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MSL3 encodes a nuclear protein that is similar to the product of the Drosophila male-specific lethal-3 gene. De plus, nous expédions MSL3 Anticorps (37) et beaucoup plus de produits pour cette protéine.
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Characterization of syndrome that allowed us to decipher the developmental importance of MSL3 in humans.
MSL3 plays an important role in targeting the male specific lethal complex to chromatin in both humans and flies by binding to H4K20Me(1).
A multisubunit human histone acetylase complex that contains homologs of the Drosophila MSL proteins MOF, MSL1 (hampin A), MSL2, and MSL3 was described. This complex is responsible for histone H4 lysine-16 acetylation of all cellular chromosomes.
Data show that complete removal of paternally expressed gene 3 (PEG3) resulted in up-regulation of male-specific lethal 1 (Msl1) and male-specific lethal 3 (Msl3).
Msl1 interacts with Msl3 as an extended chain forming an extensive hydrophobic interface, whereas the Msl1-MOF interface involves electrostatic interactions between the HAT domain and a long helix of Msl1.
Analysis of Mid1, Hccs, Arhgap6, and Msl3l1 in X-linked polydactyly (Xpl) and Patchy-fur (Paf) mutant mice
This gene encodes a nuclear protein that is similar to the product of the Drosophila male-specific lethal-3 gene. The Drosophila protein plays a critical role in a dosage-compensation pathway, which equalizes X-linked gene expression in males and females. Thus, the human protein is thought to play a similar function in chromatin remodeling and transcriptional regulation, and it has been found as part of a complex that is responsible for histone H4 lysine-16 acetylation. This gene can undergo X inactivation. Alternative splicing results in multiple transcript variants. Related pseudogenes have been identified on chromosomes 2, 7 and 8.
male-specific lethal 3 homolog (Drosophila)
, male-specific lethal 3-like 1
, Male-specific lethal 3-like 1
, MSL3-like 1
, male-specific lethal 3 homolog
, male-specific lethal-3 protein-like 1
, male-specific lethal-3 homolog 1