| Description | EMX2 Human Pre-designed siRNA Set A contains three designed siRNAs for EMX2 gene (Human), as well as a negative control, a positive control, and a FAM-labeled negative control. Components EMX2 siRNA-1: 5 nmol (HPLC) EMX2 siRNA-2: 5 nmol (HPLC) EMX2 siRNA-3: 5 nmol (HPLC) siRNA Negative Control: 5 EMX2 Human Pre-designed siRNA Set A contains three designed siRNAs for EMX2 gene (Human), as well as a negative control, a positive control, and a FAM-labeled negative control. Components EMX2 siRNA-1: 5 nmol (HPLC) EMX2 siRNA-2: 5 nmol (HPLC) EMX2 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 | Protein Purity≥85% by SDS PAGEExtinction CoeffA280 nm = 0.631 at 1.0 mg/ml for pure C1qMolecular Weight400,000 Da (18 chains)General DescriptionRat C1q is purified from pooled normal rat serum. C1q is part of the C1 complex, which is the first complement component in the classical pathway of Protein Purity≥85% by SDS PAGEExtinction CoeffA280 nm = 0.631 at 1.0 mg/ml for pure C1qMolecular Weight400,000 Da (18 chains)General DescriptionRat C1q is purified from pooled normal rat serum. C1q is part of the C1 complex, which is the first complement component in the classical pathway of complement. The C1 complex is a non-covalent assembly of three different proteins (C1q, C1r, and C1s) bound together in a calcium-dependent complex. C1q has six extended arms with domains at the end of each arm that bind to the Fc domains of immunoglobulins such as IgG or IgM. When antibodies bind toantigens, forming immune complexes, they cluster allowing two or more of the six C1q arms to bind to the Fc domains of antibodies. Rat IgG2 is very efficient when compared to IgG1 in activating complement (Medgyesi, G.A et., al., 1981). This is in contrast to the human system in which IgG1 activates complement but not IgG2 (Redpath, S. et. al., 1998). The binding of multiple arms of C1q to immune complexes causes the two C1r proteins in the complex (protease zymogens) to auto-activate. The activated C1r proteases cleave and activate the two C1s protease zymogens in the complex. The activated C1s cleaves complement component C4 releasing C4a and initiating covalent attachment of C4b to the activating surface. Activated C1s also cleaves C2 and the larger fragment of C2 binds to the surface-attached C4b forming C4b,C2a, the C3/C5 convertase of the classical pathway.Rat IgG1 cannot activate complement whereas rat IgG2 does.Physical Characteristics & StructureThe apparent molecular weight of rat C1q as determined by gel filtration has been reported to be 400,000 by Veerhuis, R. et al., (1985) and is calculated to be 420,000 based on its amino acid sequence. Rat C1q is a high molecular weight complex of 18 polypeptide chains. Each of the six arms of rat C1q contains three chains, an A chain (~30,000 daltons), a B chain (~28,000 daltons) and a C chain (~26,000 daltons) as determined by SDS/polyacrylamide gel electrophoresis (Wing, M.G. et al., (1993)).FunctionThe biological functions of C1q are described above in the General Description and Physical Characteristics sections.ApplicationsRat C1q can be used to coat ELISA plates to capture and quantitate immune complexes in samples from rat models used for studying immune complex related diseases and conditions.GeneticsNCBI Gene ID numbers for rat C1q are: C1q A chain (298566), C1q B chain (29687), and C1q C chain (362634). The genes for C1q chains A, B and C are all located on chromosome 5. The UniprotKB primary accession numbers for rat C1q are: C1q A chain (P31720), C1q B chain (P31721), and C1q C chain (P31722).Precautions/Toxicity/HazardsThis protein is purified from animal plasma/serum and therefore precautions appropriate for handling any animal blood-derived product must be used.ReferencesMedgyesi, G.A et., Miklos, K., Kulics, J., Fust, G., and Gergely, J. Bazin, H. (1981). Classes and subclasses of rat antibodies: reaction with the antigen and interaction of the complex with the complement system. Immunology 43, 171-176.Redpath, S., Michaelsen, T., Sandlie, I. and Clark, M. R. (1998). Activation of complement by human IgG1 and human IgG3 antibodies against the human leucocyte antigen CD52. Immunology 93, 595–600.Veerhuis, R., Van Es, L.A. and Daha, M.R. (1985). In vivo degradation of rat C1q induced by