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SDS-PAGE Analysis of Purified ER-beta Mouse Monoclonal Antibody (ESR2/3207). Confirmation of Purity and Integrity of Antibody.
Analysis of Protein Array containing more than 19,000 full-length human proteins using Estrogen Receptor beta-1 Mouse Monoclonal Antibody (ESR2/3207) Z- and S- Score: The Z-score represents the strength of a signal that a monoclonal antibody (MAb) (in combination with a fluorescently-tagged anti-IgG secondary antibody) produces when binding to a particular protein on the HuProtTM array. Z-scores are described in units of standard deviations (SD's) above the mean value of all signals generated on that array. If targets on HuProtTM are arranged in descending order of the Z-score, the S-score is the difference (also in units of SD's) between the Z-score. S-score therefore represents the relative target specificity of a MAb to its intended target. A MAb is considered to specific to its intended target, if the MAb has an S-score of at least 2.5. For example, if a MAb binds to protein X with a Z-score of 43 and to protein Y with a Z-score of 14, then the S-score for the binding of that MAb to protein X is equal to 29.
Estrogen receptors (ER) are members of the steroid/thyroid hormone receptor superfamily of ligand-activated transcription factors. Estrogen receptors, including ER-alpha and ER-beta, contain DNA binding and ligand binding domains and are critically involved in regulating the normal function of reproductive tissues. They are located in the nucleus, though some estrogen receptors associate with the cell surface membrane and can be rapidly activated by exposure of cells to estrogen. ER-alpha and ER-beta are differentially activated by various ligands. Receptor-ligand interactions trigger a cascade of events, including dissociation from heat shock proteins, receptor dimerization, phosphorylation and the association of the hormone activated receptor with specific regulatory elements in target genes. Evidence suggests that ER-alpha and ER-beta may be regulated by distinct mechanisms even though they share many functional characteristics.
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