Mouse anti E-Cadherin / Cadherin-1

Nordic MuBio
Product Code: MUB0302P
Product Group: Primary Antibodies
Supplier: Nordic MuBio
CodeSizePrice
MUB0302P0.1 mg£326.00
Quantity:
Prices exclude any Taxes / VAT

Overview

Host Type: Mouse
Antibody Isotype: IgG1
Antibody Clonality: Monoclonal
Antibody Clone: 6F9
Regulatory Status: RUO
Target Species: Human
Applications:
  • Immunocytochemistry (ICC)
  • Immunohistochemistry (IHC)
  • Western Blot (WB)
Storage:
Store at 4°C or in small aliquots at -20°C.

Further Information

Applications Description:
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.
Background:
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 ?E?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.
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.
This product contains sodium azide. To prevent formation of toxic vapors, do not mix with strong acidic solutions. To prevent formation of potentially explosive metallic azides in metal plumbing, always wash into drain with copious quantities of water.
This datasheet is as accurate as reasonably achievable, but Nordic-MUbio accepts no liability for any inaccuracies or omissions in this information.
Field of Interest:
Cancer|Cell adhesion
Formulation:
Each vial contains 100 ul 1 mg/ml purified monoclonal antibody in PBS containing 0.09% sodium azide.
Product:
Each vial contains 100 ul 1 mg/ml purified monoclonal antibody in PBS containing 0.09% sodium azide.
Source:
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.
Specificity:
6F9 recognizes both the 120 kD E-cadherin and its 80 kD trypsin-resistant extracellular part.
UniProt:
P12830

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.