BAG3 antibody
- Known as:
- BAG3 (anti-)
- Catalog number:
- orb101835
- Product Quantity:
- EUR
- Category:
- -
- Supplier:
- Biorbyt biorb
- Gene target:
- BAG3 antibody
Related genes to: BAG3 antibody
- Gene:
- BAG3 NIH gene
- Name:
- BCL2 associated athanogene 3
- Previous symbol:
- -
- Synonyms:
- -
- Chromosome:
- 10q26.11
- Locus Type:
- gene with protein product
- Date approved:
- 1999-04-23
- Date modifiied:
- 2019-04-23
Related products to: BAG3 antibody
Related articles to: BAG3 antibody
- Mechanical stress plays a critical role in regulating cardiomyocyte structure and physiology. However, mechanobiology studies still rely on static systems that failed to capture the progressive nature of native cardiac remodeling. Building on our prior shape memory polymer (SMP)-based platform, the present study integrates microcontact printing onto SMP substrates to achieve single-cell geometric control and on-demand dynamic mechanical modulation. Using CRISPR/Cas9-engineered MYBPC3- and BAG3-mutant hiPSC-CMs along with isogenic wild-type (WT) control, we systematically assessed sarcomere organization and contractile behavior under static and dynamic mechanical conditions. WT hiPSC-CMs displayed robust morphological adaptability and coordinated sarcomere remodeling in response to dynamic mechanical cues, whereas MYBPC3- and BAG3-deficient hiPSC-CMs exhibited mutation-specific defects in sarcomere integrity and contractile behavior that were exacerbated by dynamic mechanical stress. These results demonstrate that this SMP-based platform enables us to systematically compare genotype-based mechanical sensitivity to develop more severe cardiomyopathy phenotypes. - Source: PubMed
Publication date: 2026/09/11
Wang ChenyanMai Nhu YDonelson Fred JMoradi Nasab SusanShi HuaiyuYang HuaxiaoMather Patrick TWang XinruiHenderson James HMa Zhen - Cardiovascular disease (CVD) is a result of complex pathophysiological processes affecting the heart and blood vessels. Heat shock proteins (HSPs) are evolutionarily conserved molecular chaperones that play key roles in maintaining protein homeostasis and cell survival under various stress conditions. Studies have shown the role of HSPs in diseases, including autoimmune disorders, liver, pancreatic, cancer, diabetes, and kidney disorders. Important findings regarding the role of HSPs in cardiovascular diseases include atherosclerosis, ischemic heart disease, atrial fibrillation, cardiomyopathy, heart failure, deep vein thrombosis, and peripheral vascular disease. Several proteins related to HSPs have been identified in various molecular mechanisms, including autophagy, apoptosis, oxidative stress, inflammatory responses, and fibrosis in cardiac disease. This review provides a comprehensive overview of the molecular biology and classification of HSPs, including extracellular HSPs, small HSPs, and co-chaperone molecules. We explored the roles of HSPs in regulated cell death mechanisms and in modulating oxidative stress and inflammatory responses. Furthermore, we demonstrated the pathological and protective roles of specific HSPs by regulating gene expression in response to drugs and cytokines, including geldanamycin and geranylgeranylacetone (GGA), across various cardiovascular conditions, highlighting the potential for HSP-targeted therapies. Promising strategies, including small-molecule inhibitors, inducers, and gene therapies, such as Bcl-2-associated athanogene 3 (BAG3) modulation, are discussed in the context of clinical relevance and therapeutic potential. However, despite promising experimental and clinical evidence, the translational application of HSPs remains limited by their context-dependent biological functions, the lack of standardized biomarker assays, heterogeneous clinical findings, and insufficient large-scale prospective validation. This narrative review was not prospectively registered, and received no external funding. It was conducted by searching PubMed, Scopus, Google scholar and Web of Science for relevant published articles. Understanding the multifaceted roles of HSPs offers new insights into cardiovascular disease mechanisms and paves the way for novel diagnostic and therapeutic approaches. - Source: PubMed
Publication date: 2026/08/19
Naderi NiloofarBolhassani AzamPirani Fatemeh - Chronic obstructive pulmonary disease (COPD) has high morbidity and mortality, and integrated stress response (ISR) participates in its progression. Traditional COPD diagnosis relies mainly on GOLD criteria, while ISR-based auxiliary molecular markers are still lacking. This study aimed to comprehensively analyze and identify ISR-related biomarkers in COPD, and to uncover their underlying molecular mechanisms. - Source: PubMed
Publication date: 2026/09/01
Liu XuepingWang LuTang TingQian HangHe BinfengXu ZhiWang GuansongZhang Mingzhou - Hypertrophic cardiomyopathy (HCM) is a heritable trait with marked variability in expression and outcomes. Our aims were to discover new genetic loci associated with HCM and to test the effect of a new polygenic risk score (PRS) on incidence, phenotype and outcomes stratified by genotype status. - Source: PubMed
Publication date: 2026/09/04
Lopes Luis RAung NayVan Duijvenboden StefanNicholls Hannah LBurns RichardJager JoannaLorenzini MassimilianoAkhtar Mohammed MajidProtonotarios AlexandrosBarbeito-Caamaño CayetanaLarrañaga-Moreira Jose MaríaBarriales-Villa RobertoColey KayeshaBatini ChiaraSze GeraldTobin Martin DJohn CatherinePetersen Steffen ESyrris PetrosMunroe Patricia BElliott Perry M - Chaperone-assisted selective autophagy (CASA) is a crucial process aimed at maintaining proteostasis in several neurodegenerative diseases associated with protein misfolding, including polyglutamine (polyQ) diseases. Autophagy is a critical lysosome-mediated degradation pathway, particularly essential in neurons, which are highly susceptible to proteotoxic stress due to their post-mitotic nature. Selective autophagy pathways, including CASA, ensure the targeted removal of misfolded proteins and damaged organelles, thereby preserving cellular homeostasis. CASA is based on the intersection of chaperones and autophagy, where HSPB8 and BAG3 interact with HSPA and STUB1 forming a complex that identifies, ubiquitinates, and directs aberrant proteins toward autophagosomes for subsequent lysosomal degradation. In polyQ diseases, such as spinal and bul muscular atrophy (SBMA) and Huntington's disease (HD), mutant proteins accumulate, overwhelming the protein quality control systems. The CASA components are upregulated as a compensatory response, promoting toxic aggregates clearance and cellular damage mitigation. However, chronic proteotoxic stress and progressive impairment of autophagic and lysosomal pathways eventually limit CASA efficiency, contributing to disease progression. The review highlights how CASA exerts its protective activities in polyQ diseases and reports therapeutic strategies aimed at enhancing CASA activity, including pharmacological inducers and combinatorial approaches targeting autophagy and the ubiquitin-proteasome system. Overall, CASA emerges as a crucial adaptive mechanism and a promising therapeutic target in polyQ-related neurodegeneration. - Source: PubMed
Publication date: 2026/09/03
Tedesco BarbaraChierichetti MartaCristofani RiccardoPoletti Angelo