Mouse Crystallin Alpha B (CRYaB) ELISA Kit-Sandwich

Alpha-crystallin B chain may play a role in maintaining the transparency and refractive index of the lens. It exhibits chaperone-like activity, preventing the aggregation of various proteins under diverse stress conditions. In lens epithelial cells, it helps stabilize the ATP6V1A protein, protecting it from proteasomal degradation. In mice, αB-crystallin serves multiple biological functions, including acting as a molecular chaperone to prevent protein aggregation, protecting heart and muscle tissues, inhibiting tumor invasion, and maintaining eye transparency. Studies on mouse eyes show that αB-crystallin coexists with αA-crystallin in the lens and is crucial for lens transparency. Mice lacking αA-crystallin develop early cataracts, although the expression of αB-crystallin remains unaffected.