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| beta-Amyloid (1-42) human Basic information |
| beta-Amyloid (1-42) human Chemical Properties |
| storage temp. | -20°C | | solubility | Soluble in ammonium hydroxide, pH >9. Also soluble in DMSO. | | form | Lyophilized | | InChIKey | XPESWQNHKICWDY-QYFPAAMGSA-N | | CAS DataBase Reference | 107761-42-2(CAS DataBase Reference) |
| Safety Statements | 24/25 | | WGK Germany | 3 | | HS Code | 29332900 |
| beta-Amyloid (1-42) human Usage And Synthesis |
| Chemical Properties | Solid | | Uses | 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. | | Application | 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.
| | General Description | Amyloid β Protein 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. | | Biochem/physiol Actions | 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. |
| beta-Amyloid (1-42) human Preparation Products And Raw materials |
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