Recombinant Human CKIP-1 protein (ab162446)

Plays a role in the regulation of the actin cytoskeleton through its interactions with actin capping protein (CP). May function to target CK2 to the plasma membrane thereby serving as an adapter to facilitate the phosphorylation of CP by protein kinase 2 (CK2). Appears to target ATM to the plasma membrane. Appears to also inhibit tumor cell growth by inhibiting AKT-mediated cell-survival. Also implicated in PI3K-regulated muscle differentiation, the regulation of AP-1 activity (plasma membrane bound AP-1 regulator that translocates to the nucleus) and the promotion of apoptosis induced by tumor necrosis factor TNF. When bound to PKB, it inhibits it probably by decreasing PKB level of phosphorylation.

Abundantly expressed in skeletal muscle and heart, moderately in kidney, liver, brain and placenta and sparingly in the pancreas and lung. Easily detectable in cancer cell lines such as MOLT-4, HEK293 and Jurkat cells.

Contains 1 PH domain.

C-terminal fragments could be released during apoptosis via caspase-3-dependent cleavage.

Cell membrane. Nucleus. Cytoplasm. Predominantly localized to the plasma membrane. In C2C12 cells, with the absence of growth factor, it is found in the nucleus. It rapidly translocates to the plasma membrane after insulin stimulation. In response to TNF, it translocates from the plasma membrane to the cytoplasm and then to the nucleus accompanied by cleavage by caspase-3. However, the subcellular location is highly dependent of the cell type, and this explains why it is found exclusively at the plasma membrane, in some type of cells.