| Description | Note: 1 mU = 1 milliunit.Recombinant, streptomyces plicatus endoglycosidase H expressed in E. coli. Catalyzes the hydrolysis of asparagine-linked oligomannose and hybrid, but not complex oligosaccharides from glycoprotein. Endo H cleaves between the two N-acetylglucosamine residues in the Note: 1 mU = 1 milliunit.Recombinant, streptomyces plicatus endoglycosidase H expressed in E. coli. Catalyzes the hydrolysis of asparagine-linked oligomannose and hybrid, but not complex oligosaccharides from glycoprotein. Endo H cleaves between the two N-acetylglucosamine residues in the diacetylchitobiose core of the oligosaccharide... Read More | Inquire | Purity:>95%, by SDS-PAGE visualized with Coomassie® Blue StainingDescription:Human B7 homolog 3 (B7-H3) is a member of the B7 family of immune proteins that provide signals for the regulation of immune responses. Other family members include B7-1, B7-2, B7-H1/PD-L1, B7-H2, and PD-L2. B7 Purity:>95%, by SDS-PAGE visualized with Coomassie® Blue StainingDescription:Human B7 homolog 3 (B7-H3) is a member of the B7 family of immune proteins that provide signals for the regulation of immune responses. Other family members include B7-1, B7-2, B7-H1/PD-L1, B7-H2, and PD-L2. B7 family proteins are type I transmembrane immunoglobulin (Ig) superfamily members that contain extracellular Ig V‑like and Ig C‑like domains with a short cytoplasmic tail. Among the family members there is about 20 - 40% amino acid (aa) sequence identity. B7-H3 was initially reported to be a 316 aa type I transmembrane precursor protein that contained a signal sequence, an extracellular region with one V‑type and one C‑type Ig domain, a transmembrane segment and a short cytoplasmic tail. Subsequent studies have identified a second 110 kDa form whose precursor is 534 aa in length. Termed 4IgB7-H3 or B7-H3b, this molecule has two additional Ig-like domains (one V‑type and one C‑type) and shows a ubiquituous expression pattern. It would appear that the human 4Ig form is the principal, if not the only form of B7-H3. Its precursor contains a 26 aa signal sequence, a 435 aa extracellular region, a 31 aa transmembrane domain, and a 42 aa cytoplasmic tail. The four Ig-like domains alternate between V‑type and C‑type, and apparently are the consequence of a V‑C type tandem duplication. B7-H3b is expressed on dendritic cells as well as activated T, B and NK cells. The mouse gene differs from that of human in that it cannot code for four Ig-like domains; only a V‑type:C‑type pair. Human B7-H3b binding to an undefined receptor has shown to be inhibitory to NK cell illing and cytokine release. It also seems to be required for late stage osteoblast differentiation... Read More | 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 | Purity:>90%, by SDS-PAGE visualized with Coomassie® Blue Staining.Implicated in the control of cell proliferation and cellular aging. May also act as a chaperone |