antibody

Anti-Alpha B Crystallin Polyclonal Antibody

MBS194398

0.1 mL

320 USD

polyclonal

rabbit

nonconjugated

Antibody

Anti-Alpha B Crystallin Polyclonal Antibody

Alpha B Crystallin

Alpha B Crystallin; Anti-Alpha B Crystallin Polyclonal Antibody

alpha B crystallin; Alpha-crystallin B chain; alpha-crystallin B chain; OTTHUMP00000234278; OTTHUMP00000234282; OTTHUMP00000234283; OTTHUMP00000234284; OTTHUMP00000234287; OTTHUMP00000234289; alpha B crystallin; alpha(B)-crystallin; alpha crystallin B chain; heat shock protein beta-5; rosenthal fiber component; heat-shock 20 kD like-protein; renal carcinoma antigen NY-REN-27; crystallin, alpha B; Alpha(B)-crystallin; Heat shock protein beta-5; HspB5; Renal carcinoma antigen NY-REN-27; Rosenthal fiber component

CRYAB; CRYAB; CRYA2; CTPP2; HSPB5; CRYA2

CRYAB_HUMAN

Polyclonal

Rabbit

175

Alpha B Crystallin [Rabbit antibody recognizes Alpha B Crystallin of multiple species]. This antibody recognizes human, mouse, rat, bovine, and chicken alpha B crystallin. It does not cross-react with alpha A crystallin.

100ul whole antiserum

This antibody is stable for at least one (1) year at -20 degree C. Avoid repeated freezing and thawing.

Immunoblot

Immunoblotting: use at 1:5,000-1:10,000 dilution. A band of ~22 kDa is detected. These are recommended concentrations. User should determine optimal concentrations for their application. Positive control: HeLa cell lysate.

Antigen: Synthetic peptide corresponding to human alpha B crystallin.

Preservatives: None. Dilutions Instructions: Dilute in PBS or medium which is identical to that used in the assay system.

Heat Shock and Stress Proteins

Alpha crystallins are water-soluble lens proteins of the vertebrate eye that are related to the small heat shock protein family. Lens crystallins are divided into alpha, beta, and gamma families. Alpha crystallins are further divided into acidic (Alpha A) and basic (Alpha B) groups. In the lens, alpha crystallin maintains proper refractive index, however it can also function as a molecular chaperone that binds to denatured proteins, keeping them in solution and maintaining the translucency of the lens. In response to cellular stress, alpha crystallin is phosphorlyated and may serve a structural control function and play a role in protein maintenance. Both alpha A and alpha B crystallin prevent apoptosis by inhibiting caspases. Alpha B crystallin is found in many cells and organs outside the lens and is over-expressed in cells subjected to stress conditions and in several neurological disorders.

227018373

ACP18852.1

P02511

20,159 Da

Protein Processing In Endoplasmic Reticulum Pathway (167325); Protein Processing In Endoplasmic Reticulum Pathway (167190)

Mammalian lens crystallins are divided into alpha, beta, and gamma families. 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 (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. The encoded protein has been identified as a moonlighting protein based on its ability to perform mechanistically distinct functions. 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. Alternative splicing results in multiple transcript variants. [provided by RefSeq, Jan 2014]

CRYAB: a major structural protein of the eye lens. A member of the small heat shock protein (sHSP also known as the HSP20) family. Alpha-B is expressed in the lens as well as other tissues. Elevated expression of alpha-B crystallin occurs in many neurological diseases; a missense mutation cosegregated in a family with a desmin-related myopathy. Protein type: Heat shock protein; Chaperone. Chromosomal Location of Human Ortholog: 11q22.3-q23.1. Cellular Component: microtubule cytoskeleton; Golgi apparatus; cell surface; mitochondrion; cytoplasm; plasma membrane; actin filament bundle; nucleus; cytosol; Z disc. Molecular Function: identical protein binding; protein binding; protein homodimerization activity; microtubule binding; metal ion binding; unfolded protein binding; structural constituent of eye lens. Biological Process: lens development in camera-type eye; muscle development; protein folding; microtubule polymerization or depolymerization; stress-activated MAPK cascade; negative regulation of caspase activity; response to estradiol stimulus; tubulin folding; response to hydrogen peroxide; muscle contraction; negative regulation of intracellular transport; response to hypoxia; negative regulation of cell growth; protein homooligomerization; aging; negative regulation of apoptosis. Disease: Cataract 16, Multiple Types; Myopathy, Myofibrillar, Fatal Infantile Hypertonic, Alpha-b Crystallin-related; Myopathy, Myofibrillar, 2; Cardiomyopathy, Dilated, 1ii

0.1 mL

320 USD