Recombinant Human MRG15 protein (His tag N-Terminus)
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Recombinant Human MRG15 protein (His tag N-Terminus) is a Human Full Length protein, in the 1 to 323 aa range, expressed in Escherichia coli, with >85%, suitable for SDS-PAGE, Mass Spec.
View Alternative Names
MRG15, FWP006, HSPC008, HSPC061, PP368, MORF4L1, Mortality factor 4-like protein 1, MORF-related gene 15 protein, Protein MSL3-1, Transcription factor-like protein MRG15
- SDS-PAGE
Unknown
SDS-PAGE - Recombinant Human MRG15 protein (His tag N-Terminus) (AB124555)
15% SDS-PAGE analysis of ab124555 (3μg)
Reactivity data
Sequence info
Properties and storage information
Shipped at conditions
Appropriate short-term storage duration
Appropriate short-term storage conditions
Appropriate long-term storage conditions
Aliquoting information
Storage information
Supplementary information
This supplementary information is collated from multiple sources and compiled automatically.
Biological function summary
MRG15 integrates into several protein complexes including the histone acetyltransferase complex where it interacts with other components to regulate transcription. The structure of MRG15 enables it to bind to methylated histones facilitating histone modification and affecting gene expression levels. Researchers observe its impact on the modulation of DNA repair and replication through its participation in these complexes.
Pathways
MRG15 operates mostly within the DNA damage repair and cell cycle progression pathways. It forms critical interactions with proteins such as ASF1 and TIP60 which influence histone acetylation and chromatin structure. These tasks are essential for the correct execution of the repair mechanisms and maintenance of genomic stability.
Specifications
Form
Liquid
Additional notes
Purified by using conventional chromatography.
General info
Function
Component of the NuA4 histone acetyltransferase (HAT) complex which is involved in transcriptional activation of select genes principally by acetylation of nucleosomal histones H4 and H2A. This modification may both alter nucleosome - DNA interactions and promote interaction of the modified histones with other proteins which positively regulate transcription. This complex may be required for the activation of transcriptional programs associated with oncogene and proto-oncogene mediated growth induction, tumor suppressor mediated growth arrest and replicative senescence, apoptosis, and DNA repair. The NuA4 complex ATPase and helicase activities seem to be, at least in part, contributed by the association of RUVBL1 and RUVBL2 with EP400. NuA4 may also play a direct role in DNA repair when directly recruited to sites of DNA damage. As part of the SIN3B complex represses transcription and counteracts the histone acetyltransferase activity of EP300 through the recognition H3K27ac marks by PHF12 and the activity of the histone deacetylase HDAC2 (PubMed : 12391155, PubMed : 14966270, PubMed : 37137925). SIN3B complex is recruited downstream of the constitutively active genes transcriptional start sites through interaction with histones and mitigates histone acetylation and RNA polymerase II progression within transcribed regions contributing to the regulation of transcription (PubMed : 21041482). Required for homologous recombination repair (HRR) and resistance to mitomycin C (MMC). Involved in the localization of PALB2, BRCA2 and RAD51, but not BRCA1, to DNA-damage foci.
Subcellular localisation
Nucleus
Target data
Product promise
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