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Alpha-crystallins, which are part of the small Heat shock family members, are major water-soluble proteins present in the lens of the mammalian eye. Phosphorylation of serine residues which occurs during development and in response to stress, is intimately linked with its function. Chaperone activity requires, and is modulated by, oligomerization and is limited to binding unfolded intermediates to prevent irreversible aggregation.
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Western Blot analysis of αB-Crystallin mAb (1B6.1-3G4) (Prod. No. ENZ-ABS706): Lane 1: MW Marker, Lane 2: α-Crystallin (bovine), (native) (Prod. No. ADI-SPP-225), Lane 3: αB-Crystallin (bovine), (native) (Prod. No. ADI-SPP-227).
Immunohistochemistry analysis of human heart tissue with alpha B-Crystallin, mAb (1B6.1-3G4), (Prod. No. ENZ-ABS706), at 20µg/ml.
| Regulatory Status |
RUO – Research Use Only |
|---|
Related Products
| Application | ELISA, IHC, WB |
|---|---|
| Host | Goat |
| Species Reactivity | Mouse |
| Application | ELISA, WB |
|---|---|
| Host | Goat |
| Species Reactivity | Mouse |
| Alternative Name | CRYAB, HSPB5 |
|---|---|
| Application | ICC, IF, IHC (PS), WB |
| Host | Mouse |
| Isotype | IgG1 |
| Species Reactivity | Bovine, Chicken, Human, Mouse, Rat |
| Alternative Name | CRYAB, HspB5, Heat shock protein β-5 |
|---|---|
| Purity | ≥90% (SDS-PAGE; Western blot) |
| Source | Isolated from bovine eye lens. |