Product Type: Antibody
Descritpion: 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. Alpha crystallins are composed of two gene products: alpha-A and alpha-B, for acidic and basic, respectively. Alpha crystallins can be induced by heat shock and are members of the small heat shock protein (sHSP also known as the HSP20) family. They act as molecular chaperones although they do not renature proteins and release them in the fashion of a true chaperone; instead they hold them in large soluble aggregates. Post-translational modifications decrease the ability to chaperone. These heterogeneous aggregates consist of 30-40 subunits; the alpha-A and alpha-B subunits have a 3:1 ratio, respectively.
Research Areas: Cancer, Metabolism, Neuroscience, Signal transduction
Recommended Dilutions: WB 1:500-1:2000, IHC 1:25-1:100
Size: 200 uL
Gene Accession: BC007008
Immunogen: Recombinant protein of human CRYAB
Formulation: PBS with 0.05% sodium azide, 50% glycerol, PH7.3
Purification: Affinity purification
Calculated MW: 20kDa
Tissue Specificity/Positive Control: Lens as well as other tissues.
Cellular Localization: Cytoplasm. Nucleus. Translocates to the nucleus during heat shock and resides in sub-nuclear structures known as SC35 speckles or nuclear splicing speckles.
Storage: Store at -20C. Avoid freeze / thaw cycles.