The application notes include recommended starting dilutions; optimal dilutions/concentrations should be determined by the end user.
Application notesWB: Use at a concentration of 1-5 µg/ml.
This antibody has only been tested in WB against the recombinant fragment used as immunogen. We have no data on the detection of endogenous protein.
Not yet tested in other applications. Optimal dilutions/concentrations should be determined by the end user.
FunctionCrystallins are the dominant structural components of the vertebrate eye lens.
Involvement in diseaseDefects in CRYBB1 are the cause of cataract congenital nuclear autosomal recessive type 3 (CATCN3) [MIM:611544]. A congenital cataract affecting the central nucleus of the eye. Nuclear cataracts are often not highly visually significant. The density of the opacities varies greatly from fine dots to a dense, white and chalk-like, central cataract. The condition is usually bilateral. Nuclear cataracts are often combined with opacified cortical fibers encircling the nuclear opacity, which are referred to as cortical riders. Defects in CRYBB1 are a cause of cataract-microcornea syndrome (CAMIS) [MIM:116150]. An ocular disorder characterized by the association of congenital cataract and microcornea without any other systemic anomaly or dysmorphism. Clinical findings include a corneal diameter inferior to 10 mm in both meridians in an otherwise normal eye, and an inherited cataract, which is most often bilateral posterior polar with opacification in the lens periphery. The cataract progresses to form a total cataract after visual maturity has been achieved, requiring cataract extraction in the first to third decade of life. Microcornea-cataract syndrome can be associated with other rare ocular manifestations, including myopia, iris coloboma, sclerocornea and Peters anomaly. Transmission is in most cases autosomal dominant, but cases of autosomal recessive transmission have recently been described.
Sequence similaritiesBelongs to the beta/gamma-crystallin family. Contains 4 beta/gamma crystallin 'Greek key' domains.
DomainHas a two-domain beta-structure, folded into four very similar Greek key motifs.
Post-translational modificationsSpecific cleavages in the N-terminal arm occur during lens maturation and give rise to truncated forms, leading to impaired oligomerization and protein insolubilization.