MTBP Antibody
- Known as:
- MTBP Antibody
- Catalog number:
- 2447
- Product Quantity:
- 0.1 mg
- Category:
- -
- Supplier:
- Prosci
- Gene target:
- MTBP Antibody
Related genes to: MTBP Antibody
- Gene:
- MTBP NIH gene
- Name:
- MDM2 binding protein
- Previous symbol:
- -
- Synonyms:
- -
- Chromosome:
- 8q24.12
- Locus Type:
- gene with protein product
- Date approved:
- 2000-08-23
- Date modifiied:
- 2016-10-05
Related products to: MTBP Antibody
Related articles to: MTBP Antibody
- Despite the near-complete elimination of cholera in many developing countries, numerous lower-income countries continue to face recurring epidemics. Although extensive research has been conducted on cholera transmission dynamics and control, a comprehensive approach to managing outbreaks in resource-limited settings remains elusive. This study introduces a cholera epidemic model incorporating a resource allocation strategy to balance efforts between reducing transmission and enhancing recovery rates. The model is validated using weekly cholera data from the resurgence in Haiti (October 2022-March 2023) to estimate key parameters and the control reproduction number . Based on these estimated parameters, the proposed model exhibits rich dynamical behavior, including backward and Hopf bifurcations, highlighting its potential for a multi-wave epidemic pattern. Using a continuous-time Markov chain (CTMC) model and the Gillespie algorithm, we calculate the extinction probability of cholera, comparing it with multitype branching process (MTbp) results, which estimate the analytical form of the probability of cholera extinction and outbreak, showing excellent agreement. Finally, construct a nonlinear programming problem (NLPP) to find the optimal combination of resources to minimize outbreak probability. In solving this NLPP, we find that prioritizing resources to recovery improve interventions is more effective than reducing transmission to minimize the probability of disease outbreak. These insights can guide resource allocation strategies to reduce cholera outbreaks in resource-constrained settings. - Source: PubMed
Publication date: 2026/05/13
Panda SudiptaHalder SujitChattopadhyay Joydev - Earlier detection of colorectal cancer (CRC) can improve survival rates. A simple, effective blood test may help improve screening participation. The multi-target blood protein (MTBP; ColoSTAT) test and algorithm uses concentrations of five protein biomarkers of CRC and patient's sex and age to generate a CRC likelihood score. We compared the performance of the MTBP test in detecting CRC to colonoscopy, the 'gold standard'. - Source: PubMed
Publication date: 2026/01/16
He Emily Yvan Hazel Guy ASloss Andrew MPianko StephenBrown Gregor JClingan Philip RSingh RajvinderSolterbeck Ann CTraficante RobertFormby-Miller LouiseLockett TrevorMacrae Finlay - Replication origins in human cells form clusters ranging from tens to hundreds of kilobases called initiation zones (IZs), typically located in intergenic regions between active genes. On a larger megabase scale, chromosomes replicate following temporally defined replication timing (RT), where euchromatic regions replicate early, and heterochromatic regions replicate late. Although the stochastic model of IZ firing with a temporally regulated limiting factor can explain RT formation, this limiting factor in human cells remains unclear. To investigate the relationship between IZ and RT, we map the temporal firing pattern of IZs and examine the genome-wide distributions of replication licensing and firing factors in human cells. We identify TRESLIN-MTBP as a key limiting firing factor for replication initiation. Its loading onto phosphorylated MCM2-7 double hexamer (MCM-DH) is controlled by the opposing phosphorylation events on MCM-DH by Dbf4-dependent kinase and RIF1-Protein Phosphatase 1, which ultimately determine IZs and establish RT. - Source: PubMed
Publication date: 2025/12/02
Zhu XiaoxuanBektash AtabekHatoyama YukiMuramatsu SachikoIsobe Shin-YaObuse ChikashiToyoda AtsushiDaigaku YasukazuChen Chun-LongKanemaki Masato T - Multiple myeloma (MM), as an incurable hematologic malignancy, is driven by chromosomal translocations. Recent research suggests that targeting phase separation may offer a new therapeutic vulnerability for MM. The transcription factor c-Maf is implicated in MM-associated translocations and undergoes liquid-liquid phase separation (LLPS). Although c-Maf is historically classified as "undruggable" for its transcription factor nature, we propose a new therapeutic strategy targeting its phase separation mechanism. Comprehensive in vitro and in vivo experiments indicated that elevated c-Maf promoted MM progression through LLPS. Mechanistically, the alanine-rich intrinsically disordered regions (IDRs) in c-Maf drive hydrophobic interactions, enabling phase separation. These IDRs recruit RNA Polymerase II (RNA Pol II) through similar interactions, forming oncogenic condensates that activate the Mtbp/c-Myc axis. Notably, we discovered benzoyl benzoic acid (BBA) as a candidate compound targeting the inter-IDR interaction domain of c-Maf. BBA binding impedes c-Maf's LLPS capacity, consequently blocking RNA Pol II recruitment and Mtbp transcriptional activation. This mechanistic interference successfully inhibited c-Myc-driven MM progression in experimental models. Our study demonstrates that c-Maf-driven LLPS activates the c-Maf/RNA Pol II/Mtbp/c-Myc axis, highlighting phase separation targeting as a promising therapeutic strategy for translocation-associated MM patients. - Source: PubMed
Publication date: 2025/11/11
Wang ZeGuo MengjieYu XichaoSun YiBai HaowenZhou LianxinLiu ZihaoHuang HongmingWang ChongLiu HongGu ChunyanYang Ye - MDM2 binding protein (MTBP) is a protein that interacts directly with MDM2. This study characterized the LvMTBP, revealing a 2752 bp cDNA sequence encoding an 834-amino acid hydrophilic protein with conserved MTBP_N and MTBP_C domains. Phylogenetic analysis demonstrated close evolutionary relationships with Penaeus species. LvMTBP exhibited ubiquitous tissue expression, with highest levels in muscle. Under ammonia and nitrite nitrogen stress, LvMTBP expression was downregulated in gills and muscle. RNAi experiments showed that LvMTBP knockdown dramatically reduced shrimp survival rates under both stress conditions. Histopathological examination revealed severe tissue damage in hepatopancreas and gills following LvMTBP silencing. Mechanistic investigations demonstrated that LvMTBP depletion activated the p53-mediated mitochondrial apoptosis pathway, evidenced by upregulated Bax, p53, and Caspase 9 expression, downregulated Bcl-2 and MDM2, and increased Caspase-3 activity. Apoptosis assays confirmed higher apoptotic indices in LvMTBP-knockdown groups. Complementary experiments in HEK293T cells showed MTBP overexpression reduced apoptosis rates, supporting its anti-apoptotic function. These findings establish LvMTBP as a crucial regulator of environmental stress responses in L. vannamei, functioning through modulation of the p53-MDM2 axis and apoptosis pathways. The study provides newly identified insights into crustacean stress adaptation mechanisms and suggests LvMTBP as a potential molecular target for improving shrimp tolerance in aquaculture systems. - Source: PubMed
Publication date: 2025/10/03
Zhou XiaoxunHou YongkangZhang YuanLei YexinLiu Jianyong