intravenous injection of soluble IgG aggregates. Immunology 54, 801-810.Wing, M.G., Seilly, D. J., Bridgman, D.J. and Harrison, R.A. (1993). Rapid isolation and biochemical characterization of rat C1 and C1q. Molecular Immunology 30, 433-440... Read More | Biochemical Test:SDS-PAGE (purity > 80%); Western blot with patient sample.Calculated Isoelectric Point:pH 6.64 | Purity: >90%, by SDS-PAGE visualized with Coomassie® Blue Staining.Description：KGF (keratinocyte growth factor), also known as FGF-7 (fibroblast growth factor-7), is one of 22 known members of the mouse FGF family of secreted proteins that plays a key role in development, Purity: >90%, by SDS-PAGE visualized with Coomassie® Blue Staining.Description：KGF (keratinocyte growth factor), also known as FGF-7 (fibroblast growth factor-7), is one of 22 known members of the mouse FGF family of secreted proteins that plays a key role in development, morphogenesis, angiogenesis, wound healing, and tumorigenesis (1-4). KGF expression is restricted to cells of mesenchymal origin. When secreted, it acts as a paracrine growth factor for nearby epithelial cells (1). KGF speeds wound healing by being dramatically upregulated in response to damage to skin or internal structures that results in high local concentrations of inflammatory mediators such as IL-1 and TNF-alpha. (2, 5). KGF promotes cell migration and invasion, and mediates melanocyte transfer to keratinocytes upon UVB radiation (6, 7). It has been used ectopically to avoid chemotherapy-induced oral mucositis in patients with hematological malignancies (1). Deletion of KGF affects kidney development, producing abnormally small ureteric buds and fewer nephrons (8). It also impedes hair follicle differentiation (9). The 194 amino acid (aa) KGF precursor contains a 31 aa signal sequence and, like all other FGFs, an ~120 aa beta -trefoil scaffold that includes receptor- and heparin-binding sites. KGF signals only through the IIIb splice form of the tyrosine kinase receptor, FGF R2 (FGF R2-IIIb/KGF R) (10). Receptor dimerization requires an octameric or larger heparin or heparin sulfate proteoglycan (11). FGF-10, also called KGF2, shares 51% aa identity and similar function to KGF, but shows more limited expression than KGF and uses an additional receptor, FGF R2-IIIc (12). Following receptor engagement, KGF is typically degraded, while FGF-10 is recycled (12). Mature human KGF, which is active across species, shares 98% aa sequence identity with bovine, equine, ovine and canine, 96% with mouse and porcine, and 92% with rat KGF, respectively... Read More | Purity: >95%, by SDS-PAGE visualized with Coomassie® Blue Staining. Description： Mesothelin (MSLN), also known as CAK1 and ERC, is a glycosylated cell-surface antigen present on normal mesothelial cells and over-expressed in several human tumors. The mesothelin gene encodes a ~70 kDa Purity: >95%, by SDS-PAGE visualized with Coomassie® Blue Staining. Description： Mesothelin (MSLN), also known as CAK1 and ERC, is a glycosylated cell-surface antigen present on normal mesothelial cells and over-expressed in several human tumors. The mesothelin gene encodes a ~70 kDa precursor protein that is cleaved at a dibasic proteolytic site into a 40 kDa membrane-bound protein termed MSLN and a 31 kDa shed fragment called megakaryocyte-potentiating factor (MPF) that is released from the cell. Cleaved, human MSLN remains attached to the cell surface via a GPI linkage and shares 58% amino acid sequence identity with mouse and rat MSLN. In human, alternate splicing generates additional MSLN isoforms that have either an eight amino acid insertion following Ser408 or a substituted C‑terminal region with no GPI anchor. Mesothelin is normally expressed on mesothelial cells in the pleura, pericardium, and peritoneum as well as in the developing and postnatal pancreas. It is up‑regulated in mesotheliomas and a range of carcinomas and adenomas. Mesothelin promotes tumor cell proliferation, migration, anchorage-independent growth, and tumor progression. It is co‑expressed with the tumor antigen CA125/MUC16 on advanced ovarian adenocarcinomas and interacts with this molecule to support cell adhesion. A soluble form of Mesothelin is released from tumor cells into the serum or tissue effusions... Read More |