ELISA

Insulin-like growth factor-binding protein 7 is a protein that in humans is encoded by the IGFBP7 gene. The gene was mapped to chromosome 4q12. The major function of the protein is the regulation of availability of insulin-like growth factors(IGFs) in tissue as well as in modulating IGF binding to its receptors. IGFBP7 binds to IGF with high affinity. It also stimulates cell adhesion. The protein is implicated in some cancers.

OX-2 membrane glycoprotein, also known as CD200 is a human protein encoded by the CD200 gene. This gene is mapped to 3q13.2. The protein encoded by this gene is a type-1 membrane glycoprotein, which contains two immunoglobulin domains, and thus belongs to the immunoglobulin superfamily. Studies of the related genes in mouse and rat suggest that this gene may regulate myeloid cell activity and delivers an inhibitory signal for the macrophage lineage in diverse tissues. It is suggested that CD200-CD200R signaling plays a central role in macrophage fusion and osteoclast formation.

Fibroblast growth factor 21 is a protein that in humans is encoded by the FGF21 gene. By genomic sequence analysis, Nishimura et al.(2000) identified the FGF21 gene within the 5-prime flanking region of the FUT1 gene on chromosome 19. The protein encoded by this gene is a member of the fibroblast growth factor(FGF) family. FGF family members possess broad mitogenic and cell survival activities and are involved in a variety of biological processes including embryonic development, cell growth, morphogenesis, tissue repair, tumor growth and invasion. FGF21 stimulates glucose uptake in adipocytes but not in other cell types. This effect is additive to the activity of insulin. FGF21 treatment of adipocytes is associated with phosphorylation of FRS2, a protein linking FGF receptors to the Ras/MAP kinase pathway. FGF21 injection in ob/ob mice results in an increase in Glut1 in adipose tissue. FGF21 also protects animals from diet-induced obesity when overexpressed in transgenic mice and lower

CD166 antigen is a 100-105 kD typeI transmembrane glycoprotein that is a member of the immunoglobulin superfamily of proteins. In humans it is encoded by the ALCAM gene. The gene was mapped to human chromosome 3q13.1-q13.2 by fluorescence in situ hybridization of cDNA probes to metaphase chromosomes. It is also called CD166(cluster of differentiation 166), MEMD, SC-1/DM-GRASP/BEN in the chicken, and KG-CAM in the rat. It is expressed on activated T cells, activated monocytes, epithelial cells, fibroblasts, neurons, melanoma cells, and also in sweat and sebaceous glands. CD166 protein expression is reported to be upregulated in a cell line deriving from a metastasizing melanoma. CD166 plays an important role in mediating adhesion interactions between thymic epithelial cells and CD6+ cells during intrathymic T cell development. Recently, CD166 has also been used as a potential cancer stem cell marker.

Matrix metalloproteinase-12(MMP12), also known as MME or ME, is an enzyme that in humans is encoded by the MMP12 gene. The gene is part of a cluster of MMP genes which localize to chromosome 11q22.2. It is thought that the protein encoded by this gene is cleaved at both ends to yield the active enzyme, but this processing has not been fully described. The enzyme degrades soluble and insoluble elastin. It may play a role in aneurysm formation and studies in mice suggest a role in the development of emphysema. This gene may involved in tissue injury and remodeling.

Tumor necrosis factor receptor superfamily, member4, also known as ACT35 or CD134 is a cell surface glycoprotein that was discovered through the production of a monoclonal antibody raised against the HUT-102 cell line. It belongs to the tumor necrosis factor receptor superfamily. CD134 was mapped to 1p36 by fluorescence in situ hybridization. CD134 is the primary receptor for feline immunodeficiency virus. CD134 expression can promote viral binding and renders cells permissive for viral entry, productive infection, and syncytium formation. Stimulating the receptor can improve the response to a powerful virus vector and may be useful in vaccine development.

Intercellular adhesion molecule 2(ICAM2), also known as CD102(Cluster of Differentiation 102) is an integral membrane protein that has 2 immunoglobulin-like domains. This gene is mapped to 17q23.3. The protein encoded by this gene is a member of the intercellular adhesion molecule(ICAM) family. All ICAM proteins are type I transmembrane glycoproteins, contain 2-9 immunoglobulin-like C2-type domains, and bind to the leukocyte adhesion LFA-1 protein. This protein may play a role in lymphocyte recirculation by blocking LFA-1-dependent cell adhesion. It mediates adhesive interactions important for antigen-specific immune response, NK-cell mediated clearance, lymphocyte recirculation, and other cellular interactions important for immune response and surveillance.

Interleukin-31, also known as IL-31 is a protein that in humans is encoded by the IL31 gene. The IL31 gene is mapped to chromosome 12q24.31 and the mouse gene maps to a syntenic region on chromosome 5. IL31, which is made principally by activated Th2-type T cells, interacts with a heterodimeric receptor consisting of IL31RA and OSMR that is constitutively expressed on epithelial cells and keratinocytes. IL31 may be involved in the promotion of allergic skin disorders and in regulating other allergic diseases, such as asthma.

FAP(Fibroblast Activation Protein, Alpha) also known as FAPA or SEPRASE, is an inducible cell surface glycoprotein that was originally identified in cultured fibroblasts using monoclonal antibody F19. The protein encoded by this gene is a homodimeric integral membrane gelatinase belonging to the serine protease family. The FAP gene is mapped on 2q24.2. FAP is most closely related to DPPIV and they share about 50% of their amino acids. FAP is catalytically active as a 170kD dimer and has dipeptidase and gelatinase activity. Its gelatinase activity requires a glycine in P2 position. FAP-alpha shows 48% amino acid identity with dipeptidyl peptidase IV and 30% identity with DPP4-related protein. Northern blot analysis detected a 2.8-kb FAP-alpha mRNA in fibroblasts. Depletion of FAP-expressing cells, which made up only 2% of all tumor cells in established Lewis lung carcinomas, caused rapid hypoxic necrosis of both cancer and stromal cells in immunogenic tumors by a process involving inter