107761-42-2

Lyophilized White solid, with no soy flavor, no protein denaturation, acidic non-precipitation, heating does not coagulate, easily soluble in water, good fluidity, and other good processing properties, is an excellent health food material.

Aβ(s) peptides, their peptide fragments and mutated fragments are used to study a wide range of metabolic and regulatory functions including activation of kinases, regulation of cholesterol transport, function as a transcription factor, and regulators of inflammation. Aβ(s) peptides and their peptide fragments are also used to study oxidative stress, metal binding and mechanisms of protein cross-linking in the context of diseases such as Alzheimer?s disease and neurodegeneration.

Amyloid beta (Aβ or Abeta) is a peptide of 36-C43 amino acids that is processed from the Amyloid precursor protein. Amyloid β-Peptide (1-42) human(107761-42-2) is a 42-amino acid peptide which plays a key role in the pathogenesis of Alzheimer disease. Beta-Amyloid (1-42) human is used as follows:
for the production of Aβ-1-42 oligomer;
in western blot analysis;
for interference testing of immunomagnetic reduction (IMR) plasma Aβ42 assay;
to study the effect of resveratrol on Aβ-1-42-induced impairment of spatial learning, memory, and synaptic plasticity;
to investigate the effect of Aβ in epithelial cell cultures.

Amyloid β Protein(107761-42-2) is produced from amyloid-β precursor protein (APP). It consists of two C terminal variants, such as a long tailed Aβ 1-42 and a short tailed Aβ 1-40. APP is located on human chromosome 21q21.3.

Amyloid β-Peptide (1-42) (human) is a human form of the predominant amyloid β-peptide found in the brains of patients with Alzheimer's disease. Amyloid β Protein Fragment 1-42 (Aβ 1-42) has antioxidant and neuroprotective properties. Accumulation of amyloid β Protein is associated with Alzheimer′s disease (AD) and Down Syndrome. Aβ 1-42 regulates cholesterol transport and may function as a transcription factor. It may possess anti-inflammatory and antimicrobial properties. Downregulates bcl-2 and increases the levels of bax. Neurotoxic.

Store at -20°C

[1] CHEN L M, CHAI K X. Matriptase cleaves the amyloid-beta peptide 1–42 at Arg-5, Lys-16, and Lys-28[J]. BMC Research Notes, 2019, 12. DOI:10.1186/s13104-018-4040-z.
[2] BROWN A M, BEVAN D R. Influence of sequence and lipid type on membrane perturbation by human and rat amyloid β-peptide (1-42).[J]. Archives of biochemistry and biophysics, 2015, 614: 1-13. DOI:10.1016/j.abb.2016.11.006.
[3] MENGTING YANG. Gel Phase Membrane Retards Amyloid β-Peptide (1–42) Fibrillation by Restricting Slaved Diffusion of Peptides on Lipid Bilayers[J]. Langmuir, 2018, 34 28: 8408-8414. DOI:10.1021/acs.langmuir.8b01315.
[4] LIANG SHEN Hong F J. Comparative study on the conformational stability of human and murine amyloid β peptide[J]. Computational and Theoretical Chemistry, 2011, 972 1: Pages 44-47. DOI:10.1016/j.comptc.2011.06.012.
[5] MOUCHARD A, BOUTONNET M C, MAZZOCCO C, et al. ApoE-fragment/Aβ heteromers in the brain of patients with Alzheimer’s disease[J]. Scientific Reports, 2019, 9. DOI:10.1038/s41598-019-40438-4.