Crystallins are separated into two classes:
taxon-specific, or enzyme, and ubiquitous. The latter class
constitutes the major proteins of vertebrate eye lens and maintains
the transparency and refractive index of the lens. Since lens
central fiber cells lose their nuclei during development, these
crystallins are made and then retained throughout life, making them
extremely stable proteins. Mammalian lens crystallins are divided
into alpha, beta, and gamma families; beta and gamma crystallins
are also considered as a superfamily. Alpha and beta families are
further divided into acidic and basic groups. Seven protein regions
exist in crystallins: four homologous motifs, a connecting peptide,
and N- and C-terminal extensions. Gamma-crystallins are a
homogeneous group of highly symmetrical, monomeric proteins
typically lacking connecting peptides and terminal extensions. They
are differentially regulated after early development. Four
gamma-crystallin genes (gamma-A through gamma-D) and three
pseudogenes (gamma-E, gamma-F, gamma-G) are tandemly organized in a
genomic segment as a gene cluster. Whether due to aging or
mutations in specific genes, gamma-crystallins have been involved
in cataract formation.1) Acosta-Sampson, L., et al. J. Mol. Biol. 401(1):134-152(2010)
Immunogen
This CRYGB antibody is generated from rabbits immunized with a KLH conjugated synthetic peptide between 68-97 amino acids from the Central region of human CRYGB.
Western blot analysis in HepG2 cell line lysates (35ug/lane).
Application Notes
For WB starting dilution is: 1:1000
Additional Information
Form
Liquid
Storage Instructions
Store at 4˚C for three months and -20˚C, stable for up to one year. As with all antibodies care should be taken to avoid repeated freeze thaw cycles. Antibodies should not be exposed to prolonged high temperatures.