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SUV420H2 and the related enzyme SUV420H1 (MIM 610881) function as histone methyltransferases that specifically trimethylate nucleosomal histone H4 (see MIM 602822) on lysine-20 (K20) (Schotta et al., 2004 [PubMed 15145825]).[supplied by OMIM, Dec 2009].. Additionally we are shipping Suppressor of Variegation 4-20 Homolog 2 (Drosophila) Antibodies (19) and many more products for this protein.
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Study provides evidence that Suv420h2 controls the H4K20 methylome of osteoblasts and is critical for normal progression of osteoblastogenesis.
Altogether, these results reveal Suv4-20h-mediated histone H4K20 tri (show VANGL2 Proteins)-methylation as a critical determinant in the selection of active replication initiation sites in heterochromatin regions of mammalian genomes.
The sequences surrounding both methylation sites do not fit to the specificity profile of SUV4-20H1 (show SUV420H1 Proteins).
Upregulation of long non-coding RNA PAPAS (show PSTPIP1 Proteins) in response to hypoosmotic stress does not increase H4K20me3 because of Nedd4 (show NEDD4 Proteins)-dependent ubiquitinylation and proteasomal degradation of Suv4-20h2.
One of the most downregulated genes in response to SUV420H2 expression was the Src (show SRC Proteins) substrate, tensin-3 (show TNS3 Proteins), a focal adhesion protein that contributes to cancer cell migration.
The crystal structure of SUV420H2 was used to characterize substrate selectivity and product specificity.
SUV420H1 (show SUV420H1 Proteins) and SUV420H2 isoforms have different in their cellular localization and effects on myogenic differentiation
data indicate that H4K20me3 invokes gene repression by antagonizing hMOF (show KAT8 Proteins)-mediated H4K16Ac
The decrease in trimethylation of lysine 20 of histone H4 in breast cancer cells was accompanied by diminished expression of Suv4-20h2 histone methyltransferase.
expression of Suv4-20h2 leads to sustained levels of H4K20me3, developmental arrest, and defects in S-phase progression.
Upregulation of long non-coding RNA PAPAS (show PSTPIP1 Proteins) in response to hypoosmotic stress does not increase H4K20me3 because of Nedd4-dependent ubiquitinylation and proteasomal degradation of Suv4-20h2.
Results uncover a lncRNA-mediated mechanism that guides Suv4-20h2 to specific genomic loci to establish a more compact chromatin structure in growth-arrested cells.
Data suggest that Suv4-20h1 (show SUV420H1 Proteins)/Suv4-20h2 activity is required for fidelity of chromosome distribution during meiosis in oocyte; Suv4-20h1 (show SUV420H1 Proteins)/Suv4-20h2 appear to control histone 4 methylation, centromere structure, and oocyte maturation/oogenesis.
Suv4-20h2 is involved in the initial loading or maintenance of cohesion subunits
SUV420H2 and the related enzyme SUV420H1 (MIM 610881) function as histone methyltransferases that specifically trimethylate nucleosomal histone H4 (see MIM 602822) on lysine-20 (K20) (Schotta et al., 2004
suppressor of variegation 4-20 homolog 2 (Drosophila)
, suppressor of variegation 4-20 protein-like 2
, histone-lysine N-methyltransferase SUV420H2-like
, histone-lysine N-methyltransferase SUV420H2
, su(var)4-20 homolog 2
, lysine N-methyltransferase 5C