Amyloid beta-Protein (Human, 1 – 40) [HCl Form]

Amyloid β-Protein (Human, 1-40)

4379-v 0.5 mg | 190.00 EUR

Synthetic Product (Lyophilized from Dilute HCl Solution)

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

The purity is guaranteed to be higher than 95% by HPLC

HCl Form of Amyloid beta-Protein (Human, 1-40) | Easily Convertible to β-Structure

Amyloid β-proteins (Aβs) were detected to be major plaque components in the brains of Alzheimer’s disease patients. Recently, Kaneko et al. reported that the HCl form of Amyloid beta-protein (1-40) turns into β-structure within a few hours, and it shows neurotoxic activity. On the other hand, TFA salt of Amyloid beta-protein (1-40) needs >1 week to turn into on a β-structure under their experimental conditions [J. Neurochem., 65, 2585 (1995), ibid., 68, 438 (1997)].

We prepared the HCl form of Amyloid beta-protein (1-40) following their procedure and confirmed their observations shown above.

Characteristics of our new product Amyloid beta-protein (1-40) [HCl Form] are as follows;

1. random coil when supplied,
2. conformational change to β-structure within 24 hours (by CD measurement under our conditions), and
3. significant neurotoxic activity under our determining conditions.

To perform the reproducible study in Alzheimer’s disease research, we now offer Amyloid beta-protein (1-40) [HCl Form] with the highest quality.

Shipping | Storage | Stability
Amyloid beta-protein (1-40) [HCl Form] will be shipped at room temperature. Information about product specific storage conditions can be found on the vial. Stock solutions should be stored at -20°C. Please avoid repeated freezing and thawing by preparing aliquots.

References:

1. I. Kaneko, N. Yamada, Y. Sakuraba, M. Kamenosono, and S. Tutumi, J. Neurochem., 65, 2585 (1995) (Original; Amyloid Beta-Protein (Human, 1-40) HCl Form)
2. I. Kaneko and S. Tutumi, J. Neurochem., 68, 438 (1997) (Facile β-Structure Formation)