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The protein encoded by ELMO2 interacts with the dedicator of cyto-kinesis 1 protein. Additionally we are shipping ELMO2 Antibodies (70) and ELMO2 Kits (18) and many more products for this protein.
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These data suggest a novel link between Tiam1 and RhoG/ILK /ELMO2 pathway as upstream effectors of the Rac1-mediated phagocytic process in trabecular meshwork cells.
studies demonstrate that Elmo2 is a new regulator of insulin (show INS Proteins)-dependent Glut4 (show SLC2A4 Proteins) membrane translocation through modulating Rac1 activity and Akt (show AKT1 Proteins) membrane compartmentalization.
findings highlight the necessity of ELMO2 for maintaining vascular integrity, specifically in intramembranous bones; loss-of-function mutations in ELMO2 cause intraosseous vascular malformation by impeding RAC1 signaling
Axl (show AXL Proteins) has a role in phosphorylating the Elmo scaffold proteins to promote Rac (show AKT1 Proteins) activation and cell invasion
uncovered a role for ELMO in the recruitment of ACF7 (show MACF1 Proteins) to the membrane to promote microtubule capture and stability
Through its association with ELMO2, ILK (show ILK Proteins) plays key roles in the regulation of Rho GTPases and cross-talk pathways between adhesion and growth factor receptors.
Ilk (show ILK Proteins) and ELMO2 modulate recycling endosomes in keratinocytes undergoing intercellular adhesion mediated through cell-cell contacts, including E-cadherin (show CDH1 Proteins)-based adherens junctions.
ELMO2-RhoG-ILK (show ILK Proteins) complex has a key role in integrin-independent stabilization of the microtubule network in differentiated keratinocytes.
Collectively, our studies demonstrate that formation of an Elmo2.ClipR-59 (show CLIP3 Proteins) complex plays an important role in myoblast fusion.
Resutls show that the interaction with ELMO2 and RhoG is essential for the ability of ILK (show ILK Proteins) to induce front-rear cell polarity.
The protein encoded by this gene interacts with the dedicator of cyto-kinesis 1 protein. Similarity to a C. elegans protein suggests that this protein may function in phagocytosis of apoptotic cells and in cell migration. Alternative splicing results in multiple transcript variants encoding the same protein.
, engulfment and cell motility 2
, engulfment and cell motility protein 2-like
, engulfment and cell motility protein 2
, PH domain protein CED12A
, ced-12 homolog 2
, protein ced-12 homolog A
, CED-12 homolog A
, engulfment and cell motility 2, ced-12 homolog