ELISA Kits

TNFsRI (also known as Solube tumor necrosis factor receptor 1) is a cytokine receptor that binds tumor necrosis factors(TNF). In contrast, the p60(TNFRSF1A) and p80(TNFRSF1B) TNFA receptors self-assemble through a distinct functional domain in the TNFR extracellular domain, termed the pre-ligand assembly domain(PLAD), in the absence of ligand. Deletion of the PLAD results in monomeric presentation of p60 or p80. Flow cytometric analysis showed that efficient TNFA binding depends on receptor self-assembly. They also found that other members of the TNF receptor superfamily, including the extracellular domains of TRAIL(TNFRSF10A), CD40, and FAS(TNFRSF6), all self-associate but do not interact with heterologous receptors. By Southern blot analysis of human/Chinese hamster somatic cell hybrid DNA, the TNFR1 gene was mapped to 12pter-cen. And by nonradioactive in situ hybridization that the type 1 receptor(the p55 TNF receptor) is encoded by a gene located on chromosome 12p13.2.

Tumor necrosis factor receptor 1 (TNFR1), also known as tumor necrosis factor receptor superfamily member 1A (TNFRSF1A) and CD120a, is a ubiquitous membrane receptor that binds tumor necrosis factor-alpha (TNF alpha). The protein encoded by this gene is a member of the tumor necrosis factor receptor superfamily, which also contains TNFRSF1B. And this protein is one of the major receptors for the tumor necrosis factor-alpha. This receptor can activate the transcription factor NF-kB, mediate apoptosis, and function as a regulator of inflammation. Antiapoptotic protein BCL2-associated athanogene 4 (BAG4/SODD) and adaptor proteins TRADD and TRAF2 have been shown to interact with this receptor, and thus play regulatory roles in the signal transduction mediated by the receptor.

Tumor necrosis factor receptor p75(TNF-R p75, or TNF-R2) is a 75-kDa type I transmembrane protein expressed predominantly on cells of hematopoietic lineage. TNF-R p75 belongs to the TNF receptor superfamily characterized by cysteine-rich extracellular regions composed of three to six disulfide-linked domains. The tumor necrosis factor receptor II(TNFRII) gene localizes to 1p36. 2, a genomic region characteristically deleted in neuroblastomas and other malignancies. In addition, TNFRII is the principal mediator of the effects of TNF on cellular immunity, and it may cooperate with TNFRI in the killing of nonlymphoid cells. The standard product used in this kit is recombinant human sTNFRII, consisting of 24-206 amino acid sequence with the molecular mass of 20KDa.

Tumor necrosis factor receptor 2(TNFR2) is one of receptors of TNF. TNF has proinflammatory and immunosuppressive properties that may segregate at the level of the 2 TNF receptors(TNFRs), TNFR1 and TNFR2. The genes for TNFR1, a 55-kDa protein, and TNFR2, a 70-kDa protein, have been mapped to human chromosomes 12(12pter-cen) and 1(1pter-p32), respectively. TNFR2 was induced on glomerular endothelial cells of nephritic kidneys, and TNFR2 expression on intrinsic cells, but not leukocytes, was essential for glomerulonephritis and glomerular complement deposition. TNFR1 promotes systemic immune responses and renal T cell death, while intrinsic cell TNFR2 plays a critical role in complement-dependent tissue injury. Therefore, therapeutic blockade specifically of TNFR2 may be a promising strategy in the treatment of immune-mediated glomerulonephritis.

In the field of cell biology, TNF-related apoptosis-inducing ligand(TRAIL), is a protein which functions as a ligand which induces the process of cell death called apoptosis. TRAIL has also been designated CD253(cluster of differentiation 253).Tumor necrosis factor(TNF) family cytokines function as prominent mediators of immune regulation and the inflammatory response. Most TNF family cytokines are expressed as type II transmembrane proteins, with homology confined to approximately 150 C-terminal residues. The TNF ligands interact with a parallel family of receptors. TRAIL binds to the death receptors DR4(TRAIL-RI) and DR5(TRAIL-RII). The process of apoptosis is caspase-8-dependent. Caspase-8 activates downstream effector caspases including procaspase-3, -6, and -7, leading to activation of specific kinases. TRAIL also binds the receptors DcR1 and DcR2, which do not contain a cytoplasmic domain(DcR1) or contain a truncated death domain(DcR2). The standard product used in this kit is re

Plasminogen activator,urokinase(PLAU, uPA) converts plasminogen to plasmin. Plasmin is involved in processing of amyloid precursor protein and degrades secreted and aggregated amyloid-beta, a hallmark of Alzheimer disease(AD). Urokinase has a molecular mass of about 54 kD and is composed of 2 disulfide-linked chains, A and B, of molecular masses 18 kD and 33 kD, respectively. It localized on 10q24. uPA facilitates cell migration by localizing proteolisys on the cell surface and by inducing intracellular signalling pathways. In human vascular smooth muscle cell(VSMC), uPA stimulates migration via the uPA receptor(uPAR) signalling complex containing TYK2 and phosphatidylinositol 3-kinase(PI3-K).

The urokinase-type plasminogen activator receptor(uPAR) is a key molecule in the regulation of cell-surface plasminogen activation and, as such, plays an important role in many normal as well as pathological processes. The cDNA for Mo3, an activation antigen expressed by human monocytes and myelomonocytic cell lines after stimulation by a variety of agents. Mo3 expression in vivo is associated predominantly with macrophages in inflammatory sites. It is a highly glycosylated protein of about 50 kD in monocytes where it is anchored to the plasma membrane by glycosyl-phosphatidylinositol linkage. The complete coding sequence of the cDNA has been found to encode 419 amino acids including a predicted signal peptide of 22 residues and a hydrophobic C-terminal portion. Mo3 is identical to the human receptor for the urokinase plasminogen activator. UPAR is a useful prognostic marker for biologically aggressive forms of endometrial cancer. PLAUR is located at chromosome 19q13.1-q13.2. The stand

Vascular cell adhesion molecule 1(VCAM-1) is a cell surface glycoprotein adhesive for certain blood leukocytes and tumor cells, which is expressed by activated endothelium in a variety of pathologic conditions including atherosclerosis. Increased expression of VCAM1 is associated with a variety of chronic inflammatory conditions, making its expression and function a target for therapeutic intervention. Integrin alpha4beta1(VLA-4) and VCAM-1 facilitate a critical cell-cell adhesion event required for survival of endothelial and mural cells during vascularization. The VCAM1 gene is assigned to the 1p31-32 region of chromosome 1 based on the analysis of human-mouse hybrid cell lines and in situ hybridization. The standard product used in this kit is recombinant mouse VCAM-1, a dimeric protein linking with a disulfide bond. It consists of Phe25-Glu698 amino acid sequence of a single chain with the molecular mass of 101.9KDa. As a result of glycosylation, the molecular mass of 120KDa is rev