| Description | DNAJC30 Human Pre-designed siRNA Set A contains three designed siRNAs for DNAJC30 gene (Human), as well as a negative control, a positive control, and a FAM-labeled negative control. Components DNAJC30 siRNA-1: 5 nmol (HPLC) DNAJC30 siRNA-2: 5 nmol (HPLC) DNAJC30 siRNA-3: 5 nmol (HPLC) siRNA DNAJC30 Human Pre-designed siRNA Set A contains three designed siRNAs for DNAJC30 gene (Human), as well as a negative control, a positive control, and a FAM-labeled negative control. Components DNAJC30 siRNA-1: 5 nmol (HPLC) DNAJC30 siRNA-2: 5 nmol (HPLC) DNAJC30 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>90% SDS-PAGE.Background:Luteinizing Hormone (LH) is a 42 kDa heterodimer belonging to the glycoprotein hormone family. It is composed of noncovalently linked glycosylated alpha and beta chains. The alpha subunit (CG alpha ) is also a component of Follicle-Stimulating Hormone (FSH), ThyroidPurity>90% SDS-PAGE.Background:Luteinizing Hormone (LH) is a 42 kDa heterodimer belonging to the glycoprotein hormone family. It is composed of noncovalently linked glycosylated alpha and beta chains. The alpha subunit (CG alpha ) is also a component of Follicle-Stimulating Hormone (FSH), Thyroid-Stimulating Hormone, and Chorionic Gonadotropin. The unique beta subunit confers the protein’s specific biological action and is responsible for the interaction with its receptor. The approximately 20 kDa human CG alpha subunit shares 73% and 72% amino acid (aa) sequence identity with the mouse and rat orthologs, respectively. The approximately 18 kDa human LH beta subunit shares 71% and 72% aa sequence identity with the mouse and rat orthologs, respectively. Multiple isoforms of LH exist due to differences in the post-translational glycosylation, sialylation, and sulphation modifications of its subunits. The composition, longevity, and activity of the different LH isoforms vary throughout a woman’s menstrual cycle and reproductive life cycle. LH is produced and secreted by the anterior pituitary gland. Its secretion is controlled by Gonadotropin-Releasing Hormone from the hypothalamus; however, LH secretion can also be stimulated by estradiol. LH works in concert with FSH to regulate female reproduction; FSH stimulates follicular growth and LH induces ovulation. LH also drives formation of the corpus luteum by promoting progesterone production. Additionally, LH has been suggested to stimulate the adrenal gland in postmenopausal women to induce secretion of sulfated DHEA, a precursor to androgens. In the testis, LH induces Leydig cell production of testosterone. Hypersecretion of LH has been shown to occur in women with polycystic ovary syndrome and is associated with an increased risk of infertility and miscarriage. Additionally, increased serum LH levels are associated with decreased cognition and have been implicated in the development and progression of Alzheimer’s disease. receptor into an A-frame... Read More | Purity:>95%, by SDS-PAGE visualized with Coomassie® Blue StainingDescription:NG2, also known as CSPG4, MCSP, and AN2, is a 400-500 kDa transmembrane chondroitin sulfate proteoglycan (CSPG) with a protein core of approximately 300 kDa. The extracellular region can be proteolytically shed fromPurity:>95%, by SDS-PAGE visualized with Coomassie® Blue StainingDescription:NG2, also known as CSPG4, MCSP, and AN2, is a 400-500 kDa transmembrane chondroitin sulfate proteoglycan (CSPG) with a protein core of approximately 300 kDa. The extracellular region can be proteolytically shed from the cell surface. Mature human NG2 consists of a 2195 amino acid (aa) extracellular domain (ECD), a 21 aa transmembrane segment, and a 77 aa cytoplasmic domain. Within aa 1583-2224, human NG2/CSPG4 shares 83% aa sequence identity with mouse and rat CSPG4. NG2 binds to the extracellular matrix proteins Laminin, Tenascin, and Collagens II, V, and VI as well as to the growth factors FGF-2 and PDGF-AA. NG2 is expressed on glial cell progenitors known as O2A cells or NG2 glia. These cells are neuronally responsive and differentiate primarily into oligodendrocytes