amyloid b-protein

β-Amyloid (22-35) is a 14-aa peptide, shows aggregates and induces neurotoxicity in the hippocampal cells. Beta amyloid (22-35) is a synthetic truncated fragment of beta-amyloid peptide.

β-Amyloid (1-28), a fragment of the β-Amyloid protein, is involved in metal binding.

Amyloid β-peptide fragment; minimum section required to bind to brain proteins. Binds with high affinity to α7-nicotinic ACh receptors, and impairs memory retention following central administration in mice in vivo.

β-Amyloid (1-16) is an amyloidogenic protein fragment derived from the β-amyloid sequence, known for its ability to bind metal ions, indicating its role in metal-binding processes. β-Amyloid, a peptide, is responsible for forming amyloid plaques in the brains of people with Alzheimer's disease (AD).

β-Amyloid (1-15) (Amyloid β-Protein (1-15)) is a fragment of β-amyloid protein used in the study of Alzheimer's disease.

β-Amyloid (29-40) is a fragment of Amyloid-β peptide. Alzheimer's beta amyloid peptide (29-40/42) C-terminal fragments exhibit physical and chemical properties similar to fusion peptides of viral proteins, inducing liposome fusion in vitro.

Beta-Amyloid Protein Precursor 770 (135-155)Aβ Protein Precursor 770 (135-155)

Amyloid β-Protein (10-20) is a fragment of Amyloid-β peptide, maybe used in the research of neurological disease.Amyloid β protein fragment containing the α-secretase processing site (Lys16-Leu17 bond). It also contains the HHQK domain (residues 13-16) re

Amyloid β-Protein 10-20 acetate (Amyloid β-Protein 10-20 acetate (152286-31-2 free base)) is a fragment of Amyloid-β peptide, maybe used in the research of neurological disease.Amyloid β protein fragment containing the α-secretase processing site (Lys16-Leu17 bond). It also contains the HHQK domain (residues 13-16) responsible for binding to microglial cells.

β-amyloid (12-28) TFA, a peptide fragment of β-amyloid protein (β1-42), is the major component of senile plaque cores. β-amyloid (12-28) has aggregation properties and the potential for Alzheimer's disease research.