R Recombinant
Recombinant: Superior lot-to-lot consistency, continuous supply, and animal-free manufacturing.
Cadherin-6 (D3T3I) Rabbit mAb #48111
Filter:
- WB
- IP
- IHC
- F
Supporting Data
REACTIVITY | H Mk |
SENSITIVITY | Endogenous |
MW (kDa) | 130 |
Source/Isotype | Rabbit IgG |
Application Key:
- WB-Western Blotting
- IP-Immunoprecipitation
- IHC-Immunohistochemistry
- F-Flow Cytometry
Species Cross-Reactivity Key:
- H-Human
- Mk-Monkey
Product Information
Product Usage Information
Application | Dilution |
---|---|
Western Blotting | 1:1000 |
Immunoprecipitation | 1:50 |
Immunohistochemistry (Paraffin) | 1:800 |
Flow Cytometry (Fixed/Permeabilized) | 1:1600 |
Storage
Supplied in 10 mM sodium HEPES (pH 7.5), 150 mM NaCl, 100 µg/ml BSA, 50% glycerol and less than 0.02% sodium azide. Store at –20°C. Do not aliquot the antibody.
For a carrier free (BSA and azide free) version of this product see product #84079.
For a carrier free (BSA and azide free) version of this product see product #84079.
Protocol
Specificity / Sensitivity
Cadherin-6 (D3T3I) Rabbit mAb 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).
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.
限制使用
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For Research Use Only. Not For Use In Diagnostic Procedures.
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