Alpha B Crystallin antibody
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 formation of 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 (provided by RefSeq, Jul 2008).
Mouse anti Human alpha B crystallin chain antibody detects a band of 22 kDa. The antibody has been extensively validated for western blotting using whole cell lysates.
- Target Species
- Western Blotting
- Anti alpha B crystallin detects a band of approximately 22 kDa in human heart tissue
- Product Form
- Purified IgG - liquid
- Mouse monoclonal antibody purified by affinity chromatography on Protein G from ascites
- Buffer Solution
- Phosphate buffered saline
- Preservative Stabilisers
- 0.09% Sodium Azide (NaN3)
- Purified recombinant fragment of alpha B crystallin (aa1-175) expressed in E.coli
- Store undiluted at -20oC, avoiding repeated freeze thaw cycles.
- 12 months from date of despatch
- Entrez Gene
- 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
- PrecisionAb is a trademark of Bio-Rad Laboratories.
- For research purposes only
Applications of Alpha B Crystallin antibody
|Application Name||Verified||Min Dilution||Max Dilution|
The PrecisionAb label is reserved for antibodies that meet the defined performance criteria within Bio-Rad's ongoing antibody validation programme. Click here to learn how we validate our PrecisionAb range. Where this product has not been tested for use in a particular technique this does not necessarily exclude its use in such procedures. Further optimization may be required dependent on sample type.
Secondary Antibodies Available
|Description||Product Code||Applications||Pack Size||List Price||Quantity|
|Goat anti Mouse IgG (H/L):HRP||STAR207P||WB||2 ml|
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