ELISA

PTX3(Pentraxin 3) is a member of the pentraxin superfamily. This super family characterized by cyclic multimeric structure. The PTX3 gene is mapped to 3q25.32. The predicted 381-amino acid PTX3 protein has homology to the pentraxin protein family. Significant levels of PTX3 were detected in plasma of neutropenic patients with systemic A. PTX3 is effective in preventing CMV infection and reactivation, as well as subsequent Aspergillus infection. PTX3 activates the classical pathway of complement activation and facilitates pathogen recognition by macrophages and DCs.

Interleukin(IL)-18, also called Interferon-gamma-inducing factor(IGIF), augments natural killer(NK) activity in spleen cells. The gene encodes a precursor protein of 192 amino acids and a mature protein of 157 amino acids.1 IL-18 is a recently discovered cytokine that modulates both T helper type 1(Th1) and Th2 responses.2 IL-18 is a potent proinflammatory cytokine with potential atherogenic properties. It is highly expressed in the atherosclerotic plaques compared with control normal arteries and is localized mainly in plaque macrophages.3

Interleukin-23 subunit alpha(IL-23) is a protein that in humans is encoded by the IL23A gene. IL-23 is a heterodimeric cytokine consisting of two subunits, one called p40, which is shared with another cytokine, IL-12, and another called p19(the IL-23 alpha subunit). IL-23 is an important part of the inflammatory response against infection. It promotes upregulation of the matrix metalloprotease MMP9, increases angiogenesis and reduces CD8+ T-cell infiltration. Recently, IL-23 has been implicated in the development of cancerous tumors. he International Radiation Hybrid Mapping Consortium mapped the p19 gene to chromosome 12(stSG47812).

Dickkopf-related protein 1 is a protein that in humans is encoded by the DKK1 gene, which was mapped to chromosome 10q11.2. This gene encodes a protein that is a member of the dickkopf family. It is a secreted protein with two cysteine rich regions and is involved in embryonic development through its inhibition of the WNT signaling pathway. Elevated levels of DKK1 in bone marrow, plasma and peripheral blood is associated with the presence of osteolytic bone lesions in patients with multiple myeloma.

FSTL3(Follistatin-Like 3) also known as FLRG or FOLLISTATIN-RELATED GENE, is a member of the follistatin-module protein family, which is composed of extracellular matrix-associated glycoproteins thought to act in a paracrine manner to bind morphogens or growth/differentiation factors and regulate their activity during development. The FSTL3 gene extends over 7 kbp and contains 5 exons. The FSTL3 gene was localized to chromosome 19p13. This gene involved in hematopoiesis and in differentiation of hemopoietic progenitor cells, increases hematopoietic cell adhesion to fibronectin and seems to contribute to the adhesion of hematopoietic precursor cells to the bone marrow stroma. It may have a role in leukemogenesis.

Human platelet/endothelial cell adhesion molecule-1(PECAM1), an important member of the immunoglobulin gene superfamily, is widely distributed on cells of the vascular system and mediates cellular interactions through both homophilic and heterophilic adhesive mechanisms. The function of PECAM1 in vitro has begun to be understood, but its function in vivo is yet to be established.1 The PECAM1 locus is on the long arm of chromosome 17, in the region q23-qter. To confirm this observation and obtain a more precise localization of the PECAM1 locus, fluorescence in situ hybridization was conducted. Together our data allowed assignment of the PECAM1 locus to the region 17q23.2 To examine the functional role of PECAM-1 in regulating platelet-collagen interactions, 2 different approaches were applied using recombinant human PECAM-1-immunoglobulin chimeras and platelets derived from PECAM-1-deficient mice.3 PECAM-1, an integral membrane protein with an essential role in TEM, is found in this com

PECAM-1 is an important target GP in DITP.1 Platelet/endothelial cell adhesion molecule-1(PECAM-1) is a 130-kD member of the Ig gene superfamily that is expressed on the surface of circulating platelets, monocytes, neutrophils, and selective T-cell subsets.2 Platelet endothelial cell adhesion molecule-1(PECAM-1/CD31) is a member of the immunoglobulin(Ig) superfamily that has distinctive features of an immunoreceptor based upon its genomic structure and the presence of intrinsic immunoreceptor tyrosine inhibitory motifs(ITIMs) in its ligand binding polypeptide.3 PECAM-1 has recently been shown to contain functional immunoreceptor tyrosine-based inhibitory motifs(ITIMs) within its cytoplasmic domain, and co-ligation of PECAM-1 with the T-cell antigen receptor(TCR) results in tyrosine phosphorylation of PECAM-1, recruitment of Src homology 2 domain-containing protein tyrosine phosphatase-2(SHP-2), and attenuation of TCR-mediated cellular signaling.4 The standard used in this kit is the pr

KIM1(TIM-1), also known as Hepatitis A virus cellular receptor 1, is a protein that in Mouses is encoded by the HAVCR1 gene.[1][2][3] Infection of canine osteogenic sarcoma cells expressing HAVCR1 with HAV led Feigelstock et al.(1998) to conclude that the protein is indeed a receptor for the virus. Immunofluorescence microscopy demonstrated internalization of HAV by dog cells expressing HAVCR1. Using a monoclonal antibody to mouse Tim1, Umetsu et al.(2005) showed that Tim1 was expressed after activation of naive T cells and on T cells differentiated in Th2-polarizing conditions. By homology of synteny with the mouse Tim1 gene and database analysis, McIntire et al.(2001) mapped the HAVCR1 gene to 5q33.2. The standard used in this kit is recombinant mouse KIM-1, constituting from Y22-T212 amino acids, and 191amino acids with the molecular mass of 21.8KDa.

KIM1(TIM-1), also known as Hepatitis A virus cellular receptor 1, is a protein that in Rat is encoded by the HAVCR1 gene. Infection of canine osteogenic sarcoma cells expressing HAVCR1 with HAV led to conclude that the protein is indeed a receptor for the virus. Immunofluorescence microscopy demonstrated internalization of HAV by dog cells expressing HAVCR1. Using a monoclonal antibody to rat Tim1, Tim1 was expressed after activation of naive T cells and on T cells differentiated in Th2-polarizing conditions. By homology of synteny with the rat Tim1 gene and database analysis, was mapped the HAVCR1 gene to 5q33.2.