OB-Cadherin (P707) AntibodyProduct information
|100 µl (10 western blots)||-||Unavailable in your region|
Product Pathways - Adhesion
OB-Cadherin (P707) Antibody #4442
|4442S||100 µl (10 western blots)||---||In Stock||---|
|4442||carrier free and custom formulation / quantity||email request|
|W||1:1000||Human, Mouse, Rat||Endogenous||120||Rabbit|
Species cross-reactivity is determined by western blot.
Applications Key: W=Western Blotting, IP=Immunoprecipitation
Species predicted to react based on 100% sequence homology: Monkey, Dog.
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.
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 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).
- 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.
- Okazaki, M. et al. (1994) J. Biol. Chem. 269, 12092-12098.
- Kii, I. et al. (2004) J. Bone Miner. Res. 19, 1840-1849.
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