immunoprecipitation (IP): 1-2 μL using whole extract of mouse A-20 cells. western blot: 1:1,000-1:2,000 using whole extract of rat brain western blot: 1:2,000-1:3,000 using whole extract of human Jurkat cells.
ELMO1 (engulfment and cell motility 1) is a member of the evolutionarily conserved family of ELMO proteins.
Application
Anti-ELMO antibody produced in rabbit is suitable for immunoprecipitation at a working antibody amount of 1-2μL using a whole extract of mouse A-20 cells. It is also suitable for immunoblotting at a working dilution of 1:2000-1:3000 using a whole extract of human Jurkat cells and at 1:1000-1:2000 using a whole extract of rat brain.
Biochem/physiol Actions
ELMO proteins regulate actin cytoskeleton reorganization during engulfment and cell migration. ELMO1 and Dock180 function together as a guanine exchange factor (GEF) for the small GTPase Rac, leading to its activation and cytoskeleton rearrangement. The C-terminal PH domain of ELMO1 binds to Dock180 and the N-terminal binds to the active form of the small GTPase RhoG, targeting the ELMO/Dock180 complex to the membrane. It also interacts with BAI1, an engulfment receptor for apoptotic cells upstream of the ELMO1/Dock180/Rac module. Increased expression of ELMO1 and Dock180 are associated with the invasive phenotype of glioma cells.
Physical form
Solution in 0.01 M phosphate buffered saline, pH 7.4, containing 15 mM sodium azide.
Disclaimer
Unless otherwise stated in our catalog or other company documentation accompanying the product(s), our products are intended for research use only and are not to be used for any other purpose, which includes but is not limited to, unauthorized commercial uses, in vitro diagnostic uses, ex vivo or in vivo therapeutic uses or any type of consumption or application to humans or animals.
The C. elegans genes ced-2, ced-5, and ced-10, and their mammalian homologs crkII, dock180, and rac1, mediate cytoskeletal rearrangements during phagocytosis of apoptotic cells and cell motility. Here, we describe an additional member of this signaling pathway, ced-12, and its
Molecular biology of the cell, 19(11), 4837-4851 (2008-09-05)
The mammalian DOCK180 protein belongs to an evolutionarily conserved protein family, which together with ELMO proteins, is essential for activation of Rac GTPase-dependent biological processes. Here, we have analyzed the DOCK180-ELMO1 interaction, and map direct interaction interfaces to the N-terminal
Mammalian Dock180 and ELMO proteins, and their homologues in Caenorhabditis elegans and Drosophila melanogaster, function as critical upstream regulators of Rac during development and cell migration. The mechanism by which Dock180 or ELMO mediates Rac activation is not understood. Here
Engulfment and subsequent degradation of apoptotic cells is an essential step that occurs throughout life in all multicellular organisms. ELMO/Dock180/Rac proteins are a conserved signalling module for promoting the internalization of apoptotic cell corpses; ELMO and Dock180 function together as
A distinct feature of malignant gliomas is the intrinsic ability of single tumor cells to disperse throughout the brain, contributing to the failure of existing therapies to alter the progression and recurrence of these deadly brain tumors. Regrettably, the mechanisms
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