For research use only. Not for therapeutic Use.
β-Amyloid (35-42) is a peptide consisting of amino acid of 35 to 42 of beta amyloid protein.
β-Amyloid Aggregation Guidelines (Following is our recommended protocol. This protocol only provides a guideline, and should be modified according to your specific needs).
1. Solid Aβ peptide was dissolved in cold hexafluoro-2-propanol (HFIP). The peptide was incubated at room temperature for at least 1h to establish monomerization and randomization of structure.
2. The HFIP was removed by evaporation, and the resulting peptide was stored as a film at -20 or -80 ℃.
3. The resulting film was dissolved in anhydrous DMSO at 5 mM and then diluted into the appropriate concentration and buffer (serum- and phenol red-free culture medium) with vortexing.
4. Next, the solution was age 48h at 4-8 ℃. The sample was then centrifuged at 14000g for 10 min at 4-8 ℃; the soluble oligomers were in the supernatant. The supernatant was diluted 10-200-fold for experiments.
Methods vary depends on the downstream applications.
Catalog Number | I018318 |
CAS Number | 183292-41-3 |
Synonyms | (2S)-2-[[(2S,3S)-2-[[(2S)-2-[[(2S)-2-[[2-[[2-[[(2S)-2-[[(2S)-2-amino-4-methylsulfanylbutanoyl]amino]-3-methylbutanoyl]amino]acetyl]amino]acetyl]amino]-3-methylbutanoyl]amino]-3-methylbutanoyl]amino]-3-methylpentanoyl]amino]propanoic acid |
Molecular Formula | C33H60N8O9S |
Purity | ≥95% |
InChI | InChI=1S/C33H60N8O9S/c1-11-19(8)27(32(48)37-20(9)33(49)50)41-31(47)26(18(6)7)40-30(46)25(17(4)5)38-23(43)15-35-22(42)14-36-29(45)24(16(2)3)39-28(44)21(34)12-13-51-10/h16-21,24-27H,11-15,34H2,1-10H3,(H,35,42)(H,36,45)(H,37,48)(H,38,43)(H,39,44)(H,40,46)(H,41,47)(H,49,50)/t19-,20-,21-,24-,25-,26-,27-/m0/s1 |
InChIKey | WMASSBNUXWFHBX-CMCOHCKLSA-N |
SMILES | CCC(C)C(C(=O)NC(C)C(=O)O)NC(=O)C(C(C)C)NC(=O)C(C(C)C)NC(=O)CNC(=O)CNC(=O)C(C(C)C)NC(=O)C(CCSC)N |
Reference | [1]. Hubin E, et, al. Two distinct β-sheet structures in Italian-mutant amyloid-beta fibrils: a potential link to different clinical phenotypes. Cell Mol Life Sci. 2015 Dec;72(24):4899-913. |