ELISA

TNFRSF17(Tumor necrosis factor receptor superfamily member 17), also called BCMA, is a protein that in humans is encoded by the TNFRSF17 gene. The protein encoded by this gene is a member of the TNF-receptor superfamily and is mapped to 16p13.13. This receptor is preferentially expressed in mature B lymphocytes, and may be important for B cell development and autoimmune response. This receptor has been shown to specifically bind to the tumor necrosis factor(ligand) superfamily, member 13b(TNFSF13B/TALL-1/BAFF), and to lead to NF-kappaB and MAPK8/JNK activation. This receptor also binds to various TRAF family members, and thus may transduce signals for cell survival and proliferation.

BAFF was regularly detected by enzyme-linked immunosorbent assay in brain tissue lysates and in normal spinal fluid, and in astrocytes by double fluorescence microscopy. BAFF was localized in astrocytes close to BAFF-R-expressing immune cells. BAFF receptors were strongly expressed in situ in primary central nervous system(CNS) lymphomas.1 The TNF superfamily member B cell-activating factor(BAFF) plays an important role in humoral immunity and in autoimmune diseases, including RA. Local BAFF gene targeting inhibited proinflammatory cytokine expression, suppressed generation of plasma cells and Th17 cells, and markedly ameliorated joint pathology.2 The B cell activating factor BAFF(BlyS/TALL-1/zTNF4) is a tumor necrosis factor(TNF)-related ligand that promotes B cell survival and binds to three receptors(BCMA, TACI, and the recently described BAFF-R).3 Human BAFF was mapped to chromosome 13q32-34.4 The standard used in this kit is recombinant soluble human BAFF(A134-L295) with the molec

B-cell activating factor(BAFF) also known as tumor necrosis factor ligand superfamily member 13B is a protein that in humans is encoded by the TNFLSF13B gene.1,2 BAFF is a cytokine that belongs to the tumor necrosis factor(TNF) ligand family. This cytokine is a ligand for receptors TNFRSF13B/TACI, TNFRSF17/BCMA, and TNFRSF13C/BAFFR. This cytokine is expressed in B cell lineage cells, and acts as a potent B cell activator. It has been also shown to play an important role in the proliferation and differentiation of B cells.3All these ligands act as heterotrimers(i.e. three of the same molecule) interacting with heterotrimeric receptors4, although BAFF has been known to be active as either a hetero- or homotrimer.5 The standard used in this kit is recombinant mouse soluble BAFF(A127-L309) with molecular weight 23.2KDa.

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.