Amphiphysin is a brain-enriched protein that exhibits N-terminal lipid interaction and functions as a dimer. Amphiphysin contains a membrane bending BAR domain, a middle Clathrin and adaptor binding domain, and a C-terminal SH3 domain. In the brain, Amphiphysin I and II form heterodimers that bind to the Clathrin associated GTPase Dynamin via their SH3 domains. This association is essential for synaptic vesicle recycling in neurons, as it precedes the binding of Dynamin to the Clathrin-coated pits and the subsequent vesicle budding. In other tissues, Amphiphysin may play a key role in other membrane bending and curvature stabilization events. The mammalian Amphiphysins, Amphiphysin I and Amphiphysin II, have similar overall structure. A ubiquitous splice form of Amphiphysin II that does not contain Clathrin or adaptor interactions is highly expressed in muscle tissue and is involved in the formation and stabilization of the T tubule network.
Key Feature
Clonality
Polyclonal
Isotype
IgG
Host Species
Rabbit
Tested Applications
WBIPIFELISA
recommended for detection of Amphiphysin I of human and, to a lesser extent, mouse and rat origin by WB, IP, IF and ELISA
Species Reactivity
HumanMouseRat
Concentration
1mg/ml
Purification
Affinity purified
Target Information
Alternative Names
epitope corresponding to amino acids 467-620 mapping near the C-terminus of Amphiphysin I of human origin
Tissue Specificity
epitope corresponding to amino acids 467-620 mapping near the C-terminus of Amphiphysin I of human origin