MYCBP Antibody
- Known as:
- MYCBP Antibody
- Catalog number:
- csb-ma8587101a0m
- Product Quantity:
- USD
- Category:
- -
- Supplier:
- CusAb
- Gene target:
- MYCBP Antibody
Related genes to: MYCBP Antibody
- Gene:
- MYCBP NIH gene
- Name:
- MYC binding protein
- Previous symbol:
- -
- Synonyms:
- AMY-1
- Chromosome:
- 1p34.3
- Locus Type:
- gene with protein product
- Date approved:
- 1999-11-26
- Date modifiied:
- 2016-10-05
Related products to: MYCBP Antibody
Related articles to: MYCBP Antibody
- miR-143-5p functions as a tumor-suppressive microRNA across various cancer types. The current study investigated the expression, prognostic value, and role of miR-143-5p in colorectal cancer (CRC). - Source: PubMed
Publication date: 2026/07/21
Mu ChenZhang Han - The central apparatus of motile cilia, consisting of central microtubules and various protein projections, is essential for dictating the ciliary movement. Although three proteins (FAP65, FAP147, and FAP70) have been localized to the C2a projection in , the full protein composition and functional roles of the vertebrate C2a remain inadequately defined. Here, we use three knockout mouse models corresponding to their respective homologs (, , and ) to systematically investigate their functions in vertebrates. Notably, all three knockout strains exhibit distinct phenotypes related to primary ciliary dyskinesia (PCD), including hydrocephalus and sinusitis. The ciliary incorporation of CCDC108, MYCBPAP, and CFAP70 is essential for one another's stability, with the loss of any single component triggering C2a collapse, which destabilizes the central pair microtubules, and ultimately alters the ciliary movement pattern. Furthermore, we significantly expand the vertebrate C2a proteome by identifying ARMC3 and MYCBP as additional C2a components. Collectively, our findings illuminate the proteomic composition and strict physiological requirements of the vertebrate C2a projection, providing new insights into the molecular pathogenesis of PCD. - Source: PubMed
Publication date: 2026/07/08
Lyu QianLi QingchaoLi JingruiLuo JiajunLiu ChunyuNai ShanshanLiu HongbinZhu XueliangSong TingLiu MinZhao Huijie - Papillary thyroid carcinoma (PTC) has shown a marked rise in incidence worldwide in recent decades, yet its molecular mechanisms remain largely unclear. Here, we reported that CBLB acts as a tumor suppressor in PTC. Analysis of public databases (GEPIA, UALCAN) and PTC cell lines confirmed reduced CBLB expression in tumor tissues compared to normal thyroid tissue. Functional experiments revealed that CBLB knockdown promoted malignant phenotypes, while its overexpression suppressed tumorigenic behaviors. Mechanistically, CBLB directly binds to MYCBP and promotes its poly-ubiquitination and proteasomal degradation via K48-linked ubiquitination at the K20 residue. MYCBP stabilization upon CBLB depletion activated the c-Myc pathway, upregulating oncogenic targets (CCND1, CDK4, ZEB1, E2F1, c-Jun) and downregulating E-cadherin. Collectively, our findings identify the CBLB/MYCBP/c-Myc axis as a critical regulatory pathway in PTC progression, highlighting CBLB's therapeutic potential as a targeted suppressor of MYCBP-driven oncogenesis. - Source: PubMed
Publication date: 2026/05/25
Yang YanliPei XiaoyanYang QingqingHu Xiaolei - The C2a projection of the central pair of flagella in Chlamydomonas reinhardtii harbours the A-kinase anchoring protein FAP65, FAP174, FAP147 and FAP70. FAP174, an RII-like protein with its N-terminal dimerization and docking domain, binds to the amphipathic helices of FAP65. Cryo-EM data do not reveal the entire sequences for FAP174 and FAP147. Hence, the interacting domains within this scaffold remain elusive. This study has identified the interacting domains of FAP174 with FAP147. The FAP147 protein and its MYCBPAP domain (129-639 a.a.) bind to the C-terminus of FAP174 (47-92 a.a.). In silico docking analyses using CABS-Dock to delineate the interaction identified several MYCBPAP-derived peptides, such as p3 (310-339), p4 (319-348), p9 (547-576), p13 (528-557) and p15 (350-379), to form stable interacting complexes with RMSD < 3 Å 2-3 times, and are potentially amphipathic. To gain atomistic details of the interaction, molecular dynamics (MD) simulations of the FAP147 MYCBPAP domain in complex with the FAP174 C-terminus were performed. It revealed stable interfacial contacts, a subset of which overlap with residues within the p15 peptide region of the MYCBPAP domain, while identifying G48, S49, P52, Y55, L79, Q80 and V83 as key interacting residues within the C-terminus of FAP174. Individual alanine substitution of the FAP174 residues, followed by overlay assay with FAP147, retained the interaction, indicating that the interaction does not depend solely on discrete amino acids but on broader interface interactions. - Source: PubMed
Publication date: 2026/02/22
Desai SnehaPal AbhayNair HridhyaDantu Sarath ChandraD'Souza Jacinta S - Under the U.S. Tobacco Regulatory Act of 2020, all novel nicotine-containing products require a Premarket Tobacco Product Application (PMTA) and FDA authorization before they can be marketed. However, lengthy PMTA review timelines have prompted some manufacturers to replace traditional nicotine with 6-methyl-nicotine (6-MN), a non-tobacco-derived analog that delivers comparable psychoactive effects while evading existing regulatory pathways. Despite its growing market presence as a purportedly "safer" alternative, the toxico-pharmacokinetic profile of 6-MN remains poorly characterized. This study assessed the toxicity after exposure to nicotine or 6-MN-containing e-liquid aerosols using a 3D EpiAirway tissue model. RT-qPCR analyses revealed differential effects on transcripts associated with DNA damage (53BP1, ATR), inflammation (NF-κB1), and cancer (MYCBP). Morphological evaluation of the airway tissues exposed to either aerosol showed an increase in epithelial thickness, a decrease in E-cadherin protein levels, increased goblet cell hypertrophy, evidenced by positive PAS staining and elevated mucus (MUC5AC protein) production, and a reduction in Occludin protein (part of the tight junction complex), which is suggestive of epithelial remodeling. Exposure to PG/VG aerosols alone significantly increased the release of MIP-1α, IFN-γ, and IL-4. Conversely, spearmint-flavored aerosols containing 6-MN or nicotine decreased several pro-inflammatory cytokines, significantly reducing TNF-α, Eotaxin, MCP-1, RANTES, and G-CSF levels, potentially via NF-κB and ERK1/2 pathways. Our findings reveal differential toxicological and chemical profiles for nicotine and 6-MN aerosols; however, flavorings may confer similar cytotoxicity, as measured by LDH and metabolic activity, in 6-MN formulations as they do in those with nicotine. Thus, 6-MN is not a "safer" nicotine alternative. - Source: PubMed
Publication date: 2026/01/31
Effah FelixSengupta MohanaSun YehaoFaizan Md ImamKaur GagandeepRaghu RheaElzein AtallahMarczylo TimStrongin Robert MRahman Irfan