产品名称
Anti-M-Cadherin Antibody, clone 12G4, clone 12G4, Upstate®, from mouse
biological source
mouse
conjugate
unconjugated
antibody form
purified antibody
antibody product type
primary antibodies
clone
12G4, monoclonal
species reactivity
mouse
manufacturer/tradename
Upstate®
technique(s)
ELISA: suitable
immunocytochemistry: suitable
western blot: suitable
isotype
IgG1κ
NCBI accession no.
UniProt accession no.
shipped in
wet ice
target post-translational modification
unmodified
Quality Level
Gene Information
mouse ... Cdh15(12555)
Analysis Note
routinely evaluated by immunoblot on modified RIPA lysates from C2C12 cells
Application
Anti-M-Cadherin Antibody, clone 12G4 is an antibody against M-Cadherin for use in ELISA, WB & IC.
Research Category
Cell Structure
Cell Structure
Research Sub Category
Adhesion (CAMs)
Adhesion (CAMs)
Biochem/physiol Actions
M-Cadherin
Disclaimer
Unless otherwise stated in our catalog or other company documentation accompanying the product(s), our products are intended for research use only and are not to be used for any other purpose, which includes but is not limited to, unauthorized commercial uses, in vitro diagnostic uses, ex vivo or in vivo therapeutic uses or any type of consumption or application to humans or animals.
General description
Mr 130kDa
Immunogen
Recombinant extracellular domain of mouse M-Cadherin
Physical form
Format: Purified
Thiophilic adsorption and size exclusion
Preparation Note
Stable for 1 year at -20°C from date of shipment
Legal Information
UPSTATE is a registered trademark of Merck KGaA, Darmstadt, Germany
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存储类别
10 - Combustible liquids
Convergence of Wnt, beta-catenin, and cadherin pathways.
Nelson, W James and Nusse, Roel
Science (New York, N.Y.), 303, 1483-1487 (2004)
U Kaufmann et al.
Cell and tissue research, 296(1), 191-198 (1999-04-13)
Cadherins are calcium-dependent, transmembrane intercellular adhesion proteins with morphoregulatory functions in the development and maintenance of tissues. In the development of striated muscle, the expression and function of mainly M-, N-, and R-cadherin has been studied so far. While these
Y Shimoyama et al.
The Journal of biological chemistry, 273(16), 10011-10018 (1998-05-23)
We used a novel cDNA cloning method based on the cadherin-beta-catenin protein interaction and identified a new human classic-type cadherin, which we named cadherin-15, from adult brain and skeletal muscle cDNA libraries. Sequence analysis revealed that this cadherin was closely
The cadherin-catenin complex as a focal point of cell adhesion and signalling: new insights from three-dimensional structures.
Gooding, Jane M, et al.
Bioessays, 26, 497-511 (2004)
Structure-based models of cadherin-mediated cell adhesion: the evolution continues.
Koch, A W, et al.
Cellular and Molecular Life Sciences, 61, 1884-1895 (2004)
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