.

MedChemExpress (MCE) has not independently confirmed the accuracy of these methods. They are for reference only.

4688.20

C₂₁₅H₃₀₅FN₅₃O₆₄S

1678416-08-4

FAM-Asp-Ala-Glu-Phe-Arg-His-Asp-Ser-Gly-Tyr-Glu-Val-His-His-Gln-Lys-Leu-Val-Phe-Phe-Ala-Glu-Asp-Val-Gly-Ser-Asn-Lys-Gly-Ala-Ile-Ile-Gly-Leu-Met-Val-Gly-Gly-Val-Val

FAM-DAEFRHDSGYEVHHQKLVFFAEDVGSNKGAIIGLMVGGVV

Room temperature in continental US; may vary elsewhere.

Please store the product under the recommended conditions in the Certificate of Analysis.

• [1]. L M Jungbauer, et al. Preparation of fluorescently-labeled amyloid-beta peptide assemblies: the effect of fluorophore conjugation on structure and function. J Mol Recognit. Sep-Oct 2009;22(5):403-13.  [Content Brief]

  [2]. Sonia Mazzitelli, et al. Amyloid-β 1-24 C-terminal truncated fragment promotes amyloid-β 1-42 aggregate formation in the healthy brain. Acta Neuropathol Commun. 2016 Oct 10;4(1):110.  [Content Brief]