Product Name :
Mouse anti E-Cadherin / Cadherin-1

Description :
| Clone 6F9 | Isotype IgG1 | Product Type Primary Antibodies | Units 0.1 mg | Host Mouse | Species Reactivity Human | Application Immunocytochemistry Immunohistochemistry (frozen) Western Blotting

Background :
6F9 is a Mouse monoclonal IgG1 antibody obtained by fusion of P3-X63-Ag 8,653 Mouse myeloma cells with spleen cells from a BALB/c Mouse immunized with affinity purified 80 kD extracellular fragments of E-cadherin derived from tryptic digestion of A-431 Human vulva carcinoma cells.

Source :
Cadherins constitute a family of transmembrane glycoproteins involved in Ca2+-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 αEβ7. 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. <

Product :
Each vial contains 100 ul 1 mg/ml purified monoclonal antibody in PBS containing 0.09% sodium azide. Formulation: Each vial contains 100 ul 1 mg/ml purified monoclonal antibody in PBS containing 0.09% sodium azide.

Specificity :
6F9 recognizes both the 120 kD E-cadherin and its 80 kD trypsin-resistant extracellular part.

Applications :
6F9 is suitable for immunoblotting, immunocytochemistry and immunohistochemistry on frozen tissues when using a PBS buffer containing 0.1 mM CaCl2 and 0.1 mM MgCl2. Optimal antibody dilution should be determined by titration; recommended range is 1:25 – 1:100 for immunohistochemistry with avidin-biotinylated Horseradish peroxidase complex (ABC) as detection reagent, and 1:50 – 1:500 for immunoblotting applications.

Storage :
The antibody is shipped at ambient temperature and may be stored at +4°C. For prolonged storage prepare appropriate aliquots and store at or below -20°C. Prior to use, an aliquot is thawed slowly in the dark at ambient temperature, spun down again and used to prepare working dilutions by adding sterile phosphate buffered saline (PBS, pH 7.2). Repeated thawing and freezing should be avoided. Working dilutions should be stored at +4°C, not refrozen, and preferably used the same day. If a slight precipitation occurs upon storage, this should be removed by centrifugation. It will not affect the performance or the concentration of the product.

Caution :
This product is intended FOR RESEARCH USE ONLY, and FOR TESTS IN VITRO, not for use in diagnostic or therapeutic procedures involving humans or animals. It may contain hazardous ingredients. Please refer to the Safety Data Sheets (SDS) for additional information and proper handling procedures. Dispose product remainders according to local regulations.This datasheet is as accurate as reasonably achievable, but our company accepts no liability for any inaccuracies or omissions in this information.

References :
1. Frixen, U. H., Behrens, J., Sachs, M., Eberle, G., Voss, B., Warda, A., Lochner, D., and Birchmeier, W. (1991). E-cadherin-mediated cell-cell adhesion prevents invasiveness of Human carcinoma cells, J Cell Biol 113, 173-85. 2. Schipper, J. H., Frixen, U. H., Behrens, J., Unger, A., Jahnke, K., and Birchmeier, W. (1991). E-cadherin expression in squamous cell carcinomas of head and neck: inverse correlation with tumor dedifferentiation and lymph node metastasis. Cancer Res 51, 6328-6337. 3. Mayer, B., Johnson, J. P., Leitl, F., Jauch, K. W., Heiss, M. M., Schildberg, F. W., Birchmeier, W., and Funke, I. (1993). E-cadherin expression in primary and metastatic gastric cancer: down-regulation correlates with cellular dedifferentiation and glandular disintegration. Cancer Res 53, 1690-1695. 4. Moll, R., Mitze, M., Frixen, U. H., and Birchmeier, W. (1993). Differential loss of E-cadherin expression in infiltrating ductal and lobular breast carcinomas, Am J Pathol 143, 1731-42. 5. Bohm, M., Totzeck, B., Birchmeier, W., and Wieland, I. (1994). Differences of E-cadherin expression levels and patterns in primary and metastatic Human lung cancer. Clin Exp Metastasis 12, 55-62. 6. Otto, T., Birchmeier, W., Schmidt, U., Hinke, A., Schipper, J., Rubben, H., and Raz, A. (1994). Inverse relation of E-cadherin and autocrine motility factor receptor expression as a prognostic factor in patients with bladder carcinomas. Cancer Res 54, 3120-3123. 7. Zschiesche, W., Schonborn, I., Behrens, J., Herrenknecht, K., Hartveit, F., Lilleng, P., and Birchmeier, W. (1997). Expression of E-cadherin and Catenins in invasive mammary carcinomas. Anticancer Res 17, 561-567. 8. Ghadimi, B. M., Behrens, J., Hoffmann, I., Haensch, W., Birchmeier, W., and Schlag, P. M. (1999). Immunohistological analysis of E-cadherin, alpha-, beta- and gamma-Catenin expression in colorectal cancer: impliCations for cell adhesion and signaling. Eur J Cancer 35, 60-65.

Antibodies are immunoglobulins secreted by effector lymphoid B cells into the bloodstream. Antibodies consist of two light peptide chains and two heavy peptide chains that are linked to each other by disulfide bonds to form a “Y” shaped structure. Both tips of the “Y” structure contain binding sites for a specific antigen. Antibodies are commonly used in medical research, pharmacological research, laboratory research, and health and epidemiological research. They play an important role in hot research areas such as targeted drug development, in vitro diagnostic assays, characterization of signaling pathways, detection of protein expression levels, and identification of candidate biomarkers.
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