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Binds CAPZA2 with high affinity and significantly decreases CAPZA2 affinity for actin barbed ends. Additionally we are shipping and many more products for this protein.
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LRRC16A plays a role in adult respiratory distress syndrome pathophysiology by interacting with, and being mediated through, platelets.
shown for the first time that CARMIL/LRRC16A was associated with gout, which could be due to urate transportsome failure
The results also suggest that the ability of CARMIL1 to inhibit CP in cells may be regulated.
Data suggest that CARMIL promotes uncapping by binding to a freely accessible site on Capping protein (CP) bound to a filament barbed end and inducing a change in the conformation of the actin-binding surface of CP.
The two CARMIL isoforms are both important for cell migration, but they have distinct functions.[CARMIL1, CARMIL2]
Expression of the capping-protein-binding region of CARMIL (also known as LRRC16A) impaired spindle migration and polar body extrusion during oocyte maturation and decreased the density of the cytoplasmic actin mesh
Our data argue that a large pool of freely diffusing, inactive capping protein (CP:V-1) feeds, via CARMIL-driven complex exchange, the formation of weak-capping complexes (CP:CARMIL) at the plasma membrane of protruding edges.
CARMIL leading edge localization depends on a non-canonical PH domain and dimerization.
the isolated CAH3 domain of CARMIL (and presumably the intact molecule as well) possesses the ability to uncap CP-capped actin filaments
Binds CAPZA2 with high affinity and significantly decreases CAPZA2 affinity for actin barbed ends. Increases the rate of elongation from seeds in the presence of CAPZA2, however, seems unable to nucleate filaments. Rapidly uncaps barbed ends capped by CAPZA2 and enhances barbed-end actin polymerization (By similarity).
, capping protein, Arp2/3, and Myosin-I Linker homolog 1
, leucine rich repeat containing 16
, leucine-rich repeat-containing protein 16A