[beta]-Amyloid (1-28) DAEFRHDSGYEVHHQKLVFFAEDVGSNK
€199.50*
Description
The three-dimensional solution structure of Aß (1-28) reveals the folding of the peptide to form a predominantly a-helical structure with a bend centered at residue 12 and the side chains of histidine-13 and lysine-16 in close proximity, residing on the same face of the helix. Their proximity may constitute a binding motif with the heparan sulfate proteoglycans. Aß (1-28) is highly hydrophilic and shares sequences with bA4, the major component of Aß. Its assembly is fibrillar, i.e., elongated in a single direction. Reports show that synthetic peptides Aß (1-40) and Aß (1-28) have significant effects on normal human plasma cholesterol esterification rate. Both peptides (at concentration of 1 ng/mL) inhibit plasma cholesterol esterification rate by 40-50% compared to the control value.
TechData
| Sequence: | DAEFRHDSGYEVHHQKLVFFAEDVGSNK |
| Gene: | APP |
| Delivery: | 3 weeks |
| C-Terminus: | OH |
| N-Terminus: | H |
| Amount: | 1 mg |
| Counterion: | TFA |
| Protein: | Amyloid-beta precursor protein |
| UniProt Id: | P05067 |
| IEDB Id: | 99923 |
| Species: | Human |
| Application: | ELISPOT, Flow Cytometry, Western Blotting |
| Indication: | Neuroscience |
| Purity: | 95% HPLC-MS |
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