| Product name: |
Crystallin-αB rabbit pAb |
| Reactivity: |
Human;Mouse;Rat |
| Alternative Names: |
CRYAB; CRYA2; Alpha-crystallin B chain; Alpha(B)-crystallin; Heat shock protein beta-5; HspB5; Renal carcinoma antigen NY-REN-27; Rosenthal fiber component |
| Source: |
Rabbit |
| Dilutions: |
Western Blot: 1/500 - 1/2000. Immunohistochemistry: 1/100 - 1/300. ELISA: 1/5000. Not yet tested in other applications. |
| Immunogen: |
The antiserum was produced against synthesized peptide derived from human CRYAB. AA range:10-59 |
| Storage: |
-20°C/1 year |
| Clonality: |
Polyclonal |
| Isotype: |
IgG |
| Concentration: |
1 mg/ml |
| Observed Band: |
24kD |
| GeneID: |
1410 |
| Human Swiss-Prot No: |
P02511 |
| Cellular localization: |
Cytoplasm . Nucleus . Secreted . Lysosome . Translocates to the nucleus during heat shock and resides in sub-nuclear structures known as SC35 speckles or nuclear splicing speckles (PubMed:19464326). Localizes at the Z-bands and the intercalated disk in cardiomyocytes (PubMed:28493373). Can be secreted; the secretion is dependent on protein unfolding and facilitated by the cargo receptor TMED10; it results in protein translocation from the cytoplasm into the ERGIC (endoplasmic reticulum-Golgi intermediate compartment) followed by vesicle entry and secretion (PubMed:32272059). . |
| Background: |
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 distin |
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