ELISA

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.

KIM1(TIM-1), also known as Hepatitis A virus cellular receptor 1, is a protein that in Rats 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, the HAVCR1 gene was mapped to 5q33.2.

Bone morphogenetic protein 7 or BMP7(also known as osteogenic protein-1 or OP-1) is a protein that in humans is encoded by the BMP7 gene. The protein encoded by this gene is a member of the TGF-beta superfamily. Like other members of the bone morphogenetic protein family of proteins, it plays a key role in the transformation of mesenchymal cells into bone and cartilage. It is inhibited by noggin and a similar protein, chordin, which are expressed in the Spemann-Mangold Organizer. BMP7 may be involved in bone homeostasis. It is expressed in the brain, kidneys and bladder.

Endostatin is a naturally-occurring 20-kDa C-terminal fragment derived from type XVIII collagen. It is reported to serve as an anti-angiogenic agent, similar to angiostatin and thrombospondin. And it is produced by proteolytic cleavage of collagen XVIII, a member of the multiplexin family that is characterized by interruptions in the triple helix creating multiple domains, by proteases such as cathepsins. Using a genomic clone as a probe for fluorescence in situ hybridization, Endostatin was mapped the COL18A1 gene to 21q22.3. By immunoprecipitation analysis using membrane fractions of human mammary epithelial cells, It showed that endostatin specifically bound to cell surface nucleolin with high affinity. Blockage of nucleolin with neutralizing antibody or knockdown of nucleolin by RNA interference countered the antiendothelial activity of endostatin and abrogated its antiangiogenic and antitumor activity in vivo.

HMOX1 (heme oxygenase (decycling) 1) is a human gene that encodes for the enzyme heme oxygenase 1. It is localized to chromosome 22. Heme oxygenase, an essential enzyme in heme catabolism, cleaves heme to form biliverdin, which is subsequently converted to bilirubin by biliverdin reductase, and carbon monoxide, a putative neurotransmitter. Heme oxygenase activity is induced by its substrate heme and by various nonheme substances. Heme oxygenase occurs as 2 isozymes, an inducible heme oxygenase-1 and a constitutive heme oxygenase-2. HMOX1 and HMOX2 belong to the heme oxygenase family.