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Component of histone acetyltransferase complex responsible for the majority of histone H4 acetylation at 'Lys-16' which is implicated in the formation of higher-order chromatin structure.. Zusätzlich bieten wir Ihnen und viele weitere Produktgruppen zu diesem Protein an.
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Studies identi fi ed a novel signal of nuclear localization (NLS) in all MSL1 protein isoforms and found that the combination of both NLS allows for its intra-nuclear focal accumulation and nuclear transport of TTC4 while all MSL1 isoforms affect H4K16Ac.
The MSL1 bound to Nupr1, with a moderate affinity (2.8 microM) in an entropically-driven process. MSL1 did not bind to non-damaged DNA, but it bound to chemically-damaged-DNA with a moderate affinity (1.2 microM) also in an entropically-driven process.
MSL1 (zeige SNRPB2 Antikörper) plays an important role in mediating irradiation-induced DNA repair through formation of HAT (zeige MGEA5 Antikörper) complexes and interaction with 53BP1 (zeige TP53BP1 Antikörper). P8 acts as a negative regulator of this process by interacting with MSL1 (zeige SNRPB2 Antikörper) and preventing its role on HAT (zeige MGEA5 Antikörper) activity.
A multisubunit human histone acetylase complex that contains homologs of the Drosophila MSL proteins MOF (zeige KAT8 Antikörper), MSL1 (hampin A), MSL2 (zeige MSL2 Antikörper), and MSL3 (zeige MSL3 Antikörper) 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 (zeige PEG3 Antikörper)) resulted in up-regulation of male-specific lethal 1 (Msl1 (zeige OPRK1 Antikörper)) and male-specific lethal 3 (Msl3 (zeige MSL3 Antikörper)).
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.
hampin may be linked to diverse regulatory processes in the nucleus
Describes the primary structure of the protein hampin, which shares about 26% sequence identity with the Drosophila MSL1 protein. In mouse, at least five splice isoforms exist, two of which have restricted tissue specificity (testes).
Component of histone acetyltransferase complex responsible for the majority of histone H4 acetylation at 'Lys-16' which is implicated in the formation of higher-order chromatin structure.
, male-specific lethal 1 homolog
, male-specific lethal 1-like 1
, male-specific lethal-1 homolog 1