Clathrin light chain a and b variants (CLC). By Western blot the antibody recognizes a doublet at ~35-40 kDa on rat brain extracts.
Applicazioni
This Anti-Clathrin Light Chain Antibody is validated for use in WB for the detection of Clathrin Light Chain.
Western blot: 1:50,000-1:100,000 on rat brain extracts.
Optimal working dilutions must be determined by end user.
Descrizione del bersaglio
~35-40 kDa
Note legali
CHEMICON is a registered trademark of Merck KGaA, Darmstadt, Germany
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Codice della classe di stoccaggio
10 - Combustible liquids
Classe di pericolosità dell'acqua (WGK)
WGK 1
Punto d’infiammabilità (°F)
Not applicable
Punto d’infiammabilità (°C)
Not applicable
Certificati d'analisi (COA)
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Proceedings of the National Academy of Sciences of the United States of America, 118(32) (2021-08-08)
Pancreatic β cells operate with a high rate of membrane recycling for insulin secretion, yet endocytosis in these cells is not fully understood. We investigate this process in mature mouse β cells by genetically deleting dynamin GTPase, the membrane fission
Conformational changes in endocytic proteins are regulators of clathrin-mediated endocytosis. Three clathrin heavy chains associated with clathrin light chains (CLC) assemble into triskelia that link into a geometric lattice that curves to drive endocytosis. Structural changes in CLC have been
Assembly of the endocytic machinery is a constitutively active process that is important for the organization of the plasma membrane, signal transduction, and membrane trafficking. Existing research has focused on the stochastic nature of endocytosis. Here, we report the emergence
The Journal of neuroscience : the official journal of the Society for Neuroscience, 34(49), 16544-16549 (2014-12-05)
Several proteins encoded by PD genes are implicated in synaptic vesicle traffic. Endophilin, a key factor in the endocytosis of synaptic vesicles, was shown to bind to, and be ubiquitinated by, the PD-linked E3 ubiquitin ligase Parkin. Here we report
Molecular biology of the cell, 24(15), 2378-2388 (2013-06-14)
A role for clathrin in AP-3-dependent vesicle biogenesis has been inferred from biochemical interactions and colocalization between this adaptor and clathrin. The functionality of these molecular associations, however, is controversial. We comprehensively explore the role of clathrin in AP-3-dependent vesicle
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