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Die folgenden MAPmates™ sollten nicht zusammen analysiert werden: -MAPmates™, die einen unterschiedlichen Assaypuffer erfordern. -Phosphospezifische und MAPmate™ Gesamtkombinationen wie Gesamt-GSK3β und Gesamt-GSK3β (Ser 9). -PanTyr und locusspezifische MAPmates™, z.B. Phospho-EGF-Rezeptor und Phospho-STAT1 (Tyr701). -Mehr als 1 Phospho-MAPmate™ für ein einziges Target (Akt, STAT3). -GAPDH und β-Tubulin können nicht mit Kits oder MAPmates™, die panTyr enthalten, analysiert werden.
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96-Well Plate
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Weitere Reagenzien hinzufügen (MAPmates erfordern die Verwendung eines Puffer- und Detektionskits)
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48-602MAG
Buffer Detection Kit for Magnetic Beads
1 Kit
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Anti-Spectrin beta-II , clone 2A7, Cat. No. MABT1364, is a mouse monoclonal antibody that detects Spectrin beta chain and has been tested for use in Immunocytochemistry, Immunoprecipitation, and Western Blotting.
More>>Anti-Spectrin beta-II , clone 2A7, Cat. No. MABT1364, is a mouse monoclonal antibody that detects Spectrin beta chain and has been tested for use in Immunocytochemistry, Immunoprecipitation, and Western Blotting. Less<<
Spectrin beta (UniProt: G1SN11) is encoded by the SPTBN1 gene in rabbit. Spectrins belong to the superfamily of proteins called F-actin cross linking proteins that function as scaffolding proteins for protein sorting, cell adhesion, and migration. They are principle components of a cell membrane-cytoskeleton and are composed of two alpha and two beta spectrin subunits. They are actin binding proteins that serves as a membrane organizer and stabilizer. Spectrin beta II is a multifunctional protein that contains lipid-binding sites within its two calponin-homology domains (aa 82-186 and 201-306) and a pleckstrin homology domain (aa 2224-2334) and triple helical segments. Spectrin beta II is generally associated with the cytoplasmic surface of the membrane by attachment to ankyrin.
References
Product Information
Format
Purified
Presentation
Purified mouse monoclonal antibody IgG1 in buffer containing 0.1 M Tris-Glycine (pH 7.4), 150 mM NaCl with 0.05% sodium azide.
Applications
Application
Anti-Spectrin beta-II , clone 2A7, Cat. No. MABT1364, is a mouse monoclonal antibody that detects Spectrin beta chain and has been tested for use in Immunocytochemistry, Immunoprecipitation, and Western Blotting.
Key Applications
Immunocytochemistry
Immunoprecipitation
Western Blotting
Application Notes
Immunoprecipitation Analysis: A representative lot immunoprecipitated Spectrin beta-II in Immunoprecipitation applications (Bazellieres, E., et. al. (2012). J Cell Sci. 125(Pt 4):919-31).
Immunocytochemistry Analysis: A representative lot detected Spectrin beta-II in Immunocytochemistry applications (Bazellieres, E., et. al. (2012). J Cell Sci. 125(Pt 4):919-31).
Western Blotting Analysis: A representative lot detected Spectrin beta-II in Western Blotting applications (Bazellieres, E., et. al. (2012). J Cell Sci. 125(Pt 4):919-31).
Biological Information
Immunogen
Purified spectrin from frozen rabbit lens membranes.
Clone
2A7
Concentration
Please refer to lot specific datasheet.
Host
Mouse
Specificity
Clone 2A7 is a mouse monoclonal antibody that detects beta-II spectrin.
~275 kDa observed; 271.27 kDa calculated. Uncharacterized bands may be observed in some lysate(s).
Physicochemical Information
Dimensions
Materials Information
Toxicological Information
Safety Information according to GHS
Safety Information
Product Usage Statements
Quality Assurance
Evaluated by Western Blotting in differentiated Caco2 cell lysates.
Western Blotting Analysis: 2 µg/mL of this antibody detected Spectrin beta-II in differentiated Caco2 cell lysates.
Usage Statement
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.
Apico-basal elongation requires a drebrin-E-EB3 complex in columnar human epithelial cells. Bazellières, E; Massey-Harroche, D; Barthélémy-Requin, M; Richard, F; Arsanto, JP; Le Bivic, A J Cell Sci
125
919-31
2011
Although columnar epithelial cells are known to acquire an elongated shape, the mechanisms involved in this morphological feature have not yet been completely elucidated. Using columnar human intestinal Caco2 cells, it was established here that the levels of drebrin E, an actin-binding protein, increase in the terminal web both in vitro and in vivo during the formation of the apical domain. Drebrin E depletion was found to impair cell compaction and elongation processes in the monolayer without affecting cell polarity or the formation of tight junctions. Decreasing the drebrin E levels disrupted the normal subapical F-actin-myosin-IIB-βII-spectrin network and the apical accumulation of EB3, a microtubule-plus-end-binding protein. Decreasing the EB3 levels resulted in a similar elongation phenotype to that resulting from depletion of drebrin E, without affecting cell compaction processes or the pattern of distribution of F-actin-myosin-IIB. In addition, EB3, myosin IIB and βII spectrin were found to form a drebrin-E-dependent complex. Taken together, these data suggest that this complex connects the F-actin and microtubule networks apically during epithelial cell morphogenesis, while drebrin E also contributes to stabilizing the actin-based terminal web.