FLJ11730 antibody - N-terminal region (ARP33354_P050)
- Known as:
- FLJ11730 (anti-) - N-terminal region (ARP33354_P050)
- Catalog number:
- arp33354_p050
- Product Quantity:
- USD
- Category:
- -
- Supplier:
- Aviva Systems Biology
- Gene target:
- FLJ11730 antibody - N-terminal region (ARP33354_P050)
Related genes to: FLJ11730 antibody - N-terminal region (ARP33354_P050)
- Gene:
- MEAF6 NIH gene
- Name:
- MYST/Esa1 associated factor 6
- Previous symbol:
- C1orf149
- Synonyms:
- NY-SAR-91, FLJ11730, Eaf6, CENP-28
- Chromosome:
- 1p34.3
- Locus Type:
- gene with protein product
- Date approved:
- 2005-07-13
- Date modifiied:
- 2016-10-05
Related products to: FLJ11730 antibody - N-terminal region (ARP33354_P050)
Related articles to: FLJ11730 antibody - N-terminal region (ARP33354_P050)
- The histone acetyltransferase complex HBO1 (KAT7) is an oncogenic regulator across multiple cancers, promoting cell proliferation and migration. Though clinically important, no targeted therapies address HBO1 dysregulation. HBO1 forms complexes with MEAF6, JADE(1/2/3), ING(ING4/5), and BRPF1/2/3 to acetylate histones H3 and H4, especially at H3K14, promoting transcriptional activation and genomic stability. It colocalizes with active transcriptional sites and participates in gene regulation, DNA repair and replication. Most HBO1-associated cancer mutations are missense, though their effects remain unclear. Silencing HBO1 restores normal proliferation and gene expression, underscoring its oncogenic role. HBO1 activity supports cancer pathways, including apoptosis resistance, DNA damage response, and cell cycle regulation. The HBO1 inhibitor WM-3835 disrupts H3K14 acetylation, reducing tumor growth in several cancers. This review provides insights into the function of HBO1 in cancer, especially in histone acetylation, ubiquitination, stem cell maintenance, and pro- and anti-oncogenic signaling. Understanding the roles of HBO1 may guide new epigenetic therapies for HBO1-driven malignancies. - Source: PubMed
Publication date: 2026/01/18
Marchione Alissa DKathrein Katie L - Ossifying fibromyxoid tumor (OFMT) is a rare mesenchymal neoplasm first described in 1989. It typically arises in the superficial soft tissues of the extremities as a slow-growing, painless mass. Histologically, it is commonly characterized by a multilobular architecture composed of uniform epithelioid cells embedded in a fibromyxoid matrix, often surrounded by a rim of metaplastic bone. While classic cases are readily identifiable, the tumor's histopathological heterogeneity can mimic a range of benign and malignant neoplasms, posing significant diagnostic challenges. Molecularly, most OFMTs harbor PHF1 rearrangements, commonly involving fusion partners such as EP400, MEAF6, or TFE3. This review underscores the importance of an integrated diagnostic approach- incorporating histopathological, immunohistochemical, and molecular data- to accurately classify OFMT and distinguish it from its mimics. Expanding awareness of its morphologic and molecular spectrum is essential for precise diagnosis, optimal patient management, and a deeper understanding of this enigmatic neoplasm. - Source: PubMed
Publication date: 2026/01/14
Chatzopoulos KyriakosSyrnioti AntoniaYakoub MohamedLinos Konstantinos - To investigate the clinicopathological characteristics of ossifying fibromyxoid tumor (OFMT) with rare fusion subtypes. Three cases of OFMT with rare fusion subtypes, diagnosed and consulted in the Zhejiang Hospital, Zhejiang Provincial People's Hospital, Hangzhou, China and Ningbo Clinical Pathology Diagnosis Center, Ningbo, China from January 2016 to December 2024 were collected. Immunohistochemistry (IHC), fluorescence in situ hybridization (FISH), and targeted RNA sequencing were performed to analyze the immunohistochemical and molecular genetic characteristics of these OFMT. Literature review was also conducted. All three patients were male, with ages of 50, 74, and 58 years, respectively. The tumors were located in the left foot, left thigh, and left lumbar region, respectively, and all presented as slowly growing, painless masses in the skin or subcutaneous tissue. Grossly, the tumors measured 3.5 cm, 6.3 cm, and 5.0 cm in maximum diameter, respectively, with a grayish-white to grayish-yellow, solid, lobulated cut surface. One case exhibited a noticeable myxoid texture. Microscopically, one tumor was located in the superficial dermis, while the other two were in the subcutaneous tissue. The tumors were well-demarcated and showed a lobulated or multinodular growth pattern. None of the cases had a complete surrounding bony shell (only one case had very focal ossification). The tumor cells were monomorphic, short spindle-shaped, oval to epithelioid, and arranged in solid sheets, trabeculae, and small nests within a