| request information: |
|
| Catalog Code: | NB120-13496 |
| Product Name: | alpha B Crystallin Antibody |
| Product Description: | Mouse Monoclonal anti-alpha B Crystallin (1B6.1-3G4) |
| Clone: | 1B6.1-3G4 |
| Clonality: | Monoclonal |
| ListPrice: | 325 |
| Immunogen: | Bovine áB-Crystallin protein |
| Specificity: | There is no reactivity with Beta-crystallin, AlphaA-crystallin, Hsp25,Hsp27 or Hsp47 proteins. |
| Cross Reactivity: | Cross-reacts with Human, Mouse, Rat, Cow and Chicken. Not yet tested in other species. |
| Packaging: | 0.1 mg protein G purified Mouse ascites. |
| Uses: | ICC, IHC, WB: Colorimetric. Optimal dilutions/concentrations should be determined by the end user. |
| Background: | Alpha-crystallins composed of ~20 kDa áA and áB subunits function as major water-soluble proteins accounting for almost 50% of total protein in the mammalian transparent eye lens, also existing in a variety of other tissues1. Crystallin families â and ã share homology with each other but not the á family or the small heat shock protein (sHsp) family, while Alphacrystallins, induced by heat in a variety of organisms, belong to the sHsp family2. The á-crystallins possess structural and functional similarities and share sequence homology with Hsp25/273. Most small heat shock proteins exhibit four common structural and functional features: molecular weight between 12 and 43kDa; the formation of large oligomeric complexes composed of áA-crystallin, áB-crystallin and Hsp25/27; a moderately conserved á-crystallin domain in the central region of the protein; and molecular chaperone activity2,4. The á-crystallin domain bounded by variable N-terminal and C-terminal extensions contains approximately 90 residues and participates in oligomer assembly. Oligomers, potentially 800kDa or more, exhibit dynamic subunit exchanges and organizational plasticity, which may promote functional diversity. Phosphorylation of serine residues occurs in response to stress during development, typically decreasing oligomer size4. Chaperone activity requires oligomerization (which, in turn, modulates the chaperone activity) and is confined to binding unfolded intermediates to prevent irreversible aggregation2,4, even though productive release and refolding of denatured proteins requires close cooperation with other chaperones. Other proposed functions include a role in membrane stabilization2 and modulation of intermediate filament organization during physiological stress and neurodegenerative disease5. |
| Storage: | Aliquot and store at -20C. Avoid freeze thaw cycles. |
| Purity: | protein G purified |
| Isotype: | IgG1 |
| Host Name: | Mouse |
| Buffer: | 50% Glycerol, PBS, 0.1mM PMSF. pH 7.2 |
| Application Summary: | Western Blot 1 ug/ml, Immunocytochemistry , Immunohistochemistry-Frozen Use at an assay dependent dilution |
| Species Summary: | Bv, Ch, Hu, Mu, Rt, |
| Alternate Names: | anti-AACRYA antibody, anti-Alpha crystallin B chain antibody, anti-CRYA2 antibody, anti-CRYAB antibody, anti-CTPP 2 antibody, antiCTPP2 antibody, anti-HSPB5 antibody |
| Package Size: | 0.1 mg |
| Preservative: | Sodium Azide |
| General References: | 1. Wistow, G., et al. (2005) FEBS J. 272, 2276-2291. 2. Narberhaus, F. (2002) Microbiol Mol Biol Rev. 66, 64-93. 3. Merck, K.B., et al. (1993) J Biol Chem. 268, 1046-1052. 4. MacRae, T.H. (2000) Cell Mol Life Sci. 57, 899-913. 5. Head, M.W., et al. (2000) Neuropathol Appl Neurobiol. 26, 304-312. 6. Kamradt, M.C., et al. (2001) J Biol Chem. 276, 16059-16063. |
order or
more information: | company product webpage |
|