Cell Signaling Technology

Product Pathways - Adhesion

OB-Cadherin (P707) Antibody #4442

Applications Reactivity Sensitivity MW (kDa) Source
W IP IF-IC H M R (Mk) (Dg) Endogenous 120 Rabbit

Applications Key:  W=Western Blotting  IP=Immunoprecipitation  IF-IC=Immunofluorescence (Immunocytochemistry)
Reactivity Key:  H=Human  M=Mouse  R=Rat  Mk=Monkey  Dg=Dog
Species cross-reactivity is determined by western blot. Species enclosed in parentheses are predicted to react based on 100% sequence homology.

Protocols

Specificity / Sensitivity

OB-Cadherin (P707) Antibody detects endogenous levels of total OB-cadherin protein.

Source / Purification

Polyclonal antibodies are produced by immunizing animals with a synthetic peptide corresponding to residues surrounding Pro707 of human OB-cadherin protein. Antibodies were purified by protein A and peptide affinity chromatography.

Western Blotting

Western Blotting

Western blot analysis of extracts from NCI-H460 and MDA-MB-231 cells using OB-Cadherin (P707) Antibody.

IF-IC

IF-IC

Confocal immunofluorescent analysis of PC-3 (positive, left) and LNCaP (negative, right) cells using OB-Cadherin (P707) Antibody (green). Blue pseudocolor = DRAQ5® #4084 (fluorescent DNA dye).

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). Recent studies indicate that cancer cells have up-regulated 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).

OB-cadherin (CDH11) is highly expressed in osteoblastic cell lines (9). Its upregulation during differentiation in cells of the osteo-lineage and the chondro-lineage implies a specific role in bone cell differentiation and bone formation (9,10).

  1. Wheelock, M.J. and Johnson, K.R. (2003) Annu. Rev. Cell. Dev. Biol. 19, 207-235.
  2. Christofori, G. (2003) EMBO J. 22, 2318-2323.
  3. Hazan, R.B. et al. (2004) Ann. NY Acad. Sci. 1014, 155-163.
  4. Bryant, D.M. and Stow, J.L. (2004) Trends Cell Biol. 14, 427-434.
  5. Rabascio, C. et al. (2004) Cancer Res. 64, 4373-4377.
  6. Yamaoka-Tojo, M. et al. (2006) Arterioscler. Thromb. Vasc. Biol. 26, 1991-1997.
  7. Patel, I.S. et al. (2003) Int. J. Cancer 106, 172-177.
  8. Sanders, D.S. et al. (2000) J. Pathol. 190, 526-530.
  9. Okazaki, M. et al. (1994) J. Biol. Chem. 269, 12092-12098.
  10. Kii, I. et al. (2004) J. Bone Miner. Res. 19, 1840-1849.

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