ELISA Kits

Cadherins are calcium-dependent cell-cell adhesion molecules that mediate cell-cell binding in a homophilic manner. They play an important role in the growth and development of cells via the mechanisms of control of tissue architecture and the maintenance of tissue integrity. Cadherin expression is regulated spatially as well as temporally. Cadherins are thought to play an important role in development and maintenance of tissues through selective cell-cell adhesion activity and may be involved also in the invasion and metastasis of malignant tumors. Cadherin regulates dendritic spine morphogenesis. A cadherin gene cluster is mapped to a region of chromosome 5 subject to frequent allelic loss in carcinoma. The standard product used in this kit is recombinant P-Cadherin with the molecular mass of 120-130Kda after glycosylation.

P-Cadherin, also known as Cadherin-3(CDH3), is a protein that in humans is encoded by the CDH3 gene. This gene is a classical cadherin from the cadherin superfamily. This gene is located in a six-cadherin cluster in a region on the long arm of chromosome 16 that is involved in loss of heterozygosity events in breast and prostate cancer. In addition, aberrant expression of this protein is observed in cervical adenocarcinomas. Mutations in this gene have been associated with congenital hypotrichosis with juvenile macular dystrophy. Cells expressing CDH3 also adhered to one another more tightly than the parental cell line.

Cadherin-2(CDH2), also known as neural cadherin(NCAD), is a protein that in humans is encoded by the CDH2 gene. It is a classical cadherin from the cadherin superfamily. This gene is mapped to 18q12.1. Cadherin-2 is expressed in the brain, skeletal and cardiac muscle. Cadherin-2 is commonly found in cancer cells and provides a mechanism for transendothelial migration. It is a calcium dependent cell-cell adhesion glycoprotein comprising five extracellular cadherin repeats, a transmembrane region and a highly conserved cytoplasmic tail. The protein functions during gastrulation and is required for establishment of left-right asymmetry. At certain central nervous system synapses, presynaptic to postsynaptic adhesion is mediated at least in part by this gene product.

Cathepsin B is an enzymatic protein belonging to the peptidase or protease families. In humans, it is coded by the CTSB gene.1, 2 And this gene is mapped to chromosome 8p22.3 The protein encoded by this gene is a lysosomal cysteine proteinase composed of a dimer of disulfide-linked heavy and light chains, both produced from a single protein precursor. It is a member of the peptidase C1 family. Cathepsin B was once suspected as a candidate protease participating in the conversion of beta-amyloid precursor protein into the amyloid plaques found in Alzheimer's disease patients. However, this function is now known to be mediated by BACE1 protease. It is now thought that cathepsin B can degrade beta-amyloid precursor protein into harmless fragments. Thus, it is conceivable cathepsin B may play a pivotal role in the natural defense against Alzheimer's disease.4 Overexpression of cathepsin B has been associated with esophageal adenocarcinoma and other tumors. At least five transcript variants

Cathepsin B is an enzymatic protein belonging to the peptidase or protease families. In humans, it is coded by the CTSB gene.1, 2 And this gene is mapped to chromosome 8p22.3 The protein encoded by this gene is a lysosomal cysteine proteinase composed of a dimer of disulfide-linked heavy and light chains, both produced from a single protein precursor. It is a member of the peptidase C1 family. Cathepsin B was once suspected as a candidate protease participating in the conversion of beta-amyloid precursor protein into the amyloid plaques found in Alzheimer's disease patients. However, this function is now known to be mediated by BACE1 protease. It is now thought that cathepsin B can degrade beta-amyloid precursor protein into harmless fragments. Thus, it is conceivable cathepsin B may play a pivotal role in the natural defense against Alzheimer's disease.4 Overexpression of cathepsin B has been associated with esophageal adenocarcinoma and other tumors. At least five transcript variants

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 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