CRYGD Human
Description
CRYGD is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Product Specs
MGSSHHHHHH SSGLVPRGSH MGKITLYEDR GFQGRHYECS SDHPNLQPYL SRCNSARVDS GCWMLYEQPN YSGLQYFLRR GDYADHQQWM GLSDSVRSCR LIPHSGSHRI RLYEREDYRG QMIEFTEDCS CLQDRFRFNE IHSLNVLEGS WVLYELSNYR GRQYLLMPGD YRRYQDWGAT NARVGSLRRV IDFS.
Product Science Overview
Gamma-crystallins are highly symmetrical, monomeric proteins that lack connecting peptides and terminal extensions . They are known for their stability and are crucial for maintaining the transparency and refractive index of the lens . The human γD crystallin is a 173-residue protein that folds into two homologous domains, each containing two Greek key motifs . This structure is essential for the protein’s stability and function.
Crystallins are the principal structural components of the vertebrate eye lens . The lens is an avascular tissue composed of a single layer of epithelial cells that elongate to become fiber cells during lens formation . These fiber cells produce large quantities of crystallins, which help maintain the optical properties of the lens throughout life . The high concentration of crystallins in the lens is necessary to ensure its transparency and refractive power .
Despite their stability, gamma-crystallins can accumulate damage over time, leading to protein aggregation and cataract formation . Cataracts are the leading cause of blindness worldwide, and the only current treatment is surgical removal of the lens . Mutations in the CRYGD gene have been associated with various forms of cataracts .
Recombinant human gamma D crystallin is produced using recombinant DNA technology, which allows for the expression of the human CRYGD gene in a host organism . This recombinant protein is used in research to study the structure, function, and stability of gamma D crystallins, as well as their role in cataract formation .
