Alpha B Crystallin antibody | 2E8
Lane 1: Recombinant alpha a crystallin
Lane 2: Recombinant alpha b crystallin.
Mouse anti Human alpha B crystallin, clone 2E8 recognizes the basic (b) form of alpha crystallin, alpha B crystallin, a 20kDa water-soluble major structural protein and member of the heat shock protein family, designated HSPB5, which acts as a molecular chaperone and is believed to play a role in the maintenance of ocular lens transparency/refractive index.
Besides the involvement of both alpha A and alpha B crystallin in the prevention of protein precipitation and cataract formation in the eye, alpha crystallins have also been demonstrated in other tissues including the heart, brain, kidney, spleen and thymus. Studies have shown that a mutation in alpha B crystallin is responsible for desmin-related myopathy (DRM) and cataract (Perng et al. 1999.). Alpha B crystallin is also a major component of the astrocytic inclusions known as Rosenthal fibers (RFs), found in Alexander's disease (Iwaki et al. 1989).
Besides the involvement of both alpha A and alpha B crystallin in the prevention of protein precipitation and cataract formation in the eye, alpha crystallins have also been demonstrated in other tissues including the heart, brain, kidney, spleen and thymus. Studies have shown that a mutation in alpha B crystallin is responsible for desmin-related myopathy (DRM) and cataract (Perng et al. 1999.). Alpha B crystallin is also a major component of the astrocytic inclusions known as Rosenthal fibers (RFs), found in Alexander's disease (Iwaki et al. 1989).
Product Details
- Target Species
- Human
- Species Cross-Reactivity
-
Target Species Cross Reactivity Mouse - N.B. Antibody reactivity and working conditions may vary between species.
- Product Form
- Purified IgG - liquid
- Preparation
- Purified IgG prepared by affinity chromatography on Protein G from ascites
- Buffer Solution
- Phosphate buffered saline
- Preservative Stabilisers
- 0.02% Sodium Azide (NaN3)
10% Glycerol - Immunogen
- Recombinant human alpha B crystallin (amino acids 1-175) purified from E. coli.
- Approx. Protein Concentrations
- IgG concentration 1.0mg/ml
- Fusion Partners
- Spleen cells from immunised Balb/c mice were fused with cells of the mouse Sp2/0 myeloma cell line.
Storage Information
- Storage
- Store at +4oC or at -20oC if preferred.
Storage in frost-free freezers is not recommended.
This product should be stored undiluted. Avoid repeated freezing and thawing as this may denature the antibody. Should this product contain a precipitate we recommend microcentrifugation before use. - Shelf Life
- 18 months from date of despatch.
More Information
- UniProt
- P02511 Related reagents
- Entrez Gene
- CRYAB Related reagents
- GO Terms
- GO:0051082 unfolded protein binding
- GO:0006457 protein folding
- GO:0006936 muscle contraction
- GO:0005212 structural constituent of eye lens
- GO:0005634 nucleus
- GO:0006916 anti-apoptosis
- GO:0009408 response to heat
- GO:0032387 negative regulation of intracellular transport
- GO:0042803 protein homodimerization activity
- GO:0051260 protein homooligomerization
- Regulatory
- For research purposes only
Applications of Alpha B Crystallin antibody
| Application Name | Verified | Min Dilution | Max Dilution |
|---|---|---|---|
| ELISA | |||
| Western Blotting | 1/1000 | 1/2000 |
Where this product has not been tested for use in a particular technique this does not necessarily exclude its use in such procedures. Suggested working dilutions are given as a guide only. It is recommended that the user titrates the product for use in their own system using appropriate negative/positive controls.
- Western Blotting
- MCA2697 detects a band of approximately 20kDa in mouse eye cell lysates.
Copyright © 2018 Bio-Rad Antibodies (formerly AbD Serotec)
Secondary Antibodies Available
Product Specific References
References for Alpha B Crystallin antibody
-
van Nierop, G.P. et al. (2015) Intrathecal CD8 T-cells of multiple sclerosis patients recognize lytic Epstein-Barr virus proteins.
Mult Scler. pii: 1352458515588581.
Further Reading
-
Perng, M.D. et al. (1999) The cardiomyopathy and lens cataract mutation in alphaB-crystallin alters its protein structure, chaperone activity, and interaction with intermediate filaments in vitro.
J Biol Chem. 274 (47): 33235-43.
