KMT2B Acting in Gene Development
KMT2B (Lysine [K] Methyltransferase 2B) or Mixed Lineage Leukemia 2 protein (MLL2) is a mammalian histone H3 lysine 4 (H3K4) methyltransferase. It readily forms complexes with WRAD, host cell factors 1 and 2, and Menin. These complexes confer H3K4 trimethylation to specific gene promoters and some enhancers to regulate bivalent developmental genes and stem cell/germ
SLAS 2024 Exhibitor Marketing ToolKit Blog Post 860 x 540 px
BellBrook Labs looks forward to connecting with attendees at the upcoming SLAS 2024 conference in Boston, Massachusetts. SLAS is a beacon for the life sciences community, showcasing companies from diverse backgrounds that converge onto the same mission: accelerate life sciences research and technologies. BellBrook plans to contribute to this unified mission by showcasing our cutting-edge
DDX17 Acting in Viral Innate Immunity
DDX17 (p72/p82) was first detected as a bunyavirus inhibitor. Subsequent characterization revealed that it is an ATP-dependent RNA helicase, belonging to the DEAD-box group of proteins and bearing the signature Asp-Glu-Ala-Asp sequence. The presence of a novel upstream CTG translation start site (in addition to a conventional ATG start site) produces two isoforms: p72 is
DNMT3A Actions in Epigenetics
DNA methyltransferase 3-alpha (DNMT3A) effects de novo cytosine methylation in embryonic and somatic cells through the transfer of a methyl group from S-Adenosyl-L-methionine (SAM) to the cytosine-C5 position of newly created CpG DNA residues. In somatic cells, 60 to 80% of these structures are methylated at any given time. Nonetheless, clusters of CpG residues (islands)
METTL3 Acts as a Tumor Promoter
Methyltransferase-like 3 (METTL3) is a 70 kDa protein, 580 amino acids in length. It is the principal catalytic agent for most of the N6– methyladenosine (m6A) modifications that occur in eukaryotic cell mRNA. METTL3 typically places methyl adducts at the adenosine in motifs, such as DRACH, RAC, or RRACH. As such, it influences mRNA splicing,
RNA Methyltransferase METTL16 Performing Many Functions
Methyltransferase-like protein 16 (METTL16) is a recently characterized human RNA methyltransferase in the class I SAM-methyltransferase family. It methylates adenosine at the N6 position in a consensus sequence on U6 small nuclear RNA (U6 snRNA) and S-adenosylmethionine (SAM) synthetase (MAT2A) pre-mRNA to control the activity of these molecules. By regulating SAM homeostasis in a feedback
Researchers Identify PDE5 Inhibitor Using Transcreener Assay
Phosphodiesterase 5 (PDE5) is most familiar in connection to sildenafil (Viagra), a popular pharmaceutical PDE5 inhibitor. In response to nitric acid-activated soluble guanylyl cyclase production of cGMP, dimeric PDE5 binds and hydrolyzes cGMP in vascular smooth muscles cells, lung, kidney, brain, cardiac myocytes, and platelets to create 5′-GMP. This is accomplished by cGMP binding to
DDX6 regulates RNA transcription and translation
DDX6 (RCK/p54) was first isolated from the RC-K8 B-cell lymphoma line over 30 years ago. This 472 amino acid, 53.2 kDa “DEAD-Box” ATP-dependent RNA helicase bears the signature Asp-Glu-Ala-Asp motif, characteristic of all DEAD box proteins. Dead box proteins contain both ATPase and helicase activity, and are known for their particular protein-protein and RNA-protein interactions
Scientist using Transcreener Assay to Study PIK3CA Mutation
The PIK3CA gene codes for the 110 kDa catalytic subunit (p110α) of phosphoinositide 3-kinase (PI3Ka). Together with its regulatory component, p85α (encoded by PIK3R), they comprise the powerful PI3Ka heterodimer. This heterodimer conducts growth impulses from multiple cell surface receptor tyrosine kinases (RTKs) to the interior of the cell. It is known that individual missense
DDX5 Inhibitors Targeting Colon Cancer
DDX5 (Dead-Box 5 or p68) is a member of a family of 37 “DEAD-Box” ATP-dependent RNA helicases that play a role in nearly all aspects of RNA processing and also act as nucleic acid recognition receptors for viral immunity. Dysregulation and/or overexpression of DDX5 can lead to tumor progression. It can also be hijacked by