DESCRIPTION

Amino Acid Sequence

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

Main description

Amyloid β Protein Fragment 1-40 (Aβ40) is derived from the amyloid-β protein (Aβ), which is mapped to human chromosome 21q21.3. Aβ40 is predominantly present contained within the vascular amyloid deposits. Aβ40 contains of C-terminal membrane insertion space. It reveals structural transition from random coil to a α-helical establishing in a water-micelle medium.

Biochem/physiol Actions

Amyloid β-protein is neurotrophic and neurotoxic in vivo and in vitro in human and rat neuronal cell cultures. β-Amyloid peptides (amino acids 1-42 and 1-43) are the foremost constituents of senile plaques and neurofibrillary tangles that occur contained within the hippocampus, neocortex, and amygdala of victims with Alzheimer′s sickness.
Amyloid β Protein Fragment 1-40 (Aβ40) varieties cation primarily based ion channels.

Utility

Amyloid β Protein Fragment 1-40 has been used:

  • contained within the temperature primarily based conformational analysis using Fourier rework infrared/differential scanning calorimetry (FT-IR/DSC) analysis
  • as a reference commonplace in sandwich-type enzyme immunoassay for quantifying amyloid A4 protein in cerebrospinal fluid of victims with head trauma
  • as a aspect of embryonic stem cell medium to inhibit amyloid deposition in fibroblasts

 

amyloid

amyloid

Reconstitution

For maximal pure put together, dilute the stock in calcium-free PBS to 1 mg/ml and incubate at 37 °C for 4 days.

Totally utterly totally different Notes

Lyophilized from 0.1% TFA in H2O

Abstract

Alzheimer’s sickness (AD) pathogenesis is broadly believed to be pushed by the manufacturing and deposition of the β-amyloid peptide (Aβ). For just a few years, investigators have been puzzled by the weak to nonexistent correlation between the amount of neuritic plaque pathology contained within the human concepts and the diploma of scientific dementia. Present advances in our understanding of the occasion of amyloid pathology have helped treatment this thriller. Substantial proof now signifies that the solubility of Aβ, and the quantity of Aβ in pretty a lot of swimming swimming swimming swimming pools, may be extra fastidiously related to sickness state.

The composition of these swimming swimming swimming swimming pools of Aβ reveals completely absolutely utterly totally different populations of amyloid deposits, and has categorical correlates with the scientific standing of the affected individual. Imaging utilized sciences, along with new amyloid imaging brokers primarily based completely utterly on the chemical establishing of histologic dyes, at the moment are making it doable to hint amyloid pathology along with sickness enchancment contained within the residing affected explicit individual. Curiously, these approaches diploma out that the Aβ deposited in AD is totally absolutely utterly totally different from that current in animal fashions.

Key phrases: Amyloid, β-Amyloid Precursor Protein, Aβ, oligomer, fibril
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