Product Name: CRYAB Antibody [10D5F4]
Species Reactivity: Human
Tested Applications: ELISA, IHC
Applications: Western Blot:1:500 – 1:2,000 IHC(P):1:500 – 1:2,000 ELISA:Propose dilution 1:10,000.
User Note: Optimal dilutions for each application to be determined by the researcher.
Predicted Molecular Weight:
Immunogen: Purified full length recombinant CRYAB-Trx (aa1-175) is expressed in E.Coli strain BL21 (DE3).
Host Species: Mouse
Purification:
Physical State:
CAS NO.: 138489-18-6
Product: Ro 31-8220 (mesylate)
Buffer: Ascitic fluid containing 0.03% sodium azide.
Concentration:
Storage Conditions: CRYAB monoclonal antibody can be stored at -20˚C, stable for 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.
Clonality: Monoclonal
Conjugate: Unconjugated
Alternate Names: CRYA2, Heat shock protein beta-5, HspB5, MFM2, CRYA2, CTPP2, HSPB5, CMD1II, CTRCT16, HEL-S-101
Accession NO.: P02511
Protein Ino: 117385
Official Symbol: CRYAB
Geneid: 1410
Background: Crystallin, alpha B.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.
PubMed ID:http://aac.asm.org/content/37/4/775.abstract
