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Mouse (Murine) Polyclonal MORF4L1 Primary Antibody for IHC (p), IHC - ABIN250010
Pardo, Leung, Lucchesi, Pereira-Smith: MRG15, a novel chromodomain protein, is present in two distinct multiprotein complexes involved in transcriptional activation. in The Journal of biological chemistry 2002
Cow (Bovine) Polyclonal MORF4L1 Primary Antibody for IHC, WB - ABIN2777616
Bertram, Bérubé, Hang-Swanson, Ran, Leung, Bryce, Spurgers, Bick, Baldini, Ning, Clark, Parkinson, Barrett, Smith, Pereira-Smith: Identification of a gene that reverses the immortal phenotype of a subset of cells and is a member of a novel family of transcription factor-like genes. in Molecular and cellular biology 1999
Show all 2 Pubmed References
PALB2 associates with active genes through its major binding partner, MRG15, which recognizes histone H3 trimethylated at lysine 36 (H3K36me3) by the SETD2 methyltransferase
Both MRG15 CD and Pf1 PHD1 bind to their targets with >100 muM affinity.
While the present study expands on the role of MRG15 in the control of genomic stability, weak associations can not be ruled out for potential low-penetrance variants at MORF4L1 and breast cancer risk among BRCA2 mutation carriers
it seems unlikely that any constitutional changes in MRG15 confer an increased risk for breast cancer.
gene deficiency reduces DNA repair and increase sensitivity to DNA-crosslinking agents
a novel chromodomain protein that is present in two distinct multiprotein complexes involved in transcriptional activation
Site-directed mutagenesis studies of a prototypic MRG domain from human MRG15 based on the X-ray structure and bioinformatics identify key residues involved in the binding of PAM14 and MRGBP.
identify MRG15 residues that form a shallow hydrophobic pocket to interact with the N-terminal 50 residues of PAM14 through primarily hydrophobic interactions
The MRG15 chromo domain may function as an adaptor module which can bind to a modified histone H3 in a mode different from that of the HP1/Pc chromo domains.
MORF4 has a role in cellular aging, and MRG15 associates with both histone deacetylases and histone acetyl transferase complexes [review]
RBP2 associates with MRG15 complex to maintain reduced H3K4 methylation at transcribed regions, which may ensure the transcriptional elongation state
MRG15 is a novel PALB2-interacting factor involved in homologous recombination
In round spermatids, MRG15 colocalizes with splicing factors PTBP1 and PTBP2 at H3K36me3 sites between the exons and single intron of transition nuclear protein 2 (Tnp2). Thus, our results reveal that MRG15 is essential for pre-mRNA splicing during spermatogenesis and that epigenetic regulation of pre-mRNA splicing by histone modification could be useful to understand not only spermatogenesis but also, epigenetic disorder
HDAC2-dependent deacetylation of MORF4L1 enhances MORF4L1 homodimerization, thus facilitating the functionality of complex formation to repress cell proliferation.
DNA damage foci, as indicated by immunostaining for gammaH2AX and 53BP1, are detectable in a sub-population of Mrg15 deficient NSC cultures under normal growing conditions and the majority of p21-positive cells are also positive for 53BP1 foci.
MRG15 has an essential role in embryonic development via chromatin remodeling and transcriptional regulation.
Formation of phosphorylated H2AX and 53BP1 foci was delayed in Mrg15 mutant versus wild-type cells following irradiation. These data implicate a novel role for MRG15 in DNA-damage repair in mammalian cells.
Our results demonstrate that MRG15 has more than one function in neurogenesis and defines a novel role for this chromatin regulator that integrates proliferation and cell-fate determination in neurogenesis during development.
Mrg15 is a subunit of the Ash1 complex, a stimulator of Ash1 enzymatic activity and a critical regulator of the TrxG protein function of Ash1 in Drosophila.
Ash1 HMTase activity is activated by MRG15, a subunit of the identified Ash1 complex, and that this complex, rather than the Ash1 protein alone, is the active form of this H3K36 methyltransferase, both in vitro and in vivo.
Mrg15 interacts with Cap-H2 condensin subunit.
Drosophila DmMRG15 gene function is required for female fertility, larval survival and adult life span, and provides reagents that should be useful for further dissecting the role of DmMRG15 in cell proliferation and aging.
Component of the NuA4 histone acetyltransferase 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. Also component of the mSin3A complex which acts to repress transcription by deacetylation of nucleosomal histones. 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 (By similarity).
Esa1p-associated factor 3 homolog
, MORF-related gene 15 protein
, MORF-related gene on chromosome 15
, mortality factor 4-like protein 1
, protein MSL3-1
, transcription factor-like protein MRG15
, testis expressed gene 189
, testis-expressed gene 189 protein
, MORF-related gene 15
, mortality factor 4 like 2