Visinin was originally isolated biochemically from chicken retina as a major protein of ~24kDa on SDS-PAGE gels. The protein belongs to the large superfamily of calmodulin and paravalbumin type proteins which function by binding Calcium ions. Calcium binding alters the conformation of these proteins and allow them to interact with other binding partners, the properties of which they may alter. Visinin-like protein 1 has four “EF hand” domains, which are negatively charged helix-turn-helix peptides which are responsible for Calcium binding. The protein is 191 amino acids in size and has a molecular weight on SDS-PAGE of 18kDa. The protein has recently been suggested to be a useful blood biomarker of Alzheimer’s disease and traumatic brain injury.
RA22155 antibody was made against full length recombinant human visinin-like protein 1, and expressed in and purified from E. Coli. It can be used to track this protein by ELISA, on western blots and in cells in culture and sections.
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