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In conclusion, our study revealed that miR (show MLXIP Proteins)-214 acts as a tumor suppressor via inhibiting proliferation, migration and invasion of cervical cancer cells through targeting ARL2, and that both miR (show MLXIP Proteins)-214 and ARL2 may serve as prognostic or therapeutic targets for cervical cancer.
Novel Biochemical and Structural Insights into the Interaction of Myristoylated Cargo with Unc119 (show UNC119 Proteins) Protein and Their Release by Arl2/3.
We hypothesize that ARL2 plays essential roles inside mitochondria along with other cellular functions, at least in part to provide coupling of regulation between these essential cell processes.
MiR (show MLXIP Proteins)-195 regulates cell apoptosis in a context-dependent manner through directly targeting ARL2.
The G proteins Arl2 acts in a GTP (show AK3 Proteins)-dependent manner as allosteric release factors for farnesylated cargo.
a novel function of miR-16 (show GDE1 Proteins) targeting ARL2 in modulating proliferation and cell cycle progression.
Data show that bovine and human TBCD (show TBCD Proteins) have functionally identical roles in tubulin (show TUBB Proteins) heterodimer assembly, and that the inability of human TBCD (show TBCD Proteins) to disrupt microtubule integrity can be overcome by siRNA-mediated suppression of expression of Arl2.
C. elegans evl-20 gene encodes a functional homolog of human ARL2. Elimination of evl-20 function results in abnormal vulval, gonad, and male tail development and disrupts embryonic proliferation, hypodermal enclosure, and elongation.
Arl2 is present in centrosomes and propose that its action in regulating tubulin (show TUBB Proteins) polymerization is mediated at centrosomes
In summary, alterations in Arl2 protein content were found to be associated with modifications in tubulin (show TUBB Proteins) pools, microtubule dynamics as well as cell cycle progression.
two pathways in mitochondria, one affecting ATP levels that is independent of ELMOD2 (show ELMOD2 Proteins) and the other leading to mitochondrial fusion involving MFN2 (show MFN2 Proteins) that does involve ELMOD2 (show ELMOD2 Proteins)
Studies indicate that Arf-like proteins ARL2 and ARL3 are not substrates for N-myristoyl transferase.
Arl2, a small GTPase (show RACGAP1 Proteins), has an important regulator of breast tumor cell aggressivity, both in vitro and in vivo
Arf-like protein 2 interaction with PDEdelta is dependent on GTP (show AK3 Proteins), and the binding of PDEdelta substantially stabilizes GTP binding (show RND2 Proteins); data suggests that Arl2/3 are specific regulators of PDEdelta
This gene encodes a small GTP-binding protein of the RAS superfamily which functions as an ADP-ribosylation factor (ARF). The encoded protein is one of a functionally distinct group of ARF-like genes.
ADP-ribosylation factor-like 2
, ADP-ribosylation factor-like protein 2
, ADP-ribosylation-like 2
, arf-like protein 2