*Optimal dilutions/concentrations should be determined by the researcher.
Not tested in other applications.
Human, Rabbit, Sheep, Bovine, Chicken, Guinea pig, Rhesus Monkey(>80% identity)
0.1M Tris, 0.1M Glycine, 20% Glycerol (pH7). 0.01% Thimerosal was added as a preservative.
Store as concentrated solution. Centrifuge briefly prior to opening vial. For short-term storage (1-2 weeks), store at 4ºC. For long-term storage, aliquot and store at -20ºC or below. Avoid multiple freeze-thaw cycles.
0.98 mg/ml (Please refer to the vial label for the specific concentration.)
Recombinant protein encompassing a sequence within the center region of human crystallin alpha B. The exact sequence is proprietary.
Purified by antigen-affinity chromatography.
For laboratory use only. Not for any clinical, therapeutic, or diagnostic use in humans or animals. Not for animal or human consumption.
crystallin alpha B , CMD1II , CRYA2 , CTPP2 , CTRCT16 , HEL-S-101 , HSPB5 , MFM2
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. Elevated expression of alpha-B crystallin occurs in many neurological diseases; a missense mutation cosegregated in a family with a desmin-related myopathy. [provided by RefSeq]
GTX103053 WB Image
Various tissue extracts (50 μg) were separated by 15% SDS-PAGE, and the membrane was blotted with alpha B Crystallin antibody (GTX103053) diluted at 1:50000. The HRP-conjugated anti-rabbit IgG antibody (GTX213110-01) was used to detect the primary antibody.