WB

Synthesized peptide derived from human CRGA AA range: 105-155

This antibody detects endogenous levels of CRGA at Human/Mouse/Rat

Monoclonal, Mouse,IgG

Liquid in PBS containing 50% glycerol, 0.5% BSA and 0.02% sodium azide.

WB 1:500-2000

The antibody was affinity-purified from mouse serum by affinity-chromatography using specific immunogen.

1 mg/ml

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. [provided by RefSeq, Jul 2008],

domain:Has a two-domain beta-structure, folded into four very similar Greek key motifs.,function:Crystallins are the dominant structural components of the vertebrate eye lens.,similarity:Belongs to the beta/gamma-crystallin family.,similarity:Contains 4 beta/gamma crystallin 'Greek key' domains.,subunit:Monomer.,

CRYGA CRYG1

CRGA

CRGA

-20°C/1 year