Detection Method:Sandwich
Test principle:This assay employs a two-site sandwich ELISA to quantitate SSH2 in samples. An antibody specific for SSH2 has been pre-coated onto a microplate. Standards and samples are pipetted into the wells and anySSH2 present is bound by the immobilized antibody. After removing any unbound substances, a biotin-conjugated antibody specific for SSH2 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 SSH2 bound in the initial step. The color development is stopped and the intensity of the color is measured.
Product Overview:Two of the human proteins, SSH1L and SSH2, were enzymatically active when reacted with an artificial substrate, p-nitrophenyl phosphate. SSH3 did not exhibit activity toward p-nitrophenyl phosphate, and its expression did not reduce the level of P-cofilin in COS-7 cells. In mammalian cells, SSH1L and SSH2 suppressed LIMK1-induced actin reorganization. Furthermore, ssh, SSH1L, and SSH2 dephosphorylated P-cofilin in cultured cells and in cell-free assays. SSH1 encodes 3 isoforms, SSH1L, SSH1S, and SSH1B, and SSH2 encodes 2 isoforms, SSH2 and SSH2B. The SSH3 protein has 471 amino acids. Besides the catalytic domain, 2 other domains are conserved between Drosophila ssh and the human SSHs (domains A and B) and are unique to the SSH family.
