AlphaB Crystallin/CRYAB Antibody Summary
| Immunogen |
Peptide with sequence C-RLEKDRFSVNLD corresponding to internal region according to NP_001876.1.
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| Epitope |
RLEKDRFSVNLD
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| Localization |
Cytoplasmic
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| Clonality |
Polyclonal
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| Host |
Goat
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| Gene |
CRYAB
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| Purity |
Immunogen affinity purified
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Applications/Dilutions
| Dilutions |
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| Application Notes |
WB: Approx. 22 kDa band observed in mouse and rat eye lysates (calculated MW of 20.1 kDa band according to mouse NP_034094.1 and rat NP_037067.1).
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| Positive Control |
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| Publications |
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Reactivity Notes
Predicted cross-reactivity based on sequence identity: Human.
Packaging, Storage & Formulations
| Storage |
Store at -20C. Avoid freeze-thaw cycles.
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| Buffer |
0.5 mg/ml Tris (pH 7.3) and 0.5% BSA
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| Preservative |
0.02% Sodium Azide
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| Concentration |
0.5 mg/ml
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| Purity |
Immunogen affinity purified
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Alternate Names for AlphaB Crystallin/CRYAB Antibody
- 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
Crystallins are separated into two classes: taxon-specific, or enzyme, and ubiquitous. The latter class constitutes the major proteins of vertebrate eye lens and maintains the transparency and refractive index of the lens. Since lens central fiber cells lose their nuclei during development, these crystallins are made and then retained throughout life, making them extremely stable proteins. Mammalian lens crystallins are divided into alpha, beta, and gamma families; beta and gamma crystallins are also considered as a superfamily. Alpha and beta families are further divided into acidic and basic groups. Seven protein regions exist in crystallins: four homologous motifs, a connecting peptide, and N- and C-terminal extensions. 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 (sHSP also known as the 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. Alpha-A and alpha-B gene products are differentially expressed; alpha-A is preferentially restricted to the lens and alpha-B is expressed widely in many tissues and organs. Elevated expression of alpha-B crystallin occurs in many neurological diseases; a missense mutation cosegregated in a family with a desmin-related myopathy.