ELISA

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.

P53(also known as protein 53 or tumor protein 53), is a tumor suppressor protein that in humans is encoded by the TP53 gene. The human P53 gene is mapped to chromosome 17. Human p53 is 393 amino acids long and has seven domains. It runs as a 53-kilodalton(kDa) protein on SDS-PAGE. The pattern of p53 splicing was specific for brain areas and for individuals. And human kidney and heart expressed only full-length p53. It has played a vital role in conserving stability by preventing genome mutation.

Pigment epithelium-derived factor (PEDF) is also known as serpin F1 (SERPINF1). In humans, it is encoded by the SERPINF1 gene. PEDF has a variety of functions including antiangiogenic, antitumorigenic, and neurotrophic properties. It suppresses retinal neovascularization and endothelial cell proliferation. And Antiangiogenic function is also conferred by PEDF through inhibition of both VEGFR-1 and VEGFR-2. In addition, the antitumorigenic effects of PEDF are not only due to inhibition of supporting vasculature, but also due to effects on the cancer cells themselves. PEDF is shown to inhibit cancer cell proliferation and increase apoptosis via the FAS/FASL pathway. Expression of PEDF in the human retina is found at 7.4 weeks of gestation, suggesting it may play a role in retinal neuron differentiation.

Plasminogen activator, tissue, also called PLAT or TPA is a serine protease. This gene encodes tissue-type plasminogen activator, a secreted serine protease which converts the proenzyme plasminogen to plasmin, a fibrinolytic enzyme. Tissue-type plasminogen activator is synthesized as a single chain which is cleaved by plasmin to a two chain disulfide linked protein. This gene was mapped to 8p11.21. This enzyme plays a role in cell migration and tissue remodeling. Increased enzymatic activity causes hyperfibrinolysis, which manifests as excessive bleeding; decreased activity leads to hypofibrinolysis which can result in thrombosis or embolism.

Tryptases are serine proteases implicated in asthma and are highly expressed in human mast cells. They are derived from at least 4 nonallelic genes clustered on chromosome 16p13.3: TPSAB1, which represents the alpha and beta-I tryptase alleles; TPSB2, which represents the beta-II and beta-III tryptase alleles; TPSG1; and TPSD1. Elevated levels of serum tryptase occur in both anaphylactic and anaphylactoid reactions, but a negative test does not exclude anaphylaxis. Tryptase is less likely to be elevated in food allergy reactions as opposed to other causes of anaphylaxis.

Thrombospondin 1, also known as THBS1, is a protein that in humans in encoded by the THBS1 gene. Thrombospondin 1 is a subunit of a disulfide-linked homotrimeric protein. This protein is an adhesive glycoprotein that mediates cell-to-cell and cell-to-matrix interactions. By in situ hybridization, the THBS1 gene was mapped to human 15q15 and the cognate gene to mouse chromosome 2(region F) and was localized to 15q11-qter by Southern analysis of human-rodent somatic cell hybrids. Thrombospondin I is a multimodular secreted protein that associates with the extracellular matrix and possesses a variety of biologic functions, including a potent antiangiogenic activity. Other thrombospondin genes include thrombospondins II, III, and IV.