[beta]-Amyloid (1-28)
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.
| Sequence: | DAEFRHDSGYEVHHQKLVFFAEDVGSNK | |
| Gene: | APP | |
| Delivery: | 3 weeks | |
| C-Terminus: | OH | |
| N-Terminus: | H | |
| Amount: | 1 mg | |
| Counter Ion: | TFA | |
| Protein: | Amyloid-beta precursor protein | |
| Species: | Human | |
| Allele: | ||
| Application : | Neuroscience | |
| Indication : | Alzheimer's Disease | |
| Purity : | 95% HPLC-MS |
Protocols and Tips
Data sheets
Safety data sheet poly peptides:For your convenience, we have compiled a selection of publications
where our peptide products have been employed:
Publications >
€181.15*
sterile and endotoxin free
Delivery Format: The product is supplied freeze dried.
Purity: 95% HPLC-MS