Detection Method:Sandwich
Test principle:This assay employs a two-site sandwich ELISA to quantitate STRN4 in samples. An antibody specific for STRN4 has been pre-coated onto a microplate. Standards and samples are pipetted into the wells and anySTRN4 present is bound by the immobilized antibody. After removing any unbound substances, a biotin-conjugated antibody specific for STRN4 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 STRN4 bound in the initial step. The color development is stopped and the intensity of the color is measured.
Product Overview:Zinedin, a "novel" protein described here, and SG2NA share with striatin identical protein-protein interaction domains and the same overall domain structure. A phylogenetic analysis supports the hypothesis that they constitute a multigenic family deriving from an ancestral gene. DNA probes and antibodies raised against specific domains of each protein showed that zinedin is mainly expressed in the central nervous system, whereas SG2NA, of more widespread occurrence, is mainly expressed in the brain and muscle. All three proteins are both cytosolic and membrane-bound. All three bind calmodulin in the presence of Ca(2+). In rat brain, SG2NA and striatin are generally not found in the same neurons. Both localize to the soma and dendrites, suggesting that they share a similar type of addressing and closely related functions.
