Price and Review,β-Amyloid (1-40) TFA

Amyloid-beta 1-40 peptide, often abbreviated as Aβ40, is a crucial protein fragment that plays a significant role in the neurological landscape, particularly in the context of Alzheimer's disease. This 40-amino-acid peptide is derived from the larger amyloid precursor protein (APP) through a process involving the enzymes β-secretase and γ-secretase. Understanding the nature and behavior of amyloid-beta 1-40 peptide is paramount for researchers and clinicians aiming to unravel the complexities of neurodegenerative disorders.

The Molecular Identity of Amyloid-Beta 1-40 Peptide

Amyloid-beta 1-40 peptide is characterized by its specific amino acid sequence, comprising 40 residues. Its molecular weight is approximately 4330 g/mol. This peptide is one of the two major C-terminal variants of the Aβ family, the other being amyloid-beta 1-42 peptide (Aβ42). While both are found in the brain, Aβ40 is generally more abundant in circulation. The sequence for human amyloid beta polypeptide 40 is Asp-Ala-Glu-Phe-Arg-His-Asp-Ser-Gly-Tyr-Glu-Val-His-His-Gln-Lys-Leu-Val-Phe-Phe-Ala-Glu-Asp-Val-Gly-Ser-Asn-Lys-Gly-Ala-Pro-Gly-Gly-Gly-Gly-Ser-Asn-Lys-Gly-Ala-Pro-Val-Val-Ile-Ala. This precise sequence contributes to its unique properties and interactions.

The deposition of amyloid-beta peptide (Aβ) in the brain is a hallmark of Alzheimer's disease (AD). While Aβ40 is a normal product of APP processing, its accumulation and aggregation into amyloid plaques are strongly associated with the pathogenesis of AD. These plaques are a primary feature observed in the brains of affected individuals. Research indicates that amyloid-beta 1-40 peptide can form oligomeric aggregates, which are believed to be particularly toxic to neurons. The presence of amyloid beta peptides of 36–43 amino acids, with Aβ40 being a significant component, is central to this pathology.

Moreover, studies have explored the correlation between circulating amyloid-beta (1-40) levels and clinical outcomes. While Aβ42 is more directly linked to plaque formation, elevated Aβ40 levels have also been associated with increased risk for certain conditions, including metabolic disease. This suggests a broader systemic implication for this peptide.

The clearance of Alzheimer's amyloid-β1-40 peptide from the brain is a critical process for maintaining neurological health. Dysregulation of these clearance mechanisms can contribute to disease progression. Researchers are investigating various avenues for enhancing Aβ clearance, including the exploration of supplements that remove amyloid plaques.

The therapeutic potential of small peptides in Alzheimer's disease is an active area of research. While the focus often leans towards Aβ42 due to its higher aggregation propensity, understanding the behavior of amyloid-beta 1-40 peptide is equally important. Strategies involving recombinant peptide Beta-Amyloid 1-40 are employed in research settings to study its interactions and potential therapeutic targets.

Amyloid-beta 1-40 peptide is extensively used in scientific research. It can be obtained as a synthetic peptide for various experimental purposes. For instance, beta-Amyloid (1-40), Ultra Pure, TFA is a common form used in laboratories. Researchers often need to reconstitute in 10mM PBS (pH7.4) to a concentration of 0.1-1.0 mg/mL, taking care to avoid vortexing and repeated freeze-thaw cycles to maintain its integrity.

Diagnostic tools, such as the Human amyloid beta peptide 1-40, Aβ1-40 ELISA Kit, are available to quantitatively measure Aβ40 levels in biological samples like serum, tissue homogenates, and cerebrospinal fluid (CSF). The sensitivity of these kits, often in the range of 31.25 pg/mL, allows for precise detection. The availability of beta-amyloid (1-40) specific antibodies further aids in the detection and study of this peptide.

It is important to note that while amyloid-beta 1-40 peptide is a primary focus, other related entities exist. For example, citrullinated amyloid-β (1-40) peptide represents a modified form that may have different biological implications. Furthermore, variations exist across species, with beta-Amyloid Peptide (1-40) (rat/mouse)**