AlphaB Crystallin/CRYAB Antibody (3A10.H4) Summary
| Immunogen |
Native Alpha B Crystallin
|
| Localization |
Cytoplasm, Nucleus
|
| Specificity |
Does not cross-react with alphaA-crystallin, BetaL-crystallin, BetaH-crystallin, gamma -crystallin, HSP25, HSP27 or HSP47 proteins.
|
| Isotype |
IgG1
|
| Clonality |
Monoclonal
|
| Host |
Mouse
|
| Gene |
CRYAB
|
| Purity |
Protein G purified
|
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|
Applications/Dilutions
| Dilutions |
|
| Application Notes |
0.5 ug/ml of this antibody was sufficient for detection of 50 ng purified alpha B crystalline by colorimetric immunoblot analysis using Goat anti-mouse IgG:HRP as the secondary antibody.
|
| Theoretical MW |
21 kDa.
Disclaimer note: The observed molecular weight of the protein may vary from the listed predicted molecular weight due to post translational modifications, post translation cleavages, relative charges, and other experimental factors. |
Packaging, Storage & Formulations
| Storage |
Store at 4C short term. Aliquot and store at -20C long term. Avoid freeze-thaw cycles.
|
| Buffer |
PBS pH7.4, 50% glycerol
|
| Preservative |
0.09% Sodium Azide
|
| Concentration |
1 mg/ml
|
| Purity |
Protein G purified
|
Alternate Names for AlphaB Crystallin/CRYAB Antibody (3A10.H4)
- alpha B crystallin
- alpha(B)-crystallin
- AlphaB Crystallin
- alpha-crystallin B chain
- CRYA2
- CRYA2alpha crystallin B chain
- CRYAB
- crystallin, alpha B
- CTPP2
- Heat shock protein beta-5
- heat-shock 20 kD like-protein
- HSPB5
- Renal carcinoma antigen NY-REN-27
- Rosenthal fiber component
Background
The alpha-crystallins are major water-soluble lens structural proteins of the vertebrate eye that are related to the small heat shock protein family. The alpha-crystallins possess structural and functional similarities with HSP25 and HSP27 (1). Mammalian lens cystallins are divided into alpha, beta and gamma families. Alpha and beta families are further divided into acidic and basic groups (Alpha-A and Alpha-B respectively). In the lens, alpha-crystallin primarily functions to maintain proper refractive index, however it can also function as a molecular chaperone that binds to the denatured proteins, keeping them in solution and thereby maintaining the translucency of the lens. When cellular stress occurs, alpha-crystallin enters its phosphorylated state and may serve a structural control function and play a role in protein maintenance (2). In addition to their interaction with proteins, alpha-crystallins also interact with native molecules such as membrane proteins, Golgi matrix protein, structural proteins, nuclear proteins and DNA (3, 4, 5, 6, and 7). Two other functions are an autokinase activity and participation in the intracellular architecture, and it has also been proven that both alpha-A and B prevent apoptosis by inhibiting caspases (8). Specifically, alpha-B cystallin is found in many cells and organs outside the lens, and alpha B is overexpressed in several neurological disorders and in cell lines under stress conditions (9).