Claudin-6 Matched Antibody Pair #16740
Filter:
- ELISA
Supporting Data
| REACTIVITY | H |
Application Key:
- ELISA-ELISA
Species Cross-Reactivity Key:
- H-Human
Product Information
Product Usage Information
Matched Antibody Pairs include capture and detection antibodies to non-overlapping epitopes. Optimal dilutions/concentrations should be determined by the end user.
Formulation
Supplied in 1X PBS (10 mM Na2HPO4, 3 mM KCl, 2 mM KH2PO4, and 140 mM NaCl (pH 7.8)). BSA and Azide Free.
Storage
Store at -20ºC. This product will freeze at -20ºC so it is recommended to aliquot into single-use vials to avoid multiple freeze/thaw cycles. A slight precipitate may be present and can be dissolved by gently vortexing. This will not interfere with antibody performance.
Product Description
The Claudin-6 Matched Antibody Pair is ideal for use with immunoassay technologies and high-throughput ELISA platforms requiring antibody pairs with specialized or custom antibody labeling. Labels include fluorophores, lanthanides, biotin, and beads. Platforms requiring conjugated Matched Antibody Pairs include MSD, Quanterix Simoa, Alpha Technology (AlphaScreen, AlphaLISA, LANCE, HTRF), and Luminex.
Learn how Matched Antibody Pairs move your projects forward, faster at cst-science.com/matched-antibody-pairs.
Learn how Matched Antibody Pairs move your projects forward, faster at cst-science.com/matched-antibody-pairs.
Background
Tight junctions, or zonula occludens, form a continuous barrier to fluids across the epithelium and endothelium. They function in regulation of paracellular permeability and in the maintenance of cell polarity, blocking the movement of transmembrane proteins between the apical and the basolateral cell surfaces. Tight junctions are composed of claudin and occludin proteins, which join the junctions to the cytoskeleton (1,2). The claudin family is composed of 23 integral membrane proteins, and their expression, which varies among tissue types, may determine both the strength and properties of the epithelial barrier. Alteration in claudin protein expression pattern is associated with several types of cancer (2,3). Claudin-1 is expressed primarily in keratinocytes (4) and normal mammary epithelial cells, but is absent or reduced in breast carcinomas and breast cancer cell lines (5,6).
Claudin-6 is a member of the CLDN family that is expressed in epithelial cell sheets. Downregulation of Claudin-6 has been reported in breast invasive ductal carcinoma associated with lymphatic metastasis, which may point to a function of Claudin-6 as a tumor suppressor. Claudin-6 is reported to play a role in inhibiting malignancy of breast cancer cells by inducing apoptosis, inhibiting proliferation and migration. Mechanisms of action of Claudin-6 have been described through various signaling pathways such as p38-MAPK, JAKs-STATs, ASK1-JNK, and other pathways (7,8). Regulation of Claudin-6 expression may occur through epigenetic mechanisms (9). Other reports describe aberrant expression in various malignancies (10,11). The clinical significance of Claudin-6 dysregulation has created interest in the potential for pharmaceutical intervention (12-14).
Claudin-6 is a member of the CLDN family that is expressed in epithelial cell sheets. Downregulation of Claudin-6 has been reported in breast invasive ductal carcinoma associated with lymphatic metastasis, which may point to a function of Claudin-6 as a tumor suppressor. Claudin-6 is reported to play a role in inhibiting malignancy of breast cancer cells by inducing apoptosis, inhibiting proliferation and migration. Mechanisms of action of Claudin-6 have been described through various signaling pathways such as p38-MAPK, JAKs-STATs, ASK1-JNK, and other pathways (7,8). Regulation of Claudin-6 expression may occur through epigenetic mechanisms (9). Other reports describe aberrant expression in various malignancies (10,11). The clinical significance of Claudin-6 dysregulation has created interest in the potential for pharmaceutical intervention (12-14).
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- Oliveira, S.S. and Morgado-Díaz, J.A. (2007) Cell Mol Life Sci 64, 17-28.
- Hewitt, K.J. et al. (2006) BMC Cancer 6, 186.
- Brandner, J.M. et al. (2002) Eur J Cell Biol 81, 253-63.
- Krämer, F. et al. (2000) Hum Genet 107, 249-56.
- Swisshelm, K. et al. (1999) Gene 226, 285-95.
- Wu, Q. et al. (2013) Chin Med J (Engl) 126, 3539-44.
- Guo, Y. et al. (2016) Int J Oncol 48, 2435-44.
- Liu, Y. et al. (2016) J Exp Clin Cancer Res 35, 120.
- Zhang, X. et al. (2015) Med Oncol 32, 148.
- Torres-Martínez, A.C. et al. (2017) Exp Cell Res 350, 226-235.
- Micke, P. et al. (2014) Int J Cancer 135, 2206-14.
- Schneider, I.C. et al. (2018) Biotechnol J 13, e1700345.
限制使用
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For Research Use Only. Not For Use In Diagnostic Procedures.
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