Cadherin-6 (D3T3I) Rabbit mAb (BSA and Azide Free) #84079
- WB
- IHC
- F
Supporting Data
| REACTIVITY | H Mk |
| SENSITIVITY | Endogenous |
| MW (kDa) | 130 |
| Source/Isotype | Rabbit IgG |
Application Key:
- WB-Western Blotting
- IHC-Immunohistochemistry
- F-Flow Cytometry
Species Cross-Reactivity Key:
- H-Human
- Mk-Monkey
Product Information
Product Usage Information
This formulation is ideal for use with technologies requiring specialized or custom antibody labeling, including fluorophores, metals, lanthanides, and oligonucleotides. It is not recommended for ChIP, ChIP-seq, CUT&RUN or CUT&Tag assays. If you require a carrier free formulation for chromatin profiling, please contact us. Optimal dilutions/concentrations should be determined by the end user.
Formulation
Storage
Specificity / Sensitivity
Cadherin-6 (D3T3I) Rabbit mAb (BSA and Azide Free) recognizes endogenous levels of total cadherin-6 protein. Staining of peripheral nerves and limited staining of immune cells has been observed. The specificity of this staining is unknown.
Species Reactivity:
Human, Monkey
Source / Purification
Monoclonal antibody is produced by immunizing animals with a synthetic peptide corresponding to residues surrounding Asp761 of human cadherin-6 protein.
Background
Cadherins are a superfamily of transmembrane glycoproteins that contain cadherin repeats of approximately 100 residues in their extracellular domain. Cadherins mediate calcium-dependent cell-cell adhesion and play critical roles in normal tissue development (1). The classic cadherin subfamily includes N-, P-, R-, B-, and E-cadherins, as well as about ten other members that are found in adherens junctions, a cellular structure near the apical surface of polarized epithelial cells. The cytoplasmic domain of classical cadherins interacts with β-catenin, γ-catenin (also called plakoglobin), and p120 catenin. β-catenin and γ-catenin associate with α-catenin, which links the cadherin-catenin complex to the actin cytoskeleton (1,2). While β- and γ-catenin play structural roles in the junctional complex, p120 regulates cadherin adhesive activity and trafficking (1-4). Investigators consider E-cadherin an active suppressor of invasion and growth of many epithelial cancers (1-3). Research studies indicate that cancer cells have upregulated N-cadherin in addition to loss of E-cadherin. This change in cadherin expression is called the "cadherin switch." N-cadherin cooperates with the FGF receptor, leading to overexpression of MMP-9 and cellular invasion (3). Research studies have shown that in endothelial cells, VE-cadherin signaling, expression, and localization correlate with vascular permeability and tumor angiogenesis (5,6). Investigators have also demonstrated that expression of P-cadherin, which is normally present in epithelial cells, is also altered in ovarian and other human cancers (7,8).
Cadherin-6, also known as kidney cadherin (K-Cadherin, CDH6) is a type II classical cadherin. While it was reported to have a tumor suppressor function in cholangiocarcinoma (9), cadherin-6 expression was shown to be a marker of epithelial mesenchymal transition, and positively correlated with stage and metastasis of papillary thyroid carcinoma (10, 11). In related studies, cadherin-6 was shown to interact with GABARAP and related proteins to restrain autophagy, thereby promoting metastatic behavior (12). Cadherin-6 has since been proposed as an antibody-drug conjugate target for the treatment of ovarian and renal cancers (13).
- Wheelock, M.J. and Johnson, K.R. (2003) Annu Rev Cell Dev Biol 19, 207-35.
- Christofori, G. (2003) EMBO J 22, 2318-23.
- Hazan, R.B. et al. (2004) Ann N Y Acad Sci 1014, 155-63.
- Bryant, D.M. and Stow, J.L. (2004) Trends Cell Biol 14, 427-34.
- Rabascio, C. et al. (2004) Cancer Res 64, 4373-7.
- Yamaoka-Tojo, M. et al. (2006) Arterioscler Thromb Vasc Biol 26, 1991-7.
- Patel, I.S. et al. (2003) Int J Cancer 106, 172-7.
- Sanders, D.S. et al. (2000) J Pathol 190, 526-30.
- Goeppert, B. et al. (2016) Epigenetics 11, 780-790.
- Zhao, L. et al. (2016) Clin Endocrinol (Oxf) 84, 748-55.
- Sancisi, V. et al. (2013) PLoS One 8, e75489.
- Gugnoni, M. et al. (2017) Oncogene 36, 667-677.
- Bialucha, C.U. et al. (2017) Cancer Discov 7, 1030-1045.
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