variably fibromyxoid stroma. Case 1 exhibited abundant pseudorosette-like structures formed by short spindle cells surrounding acellular fibrous stroma. Case 2 showed focal transition of epithelioid tumor cells into fasciculately arranged spindle cells, with extensive stromal hyalinization. Case 3 had a predominantly myxoid stroma with a rich network of thin-walled blood vessels. The tumor cells exhibited mild nuclear atypia with 1-3 mitotic figures per 50 high-power fields. All three cases showed diffuse and strong expression of CD10. Two of the three cases showed nuclear expression of TFE3, while one case showed diffuse and strong expression of desmin and S-100. Targeted RNA sequencing revealed PHF1 (ex12)::TFE3 (ex7) fusion in two cases and MEAF6 (ex5)::PHF1 (5'UTR) fusion in one case, which were further confirmed by FISH study. All three patients underwent tumor resection. Two showed no recurrence during follow-up periods of 98 months and 15 months, respectively, while one experienced local recurrence at 12 months postoperatively. OFMT with rare fusion subtypes often exhibits atypical histological and immunophenotypic features, and lacks a characteristic bony shell. Incorporating TFE3 into the diagnostic IHC panel greatly aids in screening for the cases with rare PHF1::TFE3 fusions. Familiarity with the histological and immunophenotypic characteristics, and differential diagnostic points of these rare OFMT subtypes, is essential for judicious use of molecular genetic tools in achieving a definitive diagnosis. - Source: PubMed
Chai M YYin X NRu G QPeng FZhao M - Microexon splicing is a vertebrate-conserved process through which small, often in-frame, exons are differentially included during brain development and across neuron types. Although the protein sequences encoded by these exons are highly conserved and can mediate interactions, the neurobiological functions of only a small number have been characterized. To establish a more generalized understanding of their roles in brain development, we used CRISPR/Cas9 to remove 45 microexons in zebrafish and assessed larval brain activity, morphology, and behavior. Most mutants had minimal or no phenotypes at this developmental stage. Among previously studied microexons, we uncovered baseline and stimulus-driven phenotypes for two microexons (meA and meB) in and reduced activity in the telencephalon in the B isoform. Although mild neural phenotypes were discovered for several microexons that have not been previously characterized, including in , , , , , , and . This study establishes a general approach for investigating conserved alternative splicing events and prioritizes microexons for downstream analysis. - Source: PubMed
Publication date: 2025/11/18
Calhoun Caleb C SCapps Mary E SMuya KristieGannaway William CMartina VerdionConklin Claire LKlein Morgan CWebster Jhodi MTorija-Olson Emma GThyme Summer B - The MYST family of lysine acetyltransferases are transcriptional regulators often dysregulated in cancer. In cells, MYST members form distinct multiprotein complexes that guide their histone substrate specificity, but how this selectivity is conferred is not fully understood. Here we interrogate a complex-mediated change in the substrate preference of the MYST member KAT6A, a target for cancer therapeutics. KAT6A forms a 4-protein complex with BRPF1, ING4/5, and MEAF6 to acetylate H3K23. However, additional substrates (H3K9, H3K14, and H3K27) have been proposed, and whether these residues are modified by KAT6A is unclear. We determined the histone substrate specificity of uncomplexed forms of KAT6A, including full-length KAT6A (KAT6A) and the isolated acetyltransferase (MYST) domain, and the KAT6A 4-protein complex (KAT6A 4-plex). We show that the MYST domain and KAT6A preferentially acetylate H3K14, with this selectivity linked to a glycine pair preceding K14. A structure of the MYST domain bound to an H3K14-CoA bisubstrate inhibitor is consistent with a model in which the small size and flexibility of this glycine pair facilitate K14 acetylation. Notably, when KAT6A assembles into the 4-plex, H3K23 emerges as the favored substrate, with favorable recognition of an alanine-threonine pair before K23. These changes are mediated by BRPF1 and steady-state assays with H3 peptides indicate that this scaffold protein can alter the substrate preference of KAT6A by ≈10-fold. Such context-dependent specificity illustrates how the functional properties of MYST members can be modulated by associated proteins and underscores the importance of characterizing these enzymes in their free and complex forms. - Source: PubMed
Publication date: 2025/02/03
Sengupta Raghuvir NBrodsky OlegBingham PatrickDiehl Wade CFerre RoseAnnGreasley Samantha EJohnson EricKraus MichelleLieberman WhitneyMeier Jordan LPaul Thomas AMaegley Karen A