Stressgen, BioMol, Alexis Corporation, Assay Designs, Alexis

antibody

[pSer59]αB-Crystallin polyclonal antibody

ADI-SPA-227-F

200 µg

polyclonal

domestic rabbit

nonconjugated

phosphorylated

western blot, immunoprecipitation

ADI-SPA-227-F

[pSer59]αB-Crystallin polyclonal antibody

Rabbit

Polyclonal

Phosphorylated

Antibody

200 µg

Mouse, Rat, Sheep, Porcine, Bovine

α-Crystallins composed of αA (~19 kDa) and αB (~19.2 kDa) subunits, are major water-soluble proteins accounting for almost 50% of total protein in the mammalian transparent eye lens and they are also found in a variety of other tissues. Alpha-crystallins are also referred to as small heat shock proteins, since they are induced by increased temperature in a variety of organisms. The α-crystallins have sequence homology as well as structural and functional similarities with the small Hsp’s such as Hsp25/27. Most α-crystallins have four common structural and functional features: (i) molecular weight between 12 and 43kDa; (ii) the formation of large oligomeric complexes composed of αA-crystallin, αB-crystallin and Hsp25/27; (iii) the moderately conserved α-crystallin domain in the central region of the protein; and (iv) molecular chaperone activity. The α-crystallin domain comprises approximately 90 residues, is bounded by variable N-terminal and C-terminal extensions and is involved in oligomer assembly. Oligomers can reach 800 kDa or more and are dynamic, exhibiting subunit exchanges and organizational plasticity, possibly leading to functional diversity. Phosphorylation of serine residues occurs during development and in response to stress, and usually decreases oligomer size. Chaperone activity requires, and is modulated by, oligomerization and is limited to binding unfolded intermediates to prevent irreversible aggregation. Although productive release and refolding of denatured proteins requires close cooperation with other chaperones. Other proposed functions include a role in membrane stabilization and modulation of intermediate filament organization during physiological stress and neurodegenerative disease. Alpha B Crystallin is phosphorylated on serine 45 by ERK1/2 and serine 59 by MAPKAPK-2. When mono-phosphoylated αB-crystallin is isolated it contains only αB-crystallin phosphorylated at serine 19.

CRYAB, HSPB5

Synthetic peptide corresponding to to aa 54-64 of of human αB-crystallin phosphorylated at Ser59.

Liquid. In sodium phosphate buffer, pH 7.0, containing 0.1% sodium azide, 3% BSA, and 50% glycerol.

IP, WB

-20°C