HSF2BP Antibody
- Known as:
- HSF2BP Antibody
- Catalog number:
- XW-7878
- Product Quantity:
- 0.05 mg
- Category:
- -
- Supplier:
- Prosci
- Gene target:
- HSF2BP Antibody
Related genes to: HSF2BP Antibody
- Gene:
- HSF2BP NIH gene
- Name:
- heat shock transcription factor 2 binding protein
- Previous symbol:
- -
- Synonyms:
- -
- Chromosome:
- 21q22.3
- Locus Type:
- gene with protein product
- Date approved:
- 1999-08-26
- Date modifiied:
- 2014-11-19
Related products to: HSF2BP Antibody
Related articles to: HSF2BP Antibody
- The tumor microenvironment plays a critical role in the progression and metastasis of lung adenocarcinoma (LUAD), characterized by its immunosuppressive nature. Identifying the mechanisms that contribute to the remodeling of this environment is essential for developing therapeutic strategies. Heat shock factor 2-binding protein (HSF2BP) is implicated in tumor proliferation and immune evasion, but the mechanisms by which HSF2BP exerts these effects remain poorly understood. This study investigates the role of HSF2BP in modulating Basonuclin 1 (BNC1) expression and subsequent immune responses in LUAD. Matched tumor and adjacent normal tissue samples from 30 LUAD patients were collected between January 2023 and June 2024. Using lentiviral transduction, HSF2BP and BNC1 were overexpressed or knocked down in LUAD cell lines. Gene and protein expression were quantified by real-time quantitative polymerase chain reaction (RT-qPCR) and Western blotting. We analyzed the immunological profile of LUAD tumors and assessed the interaction between HSF2BP and the BNC1/Transforming Growth Factor Beta (TGF-β)/SMAD3 signaling pathway through in vitro and in vivo experiments. Immune profiling included flow cytometry for Natural Killer (NK) cells and ELISA for cytokine analysis (IL-2, IL-4, IL-10, INF-γ, and TNF-α). In vivo studies involved subcutaneous tumorigenesis in BALB/c nude mice. Immunohistochemistry and co-immunoprecipitation were used to validate protein interactions and to assess remodeling of the tumor immune microenvironment. HSF2BP expression was markedly higher in LUAD tissues in matched adjacent normal tissues, whereas BNC1 expression was significantly reduced. Overexpression of HSF2BP in LUAD cells (H1299) enhanced proliferation, reduced the proportion of NK cells, decreased levels of IFN-γ, IL-2, and TNF-α, and increased levels of IL-4 and IL-10. Conversely, knockdown of HSF2BP in A549 cells reduced proliferation and restored the proportion of NK cells and levels of pro-inflammatory cytokines. In vivo studies using HSF2BP-overexpressing mice confirmed these findings, demonstrating increased tumor volumes and altered cytokine profiles. Molecular assays revealed that HSF2BP binds directly to BNC1, with the C-terminal hydrophobic domain being essential for this interaction, thereby modulations in TGF-β and SMAD3 signaling pathways. HSF2BP significantly promotes LUAD progression by modulating the BNC1/TGF-β/SMAD3 signaling axis and reshaping the tumor immune microenvironment. Targeting the HSF2BP-BNC1 interaction can provide novel therapeutic strategies for enhancing immune responses against LUAD. - Source: PubMed
Publication date: 2025/10/13
Liu JunyuanHan ZhigangChen LijuanSun Gang - In meiotic homologous recombination (HR), BRCA2 facilitates loading of the recombinases RAD51 and DMC1 at the sites of double-strand breaks (DSBs). The HSF2BP-BRME1 complex interacts with BRCA2. Its absence causes a severe reduction in recombinase loading at meiotic DSB. We previously showed that, in somatic cancer cells ectopically producing HSF2BP, DNA damage can trigger HSF2BP-dependent degradation of BRCA2, which prevents HR. Here, we report that, upon binding to BRCA2, HSF2BP forms octameric rings that are able to interlock into a large ring-shaped 24-mer. Addition of BRME1 leads to dissociation of both of these ring structures and cancels the disruptive effect of HSF2BP on cancer cell resistance to DNA damage. It also prevents BRCA2 degradation during interstrand DNA crosslink repair in egg extracts. We propose that, during meiosis, the control of HSF2BPBRCA2 oligomerization by BRME1 ensures timely assembly of the ring complex that concentrates BRCA2 and controls its turnover, thus promoting HR. - Source: PubMed
Publication date: 2023/10/27
Ghouil RaniaMiron SimonaSato KoichiRistic Dejanvan Rossum-Fikkert Sari ELegrand PierreOuldali MalikaWinter Jean-MarieRopars VirginieDavid GabrielArteni Ana-AndreeaWyman ClaireKnipscheer PuckKanaar RolandZelensky Alex NZinn-Justin Sophie - Glioblastoma (GBM) is notorious for its clinical and molecular heterogeneity, contributing to therapeutic failure and a grim prognosis. is one of the tumor suppressor genes important in nervous tissue or related pathologies, which was scarcely investigated in GBM for reliable associations with prognosis or disease progression despite known alterations. Recently, we observed a phenotypic heterogeneity between GBM cell lines (U87MG, T98G, U251MG, DBTRG-05MG), among which the anti-GBM activity of was generally corresponding, but colony growth and formation were inconsistent in DBTRG-05MG. This prompted us to investigate the molecular landscapes of these cell lines, intending to translate them into the clinical context. - Source: PubMed
Publication date: 2023/09/15
Kałuzińska-Kołat ŻanetaKołat DamianKośla KatarzynaPłuciennik ElżbietaBednarek Andrzej K - Endoplasmic reticulum (ER) stress plays an important role in the occurrence and development of various liver diseases. However, there are no effective prevention and treatment strategies. We aimed to determine the role of heat shock factor 2 binding protein (HSF2BP) in ER stress. - Source: PubMed
Publication date: 2023/03/24
Zhang JiaWang TaoBi JianbinKe MengyunRen YifanWang MengzhouDu ZhaoqingLiu WumingHu LiangshuoZhang XiaogangLiu XueminWang BoWu ZhengLv YiMeng LingzhongWu Rongqian - Leishmaniosis, one of the most important zoonoses in Europe, is caused , an intracellular protozoan parasite. This disease is endemic in the Mediterranean area, where the main reservoir is the dog. Several studies indicate a possible susceptibility to infection with clinical signs in some canine breeds. One of them is the boxer breed, which shows a high prevalence of disease. In this study, immunological and genomic characterization of serum samples from boxer dogs living in the Mediterranean area were evaluated to analyze the immune response and the possible genetic explanation for this susceptibility. Serum levels of cytokines IFN-γ, IL-2, IL-6, IL-8, and IL-18 were determined by ELISA commercial tests, while the genotyping study was performed using the CanineHD DNA Analysis BeadChip. The results show relevant differences in the serum levels of cytokines compared to published data on other canine breeds, as well as sequence changes that could explain the high susceptibility of the boxer breed to the disease. Concretely, polymorphic variants in the , , , , , , , , , and genes were found, which could explain the susceptibility of this breed to infection. - Source: PubMed
Publication date: 2022/11/02
Álvarez LuisMarín-García Pablo-JesúsRentero-Garrido PilarLlobat Lola