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The DYNLL2 binding region, located in an intrinsically disordered domain of the myo5a tail, has a nascent helical character.
the thermodynamic and kinetic fine-tuning of binding of various ligands to DYNLL could have physiological relevance in its interaction network.
GKAP-DLC2 interaction organizes the postsynaptic scaffold complex to enhance synaptic NMDA receptor activity.
DLC2-mutant mice display enhanced angiogenic responses.
These data show that alternative splicing of the myosin Va heavy chain controls DYNLL2-myosin Va interaction and that DYNLL2 binding alters the structure of a portion of the myosin's coiled-coil domain.
Acts as one of several non-catalytic accessory components of the cytoplasmic dynein 1 complex that are thought to be involved in linking dynein to cargos and to adapter proteins that regulate dynein function. Cytoplasmic dynein 1 acts as a motor for the intracellular retrograde motility of vesicles and organelles along microtubules. May play a role in changing or maintaining the spatial distribution of cytoskeletal structures (By similarity).
8 kDa dynein light chain b
, dynein light chain 2, cytoplasmic
, radial spoke 22 homolog
, dynein, light chain, LC8-type 2
, dynein light chain 2
, dynein light chain LC8-type 2
, dynein light chain-2