Studies on minispectrins
Expression in E. coli, purification and in vitro interaction studies
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The / -minispectrin is a shortened soluble version of spectrin constructed to study spectrin interactions in vitro. In this study we constructed a modified / ÷N-minispectrin, lacking the 37 amino acid N-terminal extension of the -minispectrin chain. The original and modified version of the minispectrin was produced in order to perform structural and functional studies. Upon production of the / - and / ÷N-minispectrin proteins, two versions of each protein were obtained, a dimer, ( / )/ ( / ÷N), and a tetramer, ( / )2/( / ÷N)2.The effect of calcium on the binding of spectrin to actin has fo...
The / -minispectrin is a shortened soluble version
of spectrin constructed to study spectrin
interactions in vitro. In this study we constructed
a modified / ÷N-minispectrin, lacking the 37 amino
acid N-terminal extension of the -minispectrin
chain. The original and modified version of the
minispectrin was produced in order to perform
structural and functional studies. Upon production
of the / - and / ÷N-minispectrin proteins, two
versions of each protein were obtained, a dimer,
( / )/ ( / ÷N), and a tetramer, ( / )2/( / ÷N)2.
The effect of calcium on the binding of spectrin to
actin has for long been a theme of dispute.
Therefore the influence of calcium on the
interaction between actin and the minispectrins were
investigated using two different methods, an
ultracentrifuge actin pull down assay and Biacore®X.
The results from both methods showed that calcium
had no direct effect on the binding of the
minispectrins to the actin.
of spectrin constructed to study spectrin
interactions in vitro. In this study we constructed
a modified / ÷N-minispectrin, lacking the 37 amino
acid N-terminal extension of the -minispectrin
chain. The original and modified version of the
minispectrin was produced in order to perform
structural and functional studies. Upon production
of the / - and / ÷N-minispectrin proteins, two
versions of each protein were obtained, a dimer,
( / )/ ( / ÷N), and a tetramer, ( / )2/( / ÷N)2.
The effect of calcium on the binding of spectrin to
actin has for long been a theme of dispute.
Therefore the influence of calcium on the
interaction between actin and the minispectrins were
investigated using two different methods, an
ultracentrifuge actin pull down assay and Biacore®X.
The results from both methods showed that calcium
had no direct effect on the binding of the
minispectrins to the actin.
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