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, none in the acidic group). Beta-crystallins form aggregates of different sizes and are able to self-associate to form dimers or to form heterodimers with other beta-crystallins.CRYbA1, a beta acidic group member, encodes two proteins (crystallin, beta A3 and crystallin, beta A1) from a single mRNA, the latter protein is 17 aa shorter than crystallin, beta A3 and is generated by use of an alternate translation initiation site. Deletion of exons 3 and 4 causes the autosomal dominant disease 'zonular cataract with sutural opacities'.
Mouse Crystallin, beta A1 (CRYBA1) ELISA Kit employs a two-site sandwich ELISA to quantitate CRYBA1 in samples. An antibody specific for CRYBA1 has been pre-coated onto a microplate. Standards and samples are pipetted into the wells and anyCRYBA1 present is bound by the immobilized antibody. After removing any unbound substances, a biotin-conjugated antibody specific for CRYBA1 is added to the wells. After washing, Streptavidin conjugated Horseradish Peroxidase (HRP) is added to the wells. Following a wash to remove any unbound avidin-enzyme reagent, a substrate solution is added to the wells and color develops in proportion to the amount of CRYBA1 bound in the initial step. The color development is stopped and the intensity of the color is measured.
Mouse Crystallin, beta A1 (CRYBA1) ELISA Kit listed herein is for research use only and is not intended for use in human or clinical diagnosis. Suggested applications of our products are not recommendations to use our products in violation of any patent or as a license. We cannot be responsible for patent infringements or other violations that may occur with the use of this product.
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