| Description | Extinction Coefficient:1.7IgD was first identified in 1965, and like other immunoglobulins, exists as both secreted and membrane forms. Its level in plasma is low with a mean concentration of 30 ug/ml. IgD is present in large quantities on the surface membrane of a majority of human circulating B Extinction Coefficient:1.7IgD was first identified in 1965, and like other immunoglobulins, exists as both secreted and membrane forms. Its level in plasma is low with a mean concentration of 30 ug/ml. IgD is present in large quantities on the surface membrane of a majority of human circulating B lymphocytes. IgD enhances humoral immune responses through its induction of IgD-receptor expression on T lymphocytes. Prepared from plasma shown to be non reactive for HBsAg, anti-HCV, anti-HBc, and negative for anti-HIV 1 & 2 by FDA-required tests.
IgD was first identified in 1965, and like other immunoglobulins, exists as both secreted and membrane forms. Its level in plasma is low with a mean concentration of 30 ug/ml. IgD is present in large quantities on the surface membrane of a majority of human circulating B lymphocytes. IgD enhances humoral immune responses through its induction of IgD-receptor expression on T lymphocytes.Prepared from plasma shown to be non reactive for HBsAg, anti-HCV, anti-HBc, and negative for anti-HIV 1 & 2 by FDA-required tests.Ref:Coico RF, Siskind GW, Thorbecke GJ 1988. Immunol. Rev. 105:45... Read More | Inquire | Inquire | Inquire | Purity:>90%, by SDS-PAGE visualized with Coomassie® Blue Staining.Description：ER alpha (Estrogen receptor alpha; also Estradiol receptor and NR3A1) is a 65-70 kDa member of the NR3 subfamily, nuclear hormone receptor family of proteins. It is widely expressed, and serves as a strong Purity:>90%, by SDS-PAGE visualized with Coomassie® Blue Staining.Description：ER alpha (Estrogen receptor alpha; also Estradiol receptor and NR3A1) is a 65-70 kDa member of the NR3 subfamily, nuclear hormone receptor family of proteins. It is widely expressed, and serves as a strong activator of estrogen-responsive genes. ER alpha is normally quiescent and bound to heat-shock proteins and immunophilins. Following beta -estradiol binding, it becomes activated, either homodimerizes or heterodimerizes with ER beta, and binds to DNA with multiple coactivators. Human ER alpha is 595 amino acids (aa) in length. It contains a DNA binding region (aa 185-250), three NLSs (aa 256-260; 266-271; 299-303), a steroid-binding site (aa 351-543), a dimerization motif (aa 497-518), and an O-GlcNAc attachment around Thr575. Major phosphorylation sites exist at Tyr537, Ser167 and Ser118. Multiple splice forms exist. There is an 80 kDa isoform that shows a substitution (duplication) of aa 412-517 for Asp411, a second isoform with a deletion of aa 255-366, a third isoform with a deletion of aa 152-412, and a fourth isoform that shows a Thr substitution for aa 152-595. Human ER alpha is only 46% aa identical to human ER beta. Over aa 1-116, human ER alpha shares 85% aa identity with mouse ER alpha... Read More |