Description
Clonality: Polyclonal
Host: Rabbit
Purification: Purified - Affinity
Reactivity: Bovine, Human, Mouse, Porcine, Rat
Neurodegenerative diseases such as Alzheimer's disease and Parkinson's disease have been increasing rapidly and have become a serious social problem. In recent years, new causative genes have been discovered for amyotrophic lateral sclerosis (ALS) and other intractable neurological diseases opening new avenues for research on pathogenesis. It has been suggested that aggregation and accumulation of specific proteins cause neurotoxicity and the formation of lesions, but the onset and progression mechanisms are still unclear. Neuropathological diagnostic and experimental model biomarkers are needed for drug construction, drug discovery, and therapeutic development.
The S100 protein is a low-molecular-weight, acidic and calcium binding protein that in functional form exist in dimers. S100 has two subunits: S100-alpha (94 aa; human chromosome 1) and S100-beta (92 aa; human chromosome 21) that forms as either homodimers (alpha-alpha known as S-100a(0) or beta-beta known as S-100b) or as heterodimers (known as S-100a) of ~21 kDa. S100-alpha and -beta chains show ~58% sequence identity and are both highly conserved among species. S100-alpha was originally believed to be localized to the CNS, but studies have shown it to be found in numerous tissues including cardiac, skeletal and vascular smooth muscle cells.
References:
Kato K, Haimoto H, Ariyoshi Y, Horisawa M, Washida H, Kimura S. (1985) High levels of S-100a0 (alpha alpha) protein in tumor tissues and in sera of patients with renal cell carcinoma. Jpn J Cancer Res. 76:856-62.