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|+1 404 474 4654|
|+1 888 205 9894 (TF)|
Cadherin 1, Type 1, E-Cadherin (Epithelial) (CDH1) antibody
|Synonyms||uvo, lcam, E-Cad, XBcad, l-cam, xcdh1, cdhc-A, xb-cad, XTCAD-1, E-cadherin, cadherin-1, uvomorulin, XB-cadherin, cdh1|
Alternatives Immunocytochemistry (ICC), Immunohistochemistry (IHC), Immunohistochemistry (Frozen Sections) (IHC (fro)), Western Blotting (WB)
|5 references available|
|Price||369.60 $ Plus shipping costs $45.00|
|Alternative name||E-Cadherin / Cadherin-1|
|Immunogen||6F9 is a mouse monoclonal IgG1 antibody obtained by fusion of P3-X63-Ag 8,653 mouse myeloma cells with spleen cells from a BABL/c mouse immunized with affinity purified 80 kD extracellular fragments of E-cadherin derived from tryptic digestion of A-431 human vulva carcinoma cells.|
|Description||Cadherins constitute a family of transmembrane glycoproteins involved in Ca 2+ -dependent cell-cell interactions. The members of this family are differentially expressed in various tissues. They function in the maintenance of tissue integrity and morphogenesis. Cadherins are divided into type I and type II subgroups. Type I cadherins include epithelial cadherin (E-cadherin, cadherin-1 or uvomorulin), neural cadherin (N-cadherin or cadherin-2), placental cadherin (P-cadherin or cadherin-3) and retinal cadherin (R-cadherin or cadherin-4), whereas kidney cadherin (K-cadherin or cadherin-6) and osteoblast cadherin (OB-cadherin or cadherin-11) are type II cadherins. One of the best characterized cadherins is E-cadherin, a 120 kD transmembrane glycoprotein consisting of an 80 kD extracellular and a 40 kD transmembrane and cytoplasmic part. The extracellular domains of E-cadherin are responsible for calcium binding which allows for homophilic interaction with other E-cadherin molecules on the same cell and neighbouring cells. In addition, E-cadherin can interact heterophilically with integrin alpha E beta 7 . The cytoplasmic domain of E-cadherin is linked to the actin cytoskeleton through the associated cytoplasmic catenin proteins, thus establishing a complex localized to adherens junctions. In carcinomas E-cadherin is frequently downregulated, which is consistent with its function of an invasion suppressor in normal epithelia.|
|Application Notes||6F9 recognizes both the 120 kD E-cadherin and its 80 kD trypsin-resistant extracellular part. 6F9 is suitable for immunoblotting, immunocytochemistry and immunohistochemistry on frozen sections when using a PBS buffer containing 0.1 mM CaCl 2 and 0.1 mM MgCl 2 and for immunohistochemistry with avidin-biotinylated horseradish peroxidase complex (ABC) as detection reagentOptimal antibody dilution should be determined by titration.|
|Storage||Store at 4 o C, or in small aliquots at -20 o C.|
|Restrictions||For Research Use only|
Schipper, Frixen, Behrens et al.: "E-cadherin expression in squamous cell carcinomas of head and neck: inverse correlation with tumor dedifferentiation and lymph node metastasis." in: Cancer research, Vol. 51, Issue 23 Pt 1, pp. 6328-37, 1991 (PubMed).
Frixen, Behrens, Sachs et al.: "E-cadherin-mediated cell-cell adhesion prevents invasiveness of human carcinoma cells." in: The Journal of cell biology, Vol. 113, Issue 1, pp. 173-85, 1991 (PubMed).
Moll, Mitze, Frixen et al.: "Differential loss of E-cadherin expression in infiltrating ductal and lobular breast carcinomas." in: The American journal of pathology, Vol. 143, Issue 6, pp. 1731-42, 1994 (PubMed).
Boehm, Totzeck, Birchmeier et al.: "Differences of E-cadherin expression levels and patterns in primary and metastatic human lung cancer." in: Clinical & experimental metastasis, Vol. 12, Issue 1, pp. 55-62, 1994 (PubMed).
Mayer, Johnson, Leitl et al.: "E-cadherin expression in primary and metastatic gastric cancer: down-regulation correlates with cellular dedifferentiation and glandular disintegration." in: Cancer research, Vol. 53, Issue 7, pp. 1690-5, 1993 (PubMed).