Use your antibodies-online credentials, if available.
No Products on your Comparison List.
Your basket is empty.
Find out more
Plays a role in the regulation of the actin cytoskeleton through its interactions with actin capping protein (CP). Additionally we are shipping Pleckstrin Homology Domain Containing, Family O Member 1 Proteins (7) and Pleckstrin Homology Domain Containing, Family O Member 1 Kits (6) and many more products for this protein.
Showing 10 out of 48 products:
Human Polyclonal PLEKHO1 Primary Antibody for EIA, WB - ABIN499637
Zhang, Tie, Tian, Xing, Song, Zhu, Sun, He: CKIP-1 recruits nuclear ATM partially to the plasma membrane through interaction with ATM. in Cellular signalling 2006
Show all 4 references for ABIN499637
Human Polyclonal PLEKHO1 Primary Antibody for EIA, WB - ABIN452845
Barrios-Rodiles, Brown, Ozdamar, Bose, Liu, Donovan, Shinjo, Liu, Dembowy, Taylor, Luga, Przulj, Robinson, Suzuki, Hayashizaki, Jurisica, Wrana: High-throughput mapping of a dynamic signaling network in mammalian cells. in Science (New York, N.Y.) 2005
There is a major role of the CK2alpha-interacting protein CKIP-1 in activation of PAK1 (show PAK1 Antibodies) for neoplastic prostate cells transformation.
CKIP-1 interacts with CARMA1 (show CARD11 Antibodies) and has an inhibitory effect on PKCtheta (show PRKCQ Antibodies);-CBM-NF-kappaB (show NFKB1 Antibodies) signaling.
CKIP-1 controlled Smurf1 (show SMURF1 Antibodies) expression in colon cancer
overexpression triggers classical monocyte activation and transactivation of the TNF (show TNF Antibodies) promoter
CKIP-1, through its leucine zipper, interacts with the Rpt6 and mediates the Smurf1 (show SMURF1 Antibodies)-Rpt6 interaction.
CKIP-1 is involved in various important signaling pathways, controlling cell growth, apoptosis, differentiation, cytoskeleton and bone formation--REVIEW
The N-terminal PH domain and C-terminal auto-inhibitory region of CKIP-1 coordinate to determine its subcellular localization and the nucleus-plasma membrane shuttling.
examination of CK2alpha for a region that mediates interactions with CKIP-1 revealed a putative HIKE domain; this motif by itself may not be sufficient to mediate interactions.
CKIP-1 plays a role in the regulation of the actin cytoskeleton through its interactions with actin capping protein (show TMOD4 Antibodies).
CKIP-1 could interact with ATM (show ATM Antibodies) and recruits nuclear ATM (show ATM Antibodies) proteins partially to the plasma membrane. The results provide the first evidence that ATM (show ATM Antibodies), a predominantly nuclear kinase, could be re-localized to the plasma membrane.
CKIP-1 is a novel inhibitor of MSC (show MSC Antibodies)-originated adipogenesis by enhancing HDAC1 (show HDAC1 Antibodies)-associated repression of C/EBPalpha (show CEBPA Antibodies).
CKIP-1 interacts with TRAF6 (show TRAF6 Antibodies), a ubiquitin ligase (show RNF123 Antibodies) required for K63-linked ubiquitination and plasma membrane recruitment of Akt (show AKT1 Antibodies), and terminates TRAF6 (show TRAF6 Antibodies)-mediated Akt (show AKT1 Antibodies) activation.
Knockdown of CKIP-1 in RAW264.7 macrophage cells resulted in impaired cell migration.
CKIP-1 was found to be an inhibitor of cardiac hypertrophy by upregulating the dephosphorylation of HDAC4 through the recruitment of protein phosphatase 2A.
CKIP-1 has a role in cell morphology that depends on its interaction with actin-capping protein (show TMOD4 Antibodies)
CKIP-1 functions as the first auxiliary factor to enhance the activation of Smurf1 (show SMURF1 Antibodies).
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. 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 (By similarity).
pleckstrin homology domain containing, family O member 1
, C-Jun-binding protein
, CK2 interacting protein 1; HQ0024c protein
, CK2-interacting protein 1
, PH domain-containing family O member 1
, casein kinase 2-interacting protein 1
, osteoclast maturation-associated gene 120 protein
, pleckstrin homology domain-containing family O member 1
, CK2 interacting protein 1
, Jun zipper-associated 2
, TNF intracellular domain-interacting protein