ELISA

Cathepsin D is a protein that in humans is encoded by the CTSD gene. This proteinase is a member of the peptidase C1 family, having a specificity similar to but narrower than that of pepsin A. It is mapped to 11p15.5. The cDNA encodes a 412-amino acid protein with 20 and 44 amino acids in a pre- and prosegment, respectively. Cathepsin D is one of the lysosomal proteinases. It is ubiquitously expressed and is involved in proteolytic degradation, cell invasion, and apoptosis. Mutations in this gene are involved in the pathogenesis of several diseases, including breast cancer and possibly Alzheimer disease and it has been considered as a breast cancer tumor marker.

Cathepsin L is an important lysosomal endopeptidase enzyme which is involved in the initiation of protein degradation. It also shows the most potent collagenolytic and elastinolytic activity in vitro of any of the cathepsins. The gene is mapped to 9q21-q22. It is a member of the Peptidase C1 family, which play an important role in diverse processes including normal lysosome mediated protein turnover, antigen and proprotein processing, and apoptosis. Cathepsin L has been reported in many organisms including fish, birds and mammals.

Cystatin C or cystatin 3(formerly gamma trace, post-gamma-globulin or neuroendocrine basic polypeptide), a protein encoded by the CST3 gene, was originally described as a constituent of normal cerebrospinal fluid(CSF) and of urine from patients with renal failure.1 Cystatin 3 has a low molecular weight(approximately 13.3 kilodaltons), and it is removed from the bloodstream by glomerular filtration in the kidneys. In humans, all cells with a nucleus(cell core containing the DNA) produce cystatin C as a chain of 120 amino acids. It is found in virtually all tissues and bodily fluids. Cystatin C, which belongs to the type II cystatin gene family, is a potent inhibitor of lysosomal proteinases2(enzymes from a special subunit of the cell that break down proteins) and probably one of the most important extracellular inhibitors of cysteine proteases3(it prevents the breakdown of proteins outside the cell by a specific type of protein degrading enzymes). Moreover, cystatin C is involved in net

Cystatin C or cystatin 3(formerly gamma trace, post-gamma-globulin or neuroendocrine basic polypeptide), a protein encoded by the CST3 gene, was originally described as a constituent of normal cerebrospinal fluid(CSF) and of urine from patients with renal failure. Cystatin 3 has a low molecular weight(approximately 13.3 kilodaltons), and it is removed from the bloodstream by glomerular filtration in the kidneys. In mouses, all cells with a nucleus(cell core containing the DNA) produce cystatin C as a chain of 120 amino acids. It is found in virtually all tissues and bodily fluids. Cystatin C, which belongs to the type II cystatin gene family, is a potent inhibitor of lysosomal proteinases(enzymes from a special subunit of the cell that break down proteins) and probably one of the most important extracellular inhibitors of cysteine proteases(it prevents the breakdown of proteins outside the cell by a specific type of protein degrading enzymes). Moreover, cystatin C is involved in networ

Carbonic anhydrase 9(CA9/CAIX) is an enzyme that in humans is encoded by the CA9 gene. Carbonic anhydrases(CAs) are a large family of zinc metalloenzymes that catalyze the reversible hydration of carbon dioxide. They participate in a variety of biological processes, including respiration, calcification, acid-base balance, bone resorption, and the formation of aqueous humor, cerebrospinal fluid, saliva, and gastric acid. This gene is mapped to 9p13.3. CA IX is a transmembrane protein and the only tumor-associated carbonic anhydrase isoenzyme known. It is expressed in all clear-cell renal cell carcinoma, but is not detected in normal kidney or most other normal tissues. It may be involved in cell proliferation and transformation.

Chemokine(C-C motif) ligand 7(CCL7) is a small cytokine known as a chemokine that was previously called monocyte-specific chemokine 3(MCP3). It belongs to the C-C chemokine family. By fluorescence in situ hybridization, mapped the MCP3 gene to chromosome 17q11.2-q12. MCP3 was identified as a physiologic substrate of gelatinase A. Cleaved MCP3 binds to CC-chemokine receptors-1, -2, and -3, but no longer induces calcium fluxes or promotes chemotaxis, and instead acts as a general chemokine antagonist that dampens inflammation, suggested that matrix metalloproteinases are both effectors and regulators of the inflammatory response.

Chemokine(C-C motif) ligand 17(CCL17) is a small cytokine belonging to the CC chemokine family that is also known as thymus and activation regulated chemokine(TARC). CCL17 is expressed constitutively in thymus, but only transiently in phytohemagglutinin-stimulated peripheral blood mononuclear cells.1 This chemokine specifically binds and induces chemotaxis in T cells and elicits its effects by interacting with the chemokine receptor CCR4.1,2The gene for CCL17 is located on chromosome 16, in humans, along with other chemokines called CCL22 and CX3CL1.3,4 The standard used in this kit is recombinant human CCL17, consisting of 71 amino acids with the molecular weight of 8Kda.

Chemokine(C-C motif) ligand 17(CCL17) is a small cytokine belonging to the CC chemokine family that is also known as thymus and activation regulated chemokine(TARC). CCL17 is expressed constitutively in thymus, but only transiently in phytohemagglutinin-stimulated peripheral blood mononuclear cells. This chemokine specifically binds and induces chemotaxis in T cells and elicits its effects by interacting with the chemokine receptor CCR4. The gene for CCL17 is located on chromosome 16, in humans, along with other chemokines called CCL22 and CX3CL1.

Chemokine(C-C motif) ligand 18(CCL18) is a small cytokine belonging to the CC chemokine family that was previously called PARC(pulmonary and activation-regulated chemokine). CCL18 is approximately 60% identical in amino acid sequence to CCL3. By analysis of a previously mapped CCL18 from 17q11.2, it is determined that the PARC gene is located within 1 of the 2 clusters of CC chemokine genes in this region. It is expressed at high levels in lung and at lower levels in certain lymphoid tissues, such as the lymph nodes, and is chemotactic for activated T cells and nonactivated lymphocytes. Beside, CCL18 recruits Th2 cells and basophils and may play a predominant role in allergic asthma.