Rabbit anti-Human a-B-Crystallin Polyclonal Antibody | anti-CRYAB antibody

Rabbit Anti a-B-Crystallin Polyclonal Antibody

Cat. Num. AAA460639

• Reactivity: Human
• Applications: Western Blot, Immunohistochemistry, ELISA, Immunoprecipitation
• Purity: Purified by Epitope Affinity Purification.
• Synonyms: a-B-Crystallin; Polyclonal Antibody; Rabbit Anti a-B-Crystallin Polyclonal Antibody; Rabbit anti Alpha-Crystallin B Polyclonal Antibody; Alpha-Crystallin B; Rb anti Alpha-Crystallin B; anti-CRYAB antibody

• Host: Rabbit
• Reactivity: Human
• Clonality: Polyclonal
• Isotype: IgG
• Specificity: This antibody recognizes ~21 kDa of human alpha-BCrystallin protein. The other species are not tested.
• Purity/Purification: Purified by Epitope Affinity Purification.
• Form/Format: Supplied in sterile Phosphatebuffered saline (pH7.2) containing antibody stabilizer.

• Applicable Applications for anti-CRYAB antibody: Western Blot (WB), Immunohistochemistry (IHC), ELISA (EIA), Immunoprecipitation (IP)
• Application Notes: WB: 0.1-1 ug/ml; ELISA: 0.01-0.1 ug/ml; IP: 2-5 ug/ml; IHC: 0.5-2 ug/m
• Antigen Preparation: A synthetic peptide corresponding to C-terminus of human Crystallin-a-B protein.
• Positive Control: Mouse liver Lysate
• Cellular Location: Cytoplasm//Nuclear
• Preparation and Storage: The antibodies are stable for 12 months from date of receipt when stored at -20 degree C to -70 degree C. The antibodies can be stored at 2 to 8 degree C for three month without detectable loss of activity. Avoid repeated freezing-thawing cycles.

Related Product Information for anti-CRYAB antibody

Crystallins belong to small heat-shock proteins. There are 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 Nand C-terminal extensions. Alpha crystallins (?B-Crystallin) 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 re-nature proteins and release them in the fashion of a true chaperone; instead they hold them in large soluble aggregates. Posttranslational 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.

References

Mainz,A., Bardiaux,B., Kuppler,F., Multhaup,G., Felli,I.C., Pierattelli,R. and Reif,B. Structural and mechanistic implications of metal binding in the small heat-shock protein alphaB-crystallin. J. Biol. Chem. 287 (2), 1128-1138 (2012).