|Recombinant Human CDH1 protein (Catalog#10204-H08H)|
|0.2 μm filtered solution in PBS|
|This antibody was produced from a hybridoma resulting from the fusion of a mouse myeloma with B cells obtained from a mouse immunized with purified, recombinant Human Cadherin-1 / CDH1 (rh Cadherin-1; Catalog#10204-H08H; Met 1-Ile 707; NP_004351.1). The IgG fraction of the cell culture supernatant was purified by Protein A affinity chromatography.|
This antibody can be used at 1:1000-1:2000 with the appropriate secondary reagents to detect Human Cadherin-1.
Anti-Histone H3 rabbit monoclonal antibody at 1:200 dilution
Lane A: NIH3T3 Whole Cell Lysate
Lane B: Hela Whole Cell Lysate
Lysates/proteins at 30 μg per lane.
Goat Anti-Rabbit IgG (H+L)/HRP at 1/10000 dilution.
Developed using the ECL technique.
Performed under reducing conditions.
Predicted band size:15 kDa
Observed band size:17 kDa
Cadherins are calcium-dependent cell adhesion proteins which preferentially interact with themselves in a homophilic manner in connecting cells, and thus may contribute to the sorting of heterogeneous cell type. E-cadherin (E-Cad), also known as CDH1 and CD324, is a calcium-dependent cell adhesion molecule the intact function of which is crucial for the establishment and maintenance of epithelial tissue polarity and structural integrity. Mutations in CDH1 occur in diffuse type gastric cancer, lobular breast cancer, and endometrial cancer. In human cancers, partial or complete loss of E-cadherin expression correlates with malignancy. During apoptosis or with calcium influx, E-Cad is cleaved by the metalloproteinase to produce fragments of about 38 kDa (E-CAD/CTF1), 33 kDa (E-CAD/CTF2) and 29 kDa (E-CAD/CTF3), respectively. E-Cad has been identified as a potent invasive suppressor, as downregulation of E-cadherin expression is involved in dysfunction of the cell-cell adhesion system, and often correlates with strong invasive potential and poor prognosis of human carcinomas.