Alpha A Crystallin (CRYAA) Mouse Monoclonal Antibody [Kloon ID: LBI2H2]

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. Two additional functions of alpha crystallins are an autokinase activity and participation in the intracellular architecture. Alpha-A and alpha-B gene products are differentially expressed; alpha-A is preferentially restricted to the lens and alpha-B is expressed widely in many tissues and organs. Defects in this gene cause autosomal dominant congenital cataract (ADCC) . [provided by RefSeq, Jul 2008]

Carrier-free (BSA/glycerol-free) CRYAA mouse monoclonal antibody, clone LBI2H2

CRYA1; CTRCT9; HSPB4

Homo sapiens crystallin alpha A (CRYAA), transcript variant 1, mRNA.

1409

P02489

Unconjugated

WB 1:2000

Lyophilized powder (original buffer 1X PBS, pH 7.3, 8% trehalose)

Lyophilized powder (original buffer 1X PBS, pH 7.3, 8% trehalose)

Stable for 1 year at -20°C from date of shipment. For maximum recovery of product, centrifuge the original vial after thawing and opening the cap. Aliquot will be stable at 4°C short term. For long-term storage, aliquot and store at -20°C or below. Stable for 12 months at -20°C. Avoid repeated freeze-thaw cycles.

CRYAA

https://www.ncbi.nlm.nih.gov/gene/?term=1409

https://www.uniprot.org/uniprot/P02489