CA125 mAb CGC, clone 1 Gold Conjugates - Cancer Marker
- Known as:
- CA125 mAb CGC, clonality 1 Gold Conjugates - Cancer Marker
- Catalog number:
- CGCA1-0701
- Product Quantity:
- 1-99 mg/ml/ea price
- Category:
- -
- Supplier:
- Arista Bio
- Gene target:
- CA125 mAb CGC clone 1 Gold Conjugates - Cancer Marker
Related genes to: CA125 mAb CGC, clone 1 Gold Conjugates - Cancer Marker
- Gene:
- MUC16 NIH gene
- Name:
- mucin 16, cell surface associated
- Previous symbol:
- -
- Synonyms:
- CA125, FLJ14303
- Chromosome:
- 19p13.2
- Locus Type:
- gene with protein product
- Date approved:
- 2001-07-20
- Date modifiied:
- 2015-09-04
- Gene:
- NBR1 NIH gene
- Name:
- NBR1 autophagy cargo receptor
- Previous symbol:
- M17S2
- Synonyms:
- CA125, KIAA0049, 1A1-3B
- Chromosome:
- 17q21.31
- Locus Type:
- gene with protein product
- Date approved:
- 1994-08-29
- Date modifiied:
- 2019-01-21
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- Human CA125, encoded by the MUC16 gene, is an ovarian cancer antigen widely used for a serum assay. Its extracellular region consists of tandem repeats of SEA domains. In this study we determined the three-dimensional structure of the SEA domain from the murine MUC16 homologue using multidimensional NMR spectroscopy. The domain forms a unique alpha/beta sandwich fold composed of two alpha helices and four antiparallel beta strands and has a characteristic turn named the TY-turn between alpha1 and alpha2. The internal mobility of the main chain is low throughout the domain. The residues that form the hydrophobic core and the TY-turn are fully conserved in all SEA domain sequences, indicating that the fold is common in the family. Interestingly, no other residues are conserved throughout the family. Thus, the sequence alignment of the SEA domain family was refined on the basis of the three-dimensional structure, which allowed us to classify the SEA domains into several subfamilies. The residues on the surface differ between these subfamilies, suggesting that each subfamily has a different function. In the MUC16 SEA domains, the conserved surface residues, Asn-10, Thr-12, Arg-63, Asp-75, Asp-112, Ser-115, and Phe-117, are clustered on the beta sheet surface, which may be functionally important. The putative epitope (residues 58-77) for anti-MUC16 antibodies is located around the beta2 and beta3 strands. On the other hand the tissue tumor marker MUC1 has a SEA domain belonging to another subfamily, and its GSVVV motif for proteolytic cleavage is located in the short loop connecting beta2 and beta3. - Source: PubMed
Publication date: 2004/02/04
Maeda TakeshiInoue MakotoKoshiba SeizoYabuki TakashiAoki MasaakiNunokawa EmiSeki EikoMatsuda TakayoshiMotoda YokoKobayashi AtsuoHiroyasu FumikoShirouzu MikakoTerada TakahoHayami NobuhiroIshizuka YoshikoShinya NaokoTatsuguchi AyakoYoshida MayumiHirota HiroshiMatsuo YoTani KazutoshiArakawa TakahiroCarninci PieroKawai JunHayashizaki YoshihideKigawa TakanoriYokoyama Shigeyuki - NBR1 (named as next to BRCA1) was originally cloned as a candidate gene for the ovarian cancer antigen CA125, using expression cloning with the anti-CA125 Ig, OC125. NBR1 has been of interest due to its position close to BRCA1, although no involvement in breast or ovarian cancer has been demonstrated. Recently, the antigen CA125 has been cloned, and identified as a new mucin, MUC16, entirely different from NBR1. The function of NBR1 remains unknown. To investigate its function, a yeast two-hybrid study was performed to identify interacting protein partners that may reflect a biological role for this protein. Here, we show that NBR1 interacts with two proteins; fasciculation and elongation protein zeta-1 (FEZ1), a PKCzeta interacting protein, and calcium and integrin binding protein (CIB), which is associated with polo-like kinases Fnk/Snk and the Alzheimer's disease presenilin 2 protein. Co-transfection of FEZ1 and NBR1 showed overlapping localization in the cytoplasm, whereas coexpression of NBR1 and CIB resulted in a shift of CIB protein expression from the nucleus to the perinuclear compartment. FEZ1 is highly expressed in the brain and in situ hybridization analysis of Nbr1 showed that its expression is also regulated in the murine brain during development. These data suggest that NBR1 may function, through interaction with CIB and FEZ1 in cell signalling pathways, with a developmentally restricted expression suggesting a possible role in neural development. - Source: PubMed
Whitehouse CarolineChambers JulieHowe KathyCobourne MartynSharpe PaulSolomon Ellen