Hsp25 Polyclonal Antibody
- Known as:
- Hsp25 Polyclonal Antibody
- Catalog number:
- ASASPA-801D
- Product Quantity:
- 50 µg
- Category:
- -
- Supplier:
- Other suppliers
- Gene target:
- Hsp25 Polyclonal Antibody
Related genes to: Hsp25 Polyclonal Antibody
- Gene:
- HSPB1 NIH gene
- Name:
- heat shock protein family B (small) member 1
- Previous symbol:
- -
- Synonyms:
- HSP27, HSP28, Hs.76067, Hsp25, CMT2F
- Chromosome:
- 7q11.23
- Locus Type:
- gene with protein product
- Date approved:
- 1991-07-09
- Date modifiied:
- 2019-04-23
Related products to: Hsp25 Polyclonal Antibody
Related articles to: Hsp25 Polyclonal Antibody
- The small heat shock protein HSPB1 is a ubiquitously expressed mechanoresponsive chaperone essential for cytoskeletal remodeling under mechanical load. Mutations in HSPB1, including S135F, cause Charcot-Marie-Tooth (CMT) peripheral neuropathy, yet the mechanisms underlying the selective vulnerability of peripheral nerves remain enigmatic. Here we demonstrate that substrate stiffness is a critical determinant of HSPB1-mediated neurodegeneration. Using stiffness-tunable polydimethylsiloxane (PDMS) substrates (1 kPa, 10 kPa, 2 MPa) and uniaxial cyclic stretch, we show that primary dorsal root ganglia (DRG) neurons and SH-SY5Y cells expressing HSPB1 exhibit profound deficits in mechanoadaptation. On compliant substrates (10 kPa), HSPB1 causes stretch-induced axon fragmentation and neuronal death, whereas HSPB1 confers robust neuroprotection. HSPB1 also disrupts stiffness-directed neuritogenesis in differentiated SH-SY5Y cells: HSPB1-expressing cells show optimal axonal outgrowth and βIII-tubulin expression on 10 kPa substrates mimicking muscle tissue stiffness, while HSPB1 mutants display disorganized focal adhesions and complete differentiation failure. Mechanistically, we uncover that HSPB1 dysregulates stage-specific transglutaminase (TGase) expression-insufficient TGase during early neuritogenesis impairs filopodia stabilization, whereas aberrant TGase persistence at late stages constrains axon extension. Our findings establish HSPB1 as a biomechanical sensor that integrates ECM stiffness signals to coordinate peripheral nerve regeneration, and identify defective mechanoadaptation as a previously unrecognized pathomechanism in CMT. These results open new avenues for stiffness-targeted therapeutic strategies in peripheral neuropathy. - Source: PubMed
Publication date: 2026/07/03
Xie JimingHan RonglinXu HaidongLi ZhiyuZhao JingyiWan YingPan XianchaoXing Juan - As global temperatures continue to rise, the incidence and mortality rates of heatstroke (HS) have significantly increased. However, the current forensic diagnostic standards lack clear pathological criteria for deaths caused by HS, and the mechanisms of multi-organ damage induced by HS are not yet fully understood. In this study, a rat model of HS-induced death was established under conditions of 39 ± 0.5 °C and 60% ± 5% humidity. Through histopathological observation, attenuated total reflection-Fourier transform infrared spectroscopy (ATR-FTIR) spectroscopy, and machine learning algorithms, the most severely damaged organs in HS were identified, including the hypothalamus, hippocampus, liver, and spleen. Next, we performed transcriptomic (UID mRNA-seq) and proteomic (Data-Independent Acquisition technology, DIA) analyses on the key target organ-the hypothalamus. Transcriptomic analysis revealed 447 differentially expressed genes (DEGs), with 197 genes upregulated and 250 genes downregulated. Proteomic analysis identified 692 differentially expressed proteins (DEPs), with 241 proteins upregulated and 451 proteins downregulated. Integrated multi-omics analysis indicated significant enrichment of pathways such as endoplasmic reticulum protein processing, MAPK signaling, and apoptosis following HS. Further, three key genes/proteins (Hspb1, Dnaja1, Jun) were identified and their expression changes in the hypothalamus of HS rats were validated using quantitative real-time PCR (qRT-PCR), Western blot, and immunohistochemistry. Overall, this study provides new insights into the diagnosis and mechanisms of HS and offers scientific evidence for the clinical treatment of HS. - Source: PubMed
