CRYBA2 / Unconjugated /
CRYBA2 / Unconjugated /
Product Details
Supplier | Aviva Systems Biology | |
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Catalog #: | ARP73138_P050 (View supplier product page) | |
Size | 100 μl | |
Price | $289.00 | |
Antigen | CRYBA2 | |
Clone | ||
Host | Rabbit | |
Isotype | IgG | |
Conjugate | Unconjugated | |
Target Species | Human | |
Applications | WB | |
Description | This is a rabbit polyclonal antibody against CRYBA2. It was validated on Western Blot by Aviva Systems Biology. At Aviva Systems Biology we manufacture rabbit polyclonal antibodies on a large scale (200-1000 products/month) of high throughput manner. Our antibodies are peptide based and protein family oriented. We usually provide antibodies covering each member of a whole protein family of your interest. We also use our best efforts to provide you antibodies recognize various epitopes of a target protein. For availability of antibody needed for your experiment, please inquire (info@avivasysbio.com). |
About CRYBA2 and Purified
CRYBA2 | Crystallins are separated into two classes: taxon-specific, or enzyme, and ubiquitous. The latter class constitutes the major proteins of the vertebrate eye, which function to maintain 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 defined 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. Beta-crystallins, the most heterogeneous, differ by the presence of the C-terminal extension (present in the basic group but absent in the acidic group). Beta-crystallins form aggregates of different sizes and are able to form homodimers through self-association or heterodimers with other beta-crystallins. This gene is a beta acidic group member. Three alternatively spliced transcript variants encoding identical proteins have been reported. [provided by RefSeq, Jul 2008] |
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