| Description | BTG4 Human Pre-designed siRNA Set A contains three designed siRNAs for BTG4 gene (Human), as well as a negative control, a positive control, and a FAM-labeled negative control. Components BTG4 siRNA-1: 5 nmol (HPLC) BTG4 siRNA-2: 5 nmol (HPLC) BTG4 siRNA-3: 5 nmol (HPLC) siRNA Negative Control: 5 BTG4 Human Pre-designed siRNA Set A contains three designed siRNAs for BTG4 gene (Human), as well as a negative control, a positive control, and a FAM-labeled negative control. Components BTG4 siRNA-1: 5 nmol (HPLC) BTG4 siRNA-2: 5 nmol (HPLC) BTG4 siRNA-3: 5 nmol (HPLC) siRNA Negative Control: 5 nmol (HPLC) FAM-labeled siRNA Negative Control: 5 nmol (HPLC) GAPDH siRNA Positive Control:5 nmol (HPLC)... Read More | H-7 dihydrochloride blocks human immunodeficiency virus (HIV-1) replication in MOLT-4 (clone No. 8) cell line. It increases the secretion of interleukin 1β (IL-1β).Application：H-7 dihydrochloride has been used to study H-7-induced inhibition of contractility in rat embryo H-7 dihydrochloride blocks human immunodeficiency virus (HIV-1) replication in MOLT-4 (clone No. 8) cell line. It increases the secretion of interleukin 1β (IL-1β).Application：H-7 dihydrochloride has been used to study H-7-induced inhibition of contractility in rat embryo fibroblasts (REF52) cells and acts as a kinase inhibitor... Read More | Purity> 97 % by SDS-PAGE and HPLC analyses.Additional sequence informationThis product is for the mature full length protein. The signal peptide is not included.FunctionInhibits hemopoiesis and stimulates chemotaxis. Chemotactic in vitro for thymocytes and activated T-cells, but not for B-cells, Purity> 97 % by SDS-PAGE and HPLC analyses.Additional sequence informationThis product is for the mature full length protein. The signal peptide is not included.FunctionInhibits hemopoiesis and stimulates chemotaxis. Chemotactic in vitro for thymocytes and activated T-cells, but not for B-cells, macrophages, or neutrophils. Shows preferential activity towards naive T-cells. May play a role in mediating homing of lymphocytes to secondary lymphoid organs... Read More | Purity>97% by SDS-PAGE and HPLC analyses.FunctionMay be involved in macrophage-mediated cellular proliferation. It is mitogenic for fibroblasts and smooth muscle but not endothelial cells. It is able to bind EGF receptors with higher affinity than EGF itself and is a far more potent mitogen for Purity>97% by SDS-PAGE and HPLC analyses.FunctionMay be involved in macrophage-mediated cellular proliferation. It is mitogenic for fibroblasts and smooth muscle but not endothelial cells. It is able to bind EGF receptors with higher affinity than EGF itself and is a far more potent mitogen for smooth muscle cells than EGF. Also acts as a diphtheria toxin receptor.Background:Human HB-EGF (Heparin-Binding EGF-like growth factor) is a 12-16 kDa member of the EGF family of peptide growth factors (1-3). Also known as the DTR (diphtheria toxin receptor), it is further classified as a group 2 ErbB ligand based on its ability to activate both the EGF/ErbB1 and ErbB4 receptors (4, 5). HB-EGF is synthesized as a 208 amino acid (aa) type I transmembrane preproprecursor (1, 6). It contains a 19 aa signal sequence, a 43 aa prosegment, an 86 aa mature region (aa 63-148), an 11 aa juxtamembrane cleavage peptide, a 24 aa transmembrane segment, and a 25 aa cytoplasmic tail (aa 184-208). As an integral membrane protein, HB-EGF is expressed as a 19-27 kDa protein in mammalian cells (7-9). The variability in molecular weight (MW) is attributed to heterogeneity in glycosylation and/or the utilization of multiple proteolytic cleavage sites during maturation. Mature HB-EGF is a soluble peptide that arises from proteolytic processing of the transmembrane form. It possesses an EGF-like domain between aa 104-144, and a heparin-binding motif between aa 93‑113. Although the aa range for "mature" HB-EGF is typically stated to be Asp63-Leu148, potential N-terminal start (cleavage) sites also exist at Gly32, Arg73, Val74, Ser77 and Ala82 (8, 10-12). Thus, differential processing (in part) likely accounts for the 16-23 kDa range in MW noted for mammalian-derived mature HB-EGF. Proteases suggested to contribute to HB-EGF processing include TACE, MMP-3 and -7, ADAM-17 and ADAM-12 (11, 13-16). When expressed recombinantly in E.coli, HB-EGF (aa 73-148) runs at 14 kDa in SDS-PAGE; when expressed in Baculovirus, HB-EGF (aa 63-148, 77-148 and 32-148) runs at 18 kDa, 15 kDa, and 19 kDa respectively (8, 12, 17). Over aa 63-148, human HB-EGF- shares 76% and 73% aa sequence identity with rat and mouse HB-EGF, respectively (1, 18). Cells known to express HB-EGF include bronchial epithelium (19), visceral and vascular smooth muscle (20, 21), CD4+ T cells (22), cardiac muscle (23), glomerular podocytes (24), keratinocytes (13) and IL-10-secreting regulatory macrophages (25). As noted earlier, HB-EGF is known to bind to both 170 kDa EGFR and 180 kDa ErbB4, and through heterodimerization, ErbB2 (13, 26). Activity associated with ErbB4 binding appears to be limited to non-mitogenic actions, while EGFR binding induces both mitogenic and non-mitogenic activity... Read More | SHP2 protein degrader-2 (SHP2-D26) is a SHP2 protein PROTAC degrader. SHP2 protein degrader-2 reduces expression level of SHP2 in various cancer cells.In VitroSHP2 protein degrader-2 (SHP2-D26) achieves excellent degradation of SHP2 with the DC 50 (the concentration where 50% of the protein has beenSHP2 protein degrader-2 (SHP2-D26) is a SHP2 protein PROTAC degrader. SHP2 protein degrader-2 reduces expression level of SHP2 in various cancer cells.In VitroSHP2 protein degrader-2 (SHP2-D26) achieves excellent degradation of SHP2 with the DC 50 (the concentration where 50% of the protein has been degraded) values of 2.6 nM and 6.0 nM for MV4;11 and KYSE520 cells, respectively. MCE has not independently confirmed the accuracy of these methods. They are for reference only.Form:Solid... Read More |