Technical Data
Crystallin, alpha B
Alpha-crystallins composed of alphaA (~19kD) and alphaB (~19.2kD) 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 (1). The two other crystallin families, beta and gama, are homologous to each other but not to the alpha family or the sHspís. Alpha-crystallins are also referred to as small heat shock proteins, since they are induced by increased temperature in a variety of organisms. (2) The alpha-crystallins have sequence homology as well as structural and functional similarities with the small Hspís such as Hsp25/27 (3). Most alpha-•crystallins have four common structural and functional features: (i) molecular weight between 12 and 43kDa; (ii) the formation of large oligomeric complexes composed of alphaA-crystallin, alphaB-crystallin and Hsp25/27; (iii) the moderately conserved alpha-•crystallin domain in the central region of the protein; and (iv) molecular chaperone activity (2,4). The alpha-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 800kDa 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 (4). Chaperone activity requires, and is modulated by, oligomerization and is limited to binding unfolded intermediates to prevent irreversible aggregation (2,4). Although productive release and refolding of denatured proteins requires close cooperation with othe chaperones. Other proposed functions include a role in membrane stabilization (2) and modulation of intermediate filament organization during physiological stress and neurodegenerative disease (5).

Suitable for use in Western Blot. Other applications have not been tested.

Recommended Dilution:
Western Blot (Colorimetric): 2ug/ml
Optimal dilutions to be determined by researcher.

Positive Controls:
Bovine alphaB-Crystallin Protein

Storage and Stability:
May be stored at 4°C for short-term only. For long-term storage, store at -20°C. Aliquots are stable for at least 12 months at -20°C. For maximum recovery of product, centrifuge the original vial after thawing and prior to removing the cap. Further dilutions can be made in assay buffer.
MabIgG14E55Affinity Purified
50ug4°C (-20°C Glycerol)Blue IceBovineMouse
Purified alphaB-crystallin from bovine eye lens.
Purified by Protein G affinity chromatography.
Supplied as a liquid in PBS, pH 7.2 containing 0.1mM PMSF and 50% glycerol.
Detects a ~20kD protein, corresponding to the apparent molecular mass of alphaB-crystallin on SDS-PAGE immunoblots. Species Crossreactivity: human, rat, bovine and chicken. There is no reactivity with beta-crystallin, alphaA-crystallin, Hsp25, Hsp27 nor Hsp47 purified proteins.
Intended for research use only. Not for use in human, therapeutic, or diagnostic applications.
1. Augusteyn, R. C., Parkhill, E. M., and Stevens, A. (1992) Exp. Eye Res. 54: 219-228.
2. Narberhaus, F. (2002) Microbiol Mol Biol Rev 66(1): 64-93.
3. Merck, K. B., Groenen, P. J., Vooter, C. E., de Haard-Hoelman, W. A., Horwitz, J.,
Bloemendal, H. and de Jong, W. W. (1993) J. Biol. Chem. 268: 1046-1052.
4. MacRae, T.H. (2000) Cell Mol Life Sci 57(6): 899-913.
5. Head, M.W., Goldman, J.E. (2000) Neuropathol Appl Neurobiol 26(4): 304-312.
6. Kamradt, M.C., Chen, F., Sam, S., Cryns, V.L. (2002) J Biol Chem 277(41): 38731-38736.
7. Kamradt, M.C., Chen, F., Cryns, V.L. (2001) J Biol Chem 276(19): 16059-16063.