Publication date: 2026/07/07
Xiong HongliBian CunhaoZhao YueWang Yu SenWei BiXiao HaoZhang LiZhu ShishengLi Jianbo - Apoptosis maintains tissue homeostasis, and its dysregulation is closely associated with breast cancer progression and therapeutic resistance. We performed an integrative analysis of apoptosis-related signaling in breast cancer tissues across five molecular subtypes and compared these patterns with systemic apoptotic responses following cryoablation of benign fibroadenomas. Gene expression profiling was conducted using mRNA microarrays and validated by qRT-PCR and ELISA. Apoptosis pathway activity was assessed with the MSigDB HALLMARK_APOPTOSIS gene set, including intrinsic and extrinsic pathway scoring and an apoptotic balance index (ABI). MicroRNA profiling combined with in silico analyses identified potential miRNA-mRNA interactions. A progressive shift toward reduced pro-apoptotic and enhanced stress-adaptive signaling was observed with increasing tumor aggressiveness, most pronounced in triple-negative and non-luminal HER2-positive cancers. This pattern included reduced intrinsic pathway activity, decreased ABI, downregulation of pro-apoptotic genes (, , ), and upregulation of stress-associated or cytoprotective genes (, ). Several expression patterns were accompanied by overexpression of miRNAs (miR-582-5p, miR-421, miR-106b-5p, miR-20a-5p, miR-20b-5p, miR-93-5p) predicted to target apoptosis-related genes. In contrast, fibroadenoma cryoablation was associated with transient systemic modulation of apoptosis-related genes and proteins followed by gradual normalization. These findings highlight differences between apoptosis-related dysregulation in malignant tissue and regulated systemic responses following benign tissue injury, supporting pathway-level interpretation and identifying candidate molecular networks warranting further mechanistic and translational investigation. - Source: PubMed
Publication date: 2026/06/07
Panfil AgataBoroń KacperSirek TomaszSirek AgataZmarzły NikolaWróbel MichalinaWróbel ZbigniewBoroń DariuszOssowski PiotrStefaniak MartynaOrdon PawełWyrobiec GrzegorzKulej WojciechOpławski MarcinOpławski BogusławLekston NataliaGrabarek Beniamin Oskar - Heat shock protein 27 (HSP27) is a crucial member of the small heat shock protein family with a molecular weight of approximately 27 kDa, playing key roles in cellular stress response, protein homeostasis, and cell survival regulation. Recent studies have revealed that HSP27 plays a complex dual role in the pathogenesis of autoimmune diseases, which we define as the "HSP27 Dual Regulatory Paradox." Aim To systematically review the bidirectional immunomodulatory mechanisms of HSP27 in autoimmune diseases and to evaluate its clinical potential as a disease biomarker and therapeutic target, based on a "cell type-microenvironment-disease stage" three-dimensional regulatory model. - Source: PubMed
Publication date: 2026/06/24
Li JianbinLi RenheWang WenwenGesang YuzhenLiu Wei - The aim of this study was to evaluate circulating levels of heat shock protein 27 (HSPB1, Hsp27), heat shock protein 60 (HSPD1, Hsp60) and heat shock protein 90 (HSPC1, Hsp90) in a large cohort of healthy non-pregnant and pregnant women, as well as in patients with preeclampsia. In addition, we investigated whether serum levels of these heat shock proteins are associated with clinical characteristics and routine laboratory parameters of the study population. - Source: PubMed
Publication date: 2026/06/15
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