| Description | DCX Human Pre-designed siRNA Set A contains three designed siRNAs for DCX gene (Human), as well as a negative control, a positive control, and a FAM-labeled negative control. Components DCX siRNA-1: 5 nmol (HPLC) DCX siRNA-2: 5 nmol (HPLC) DCX siRNA-3: 5 nmol (HPLC) siRNA Negative Control: 5 nmol (DCX Human Pre-designed siRNA Set A contains three designed siRNAs for DCX gene (Human), as well as a negative control, a positive control, and a FAM-labeled negative control. Components DCX siRNA-1: 5 nmol (HPLC) DCX siRNA-2: 5 nmol (HPLC) DCX 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 | Purity＞95% SDS-PAGE.FunctionImportant adipokine involved in the control of fat metabolism and insulin sensitivity, with direct anti-diabetic, anti-atherogenic and anti-inflammatory activities. Stimulates AMPK phosphorylation and activation in the liver and the skeletal muscle, enhancing Purity＞95% SDS-PAGE.FunctionImportant adipokine involved in the control of fat metabolism and insulin sensitivity, with direct anti-diabetic, anti-atherogenic and anti-inflammatory activities. Stimulates AMPK phosphorylation and activation in the liver and the skeletal muscle, enhancing glucose utilization and fatty-acid combustion. Antagonizes TNF-alpha by negatively regulating its expression in various tissues such as liver and macrophages, and also by counteracting its effects. Inhibits endothelial NF-kappa-B signaling through a cAMP-dependent pathway. May play a role in cell growth, angiogenesis and tissue remodeling by binding and sequestering various growth factors with distinct binding affinities, depending on the type of complex, LMW, MMW or HMW.Post-translationalHydroxylated Lys-33 was not identified in PubMed:16497731, probably due to poor representation of the N-terminal peptide in mass fingerprinting. HMW complexes are more extensively glycosylated than smaller oligomers. Hydroxylation and glycosylation of the lysine residues within the collagene-like domain of adiponectin seem to be critically involved in regulating the formation and/or secretion of HMW complexes and consequently contribute to the insulin-sensitizing activity of adiponectin in hepatocytes. O-glycosylated. Not N-glycosylated. O-linked glycans on hydroxylysines consist of Glc-Gal disaccharides bound to the oxygen atom of post-translationally added hydroxyl groups. Sialylated to varying degrees depending on tissue. Thr-22 appears to be the major site of sialylation. Higher sialylation found in SGBS adipocytes than in HEK fibroblasts. Sialylation is not required neither for heterodimerization nor for secretion. Not sialylated on the glycosylated hydroxylysines. Desialylated forms are rapidly cleared from the circulation... Read More | 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>95% SDS-PAGE. Protein Content and Purity (typically = 95%) determined by reducing and Non-reducing SDS-PAGE, UV spectroscopy at 280 nm.Additional sequence informationThis product is for the mature full length protein. The signal peptide is not included.FunctionCytokine with a wide variety Purity>95% SDS-PAGE. Protein Content and Purity (typically = 95%) determined by reducing and Non-reducing SDS-PAGE, UV spectroscopy at 280 nm.Additional sequence informationThis product is for the mature full length protein. The signal peptide is not included.FunctionCytokine with a wide variety of biological functions. It is a potent inducer of the acute phase response. Plays an essential role in the final differentiation of B-cells into Ig-secreting cells Involved in lymphocyte and monocyte differentiation. It induces myeloma and plasmacytoma growth and induces nerve cells differentiation Acts on B-cells, T-cells, hepatocytes, hematopoeitic progenitor cells and cells of the CNS. Also acts as a myokine. It is discharged into the bloodstream after muscle contraction and acts to increase the breakdown of fats and to improve insulin resistance.Post-translational:N- and O-glycosylated... Read More | The recombinant Protein A is a genetically engineering protein containing IgG-binding domains.Recombinant Protein A is ideal for purification of polyclonal or monoclonal IgG antibodies. Protein A binds to most human and mouse IgG subclasses (e.g., human IgG1, IgG2, IgG4; mouse IgG2, IgG2a, IgG2b,The recombinant Protein A is a genetically engineering protein containing IgG-binding domains.Recombinant Protein A is ideal for purification of polyclonal or monoclonal IgG antibodies. Protein A binds to most human and mouse IgG subclasses (e.g., human IgG1, IgG2, IgG4; mouse IgG2, IgG2a, IgG2b,IgG3). It also binds to cow, guinea pig, hamster, house, pig and rabbit total IgG form.Recombinant protein A can be coupled to solid separation medium (such as agarose) for monoclonaland polyclonal antibody purification. Recombinant protein A can be coupled to a variety of molecules (such as fluorescent molecules, enzyme markers, biotin, colloidal gold and radioactive markers). These coupled derivatives can be used in antibody test in the process of Western-blot, ELISA or immunohistochemical tests... Read More |