HSBP1 Antibody
- Known as:
- HSBP1 Antibody
- Catalog number:
- csb-pa00454a0rb
- Product Quantity:
- USD
- Category:
- -
- Supplier:
- CusAb
- Gene target:
- HSBP1 Antibody
Related genes to: HSBP1 Antibody
- Gene:
- HSBP1 NIH gene
- Name:
- heat shock factor binding protein 1
- Previous symbol:
- -
- Synonyms:
- -
- Chromosome:
- 16q23.3
- Locus Type:
- gene with protein product
- Date approved:
- 1998-07-30
- Date modifiied:
- 2014-11-19
Related products to: HSBP1 Antibody
Related articles to: HSBP1 Antibody
- Background: Heat shock protein beta 1 (HSPB1) is confirmed to be a ferroptosis-related gene and plays an important role in the progression of diabetic cardiomyopathy (DCM). However, the specific functions and underlying molecular mechanisms of HSPB1 in DCM progression remain to be revealed. Methods: Cardiomyocytes were exposed to high glucose (HG) to mimic DCM cell models. The levels of HSPB1, tripartite motif-containing 55 (TRIM55), upstream stimulating factor 1 (USF1) and fibrosis-related markers were detected using western blot. Cell viability, apoptosis, inflammation, ferroptosis and mitochondrial membrane potential depolarization were assessed by CCK8 assay, flow cytometry, ELISA, corresponding kit and JC-1 staining. The interaction between TRIM55 and HSPB1 or USF1 was confirmed by Co-IP assay, ubiquitination assay, and dual-luciferase reporter assay. Diabetic mouse models were constructed by streptozotocin to assess the role of HSPB1 in vivo. Results: Overexpression of HSPB1 suppressed HG-induced cardiomyocyte apoptosis, ferroptosis, inflammation, mitochondrial dysfunction and fibrosis. TRIM55 enhanced the protein degradation of HSPB1 through ubiquitination, and the inhibitory effect of TRIM55 knockdown on HG-induced cardiomyocyte injury could be reversed by HSPB1 silencing. USF1 bound to TRIM55 promoter to activate its transcription. USF1 knockdown inhibited HG-induced cardiomyocyte injury by mediating the TRIM55/HSPB1 axis. In animal study, HSPB1 overexpression could improve cardiac function, alleviate inflammation and fibrosis in diabetic mouse models. Conclusion: The USF1/TRIM55/HSPB1 axis proposed in this study provides a potential molecular target for the treatment of DCM. - Source: PubMed
Publication date: 2026/04/10
Huang LiuZheng ChengHe CuizhuQiu XiangWei HuiqingYan JieCui KunYang WenhuiYao LizhuoWei YulianNie XiaohongGuo Bingyan - Spinocerebellar ataxia type 3 (SCA3) is a polyglutamine (polyQ) neurogenerative disorder that results from CAG trinucleotide repeat expansions in the ATXN3 gene, leading to toxic protein aggregate formation and cellular pathway dysfunction. The dysfunction of cellular pathways also correlates with stress responses, such as the formation of stress granules (SG). Recent research suggests that SG and their components contribute to polyglutamine disease pathogenesis. - Source: PubMed
Publication date: 2026/03/19
Moreira-Gomes TiagoMarcelo AdrianaRajado Ana TeresaCosta Rafael GAfonso-Reis RicardoMadeira Cristiana RAfonso Inês TBrito David V CVaz Adriana ANóbrega Clévio - The cerebellar cortex presents a repetitive structure, but the main projecting neurons of this tissue, the Purkinje cells, are not identical and behave differently to various types of injury. Common patterns of neurodegeneration exist, where certain Purkinje cells die earlier than others. By contrast, lobe X of the cerebellum is a particularly resistant structure, independently of the cerebellar disease or damage. However, the mechanisms underlying the survival capability of these especially resistant Purkinje cells are still unknown. In this work, we have used the Purkinje Cell Degeneration (PCD) mouse, a model of severe cerebellar degeneration that also reproduces the human disease called childhood-onset neurodegeneration with cerebellar atrophy, to study Purkinje cell resistance. After an exhaustive immunochemical analysis of the different subpopulations of Purkinje cells, the Heat Shock Protein 25 (HSP25) and its phosphorylated version HSP25-P-Ser15 were found to be especially induced in lobe X of PCD mice. As this protein has neuroprotective properties, it may be responsible for resistance against cerebellar neurodegeneration. Taking into account the constant resistance of lobe X, the use of HSP25 may lead to new possibilities for achieving natural protection both in cerebellum and in other brain structures, or even for developing future neuroprotective therapies. - Source: PubMed
Publication date: 2026/01/23
Hernández-Pérez CarlosPérez-Revuelta LauraTéllez de Meneses Pablo GCabedo Valeria LAlonso José RamónDíaz DavidWeruaga Eduardo - Colorectal cancer exhibits limited responsiveness to immune-checkpoint blockade, primarily because an elevated intratumoral Treg/CD8 T-cell ratio extinguishes antitumor immunity. The molecular determinants that lock this immunosuppressive balance are unknown. - Source: PubMed
Publication date: 2026/02/10
Hu QiLu YangZhong XiaolanHuang PengZheng LishengJiang Bing-HuaLi WanglinZheng Song Guo - The Nonalcoholic fatty liver disease (NAFLD) is a major chronic liver condition, with its pathology remaining elusive. Consequently, a thorough exploration of the underlying mechanisms driving NAFLD progression is essential for a comprehensive understanding of this metabolism-associated disorder. - Source: PubMed
Publication date: 2026/02/02
Zhang XuechunCheng YingYu RunzhiHu XiaonaHuang Yiqin