but also into astrocytes. NG2 associates with PDGF R alpha and the AMPA R subunit GluR2. It is up-regulated on microglial cells during inflammation and contributes to the induction of inflammatory mediators. Various CSPGs in the brain inhibit neurite outgrowth through interactions with Nogo Receptor/NgR1 and NgR3. This recombinant protein product corresponds to the last 5 CSPG repeats, a region which can independently inhibit neurite outgrowth. NG2 is also expressed on vascular mural cells and capillaries. It promotes vascular endothelial cell (EC) migration and angiogenesis through interactions with Galectin-3 and Integrin alpha 3 beta 1 on EC, Plasminogen, and Angiostatin. NG2 is also expressed on a variety of tumors where it contributes to tumor cell adhesion, motility, and invasion... Read More | Purity:>90%, by SDS-PAGE visualized with Coomassie® Blue Staining.Description:BIRC5, also known as Survivin and EPR-1, is a member of theIAP family. IAP family members usually contain multiple baculovirus IAP repeat (BIR) domains, but BIRC5 has only a single BIR domain. It is expressed cell Purity:>90%, by SDS-PAGE visualized with Coomassie® Blue Staining.Description:BIRC5, also known as Survivin and EPR-1, is a member of theIAP family. IAP family members usually contain multiple baculovirus IAP repeat (BIR) domains, but BIRC5 has only a single BIR domain. It is expressed cell cycle-dependently and highly expressed at mitosis. As a multitasking protein, BIRC5 has dual roles in promoting cell proliferation and preventing apoptosis. Survivin is a component of a chromosome passage protein complex (CPC) which is essential for chromosome alignment and segregation during mitosis and cytokinesis. Survivin acts as an important regulator of the localization of this complex. It may counteract a default induction of apoptosis in G2/M phase... Read More | Background：Tumor necrosis factor alpha (TNF-alpha ), also known as cachectin and TNFSF2, is the prototypic ligand of the TNF superfamily. It is a pleiotropic molecule that plays a central role in inflammation, immune system development, apoptosis, and lipid metabolism. Rat TNF-alpha consisitsBackground：Tumor necrosis factor alpha (TNF-alpha ), also known as cachectin and TNFSF2, is the prototypic ligand of the TNF superfamily. It is a pleiotropic molecule that plays a central role in inflammation, immune system development, apoptosis, and lipid metabolism. Rat TNF-alpha consisits of a 35 amino acid (aa) cytoplasmic domain, a 21 aa transmembrane segment, and a 179 aa extracellular domain (ECD). Within the ECD, rat TNF-alpha shares 94% aa sequence identity with mouse and 69%-76% with bovine, canine, cotton rat, equine, feline, human, porcine, and rhesus TNF-alpha. TNF-alpha is produced by a wide variety of immune, epithelial, endothelial, and tumor cells. TNF-alpha is assembled intracellularly to form a noncovalently linked homotrimer which is expressed on the cell surface. Cell surface TNF-alpha can induce the lysis of neighboring tumor cells and virus infected cells, and it can generate its own downstream cell signaling following ligation by soluble TNFR I. Shedding of membrane bound TNF-alpha by TACE/ADAM17 releases the bioactive cytokine, a 55 kDa soluble trimer of the TNF-alpha extracellular domain. TNF-alpha binds the ubiquitous 55-60 kDa TNF RI and the hematopoietic cell-restricted 80 kDa TNF RII, both of which are also expressed as homotrimers. Both type I and type II receptors bind TNF-alpha with comparable affinity, although only TNF RI contains a cytoplasmic death domain which triggers the activation of apoptosis. Soluble forms of both types of receptors are released and can neutralize the biological activity of TNF-alpha. Post-translational modificationsThe soluble form derives from the membrane form by proteolytic processing.The membrane form, but not the soluble form, is phosphorylated on serine residues.Dephosphorylation of the membrane form occurs by binding to soluble TNFRSF1A/TNFR1.O-glycosylated; glycans contain galactose, N-acetylgalactosamine and N-acetylneuraminic acid... Read More |