Recombinant Human gamma C Crystallin protein (His tag N-Terminus)

Supplementary information

This supplementary information is collated from multiple sources and compiled automatically.

Gamma C Crystallin also known as CRYGC is a protein that plays an important role in maintaining the transparency and refractive index of the eye lens. This protein has a molecular mass of approximately 20 kDa. It is mainly expressed in the lens fibers of the eye. CRYGC is highly insoluble and functions to ensure clarity by packing tightly within the lens fiber cells helping to provide the necessary optical properties for proper light focus onto the retina.

Biological function summary

Gamma C Crystallin maintains lens transparency by preventing light scattering in the lens cells. It is not part of a larger protein complex but works among a family of crystallin proteins including alpha and beta crystallins which together compose the major structural proteins of the lens. The precise organization and stability of these crystallins ensure proper focusing of light and disruptions can lead to opacity in the lens.

Pathways

Gamma C Crystallin does not participate directly in metabolic or signaling pathways but is critical within the structural framework of the lens. It interacts with other crystallin proteins to maintain cellular architecture and prevent protein aggregation. While these proteins are not enzymatic their importance is seen in structural integrity with connections to other proteins such as alpha crystallins which have chaperone-like activities that aid in maintaining lens clarity.

Mutations in gamma C Crystallin are associated with congenital cataracts a condition where clouding of the lens occurs at birth or develops shortly thereafter. This is due to improper folding or aggregation of CRYGC leading to light scattering. The mutation can affect the stability and solubility of the protein disrupting lens transparency. It connects to other proteins such as alpha crystallins which can become overloaded and less effective at preventing aggregation when gamma C Crystallin is mutated.