Description
Clonality: Polyclonal
Host: Rabbit
Purification: Purified - Affinity
Reactivity: Human, 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.
Parvalbumin (PV) is a calcium binding protein expressed in specific muscle fibers and fast-firing neurons. PV consists of a single, unbranched chain of linked amino acids and belongs to a larger group of EF hand proteins. Studies have demonstrated that parvalbumin acts in the decay of calcium in the contraction/relaxation cycle of fast twitch muscles. This data has shown a positive correlation between the rate of relaxation and the concentration of parvalbumin. Parvalbumin is also expressed in a specific population of GABAergic interneurons which are thought to play a role in maintaining the balance between excitation and inhibition in the cortex as well as the hippocampus. In amyotrophic lateral sclerosis (ALS) patents, parvalbumin immunoreactivity is specifically absent from neuron populations lost early in ALS.
References:
Inaguma Y, Kurobe N, Shinohara H, Kato K. (1991) Sensitive immunoassay for rat parvalbumin: tissue distribution and developmental changes. Biochim Biophys Acta. 1075: 68-74.