Human HSP27 PicoKine ELISA Kit
- Known as:
- Human HSP27 PicoKine Enzyme-linked immunosorbent assay test Kit
- Catalog number:
- EK0881
- Product Quantity:
- 1x96 well plate
- Category:
- -
- Supplier:
- boster immunoleader
- Gene target:
- Human HSP27 PicoKine ELISA Kit
Related genes to: Human HSP27 PicoKine ELISA Kit
- 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: Human HSP27 PicoKine ELISA Kit
Related articles to: Human HSP27 PicoKine ELISA Kit
- Photodynamic therapy, as an efficient and safe method, has attracted the attention of experts. This therapeutic method is based on the application of photosensitizers and light radiation. This study was designed to assess the possible molecular mechanism of rhodium nanoparticle-based photodynamic therapy through protein-protein interaction (PPI) network analysis of proteomic data from the literature. Proteomic data about rhodium nanoparticle-based photodynamic therapy effect on the HeLa cell line proteome were retrieved from the literature and were included in the CluePedia application of Cytoscape software to create a directed PPI network. The network was analyzed, and the crucial targeted proteins were identified and compared with genes in GeneCards for "HeLa cell line" and "cervical cancer". The common gene and protein were selected and discussed. A directed PPI network of 105 proteins was formed. Six sub-networks were selected for further investigation. Comparison of the PPI data and the genes from the GeneCards database led to the introduction of HLA-B, CYCS, CD44, HSPB1, and RBBP4 as the critical targeted proteins by the applied treatment. In conclusion, a sub-network including HLA-B, CYCS, CD44, and HSPB1 and another sub-network containing RBBP4 and its neighbors were highlighted as the core of molecular effects of the applied rhodium nanoparticle-based photodynamic therapy. - Source: PubMed
Publication date: 2026/04/22
Hossein-Khannazer NikooArjmand BabakRazzaghi ZahraRazi FaridehBandarian FatemehAhmadzadeh Alireza - Cisplatin stands as a highly effective chemotherapeutic agent for ovarian cancer (OC); yet, the development of resistance to it poses a significant clinical challenge. In this study, we utilized prior RNA-sequencing and immunoprecipitation-mass spectrometry (IP-MS) data to identify downstream genes and interacting proteins altered following ESM1 knockdown, and further confirmed the impact of these changes on ferroptosis and cisplatin resistance in OC cells through electron microscopy and various molecular biology experiments. Additionally, public databases, tissue microarrays, and multiplex immunofluorescence staining were employed to assess the prognostic value of genes like ESM1 for OC patients. The results demonstrate that HSPB1 acts as a pivotal gene in ESM1-mediated cisplatin and ferroptosis resistance. Mechanistically, ESM1 binds to ERBB2 to promote HSPB1 transcription, thereby activating the FAK/SRC and NF-κB pathways, which ultimately inhibits ferroptosis and enhances cisplatin resistance in OC. Collectively, these findings elucidate a regulatory mechanism by which ESM1 drives cisplatin and ferroptosis resistance via the ERBB2/FAK/SRC/HSPB1/NF-κB axis in ovarian cancer. - Source: PubMed
Publication date: 2026/05/22
Zhang JuanTan YingzhengYang HaibingTang XingLiu DanZhou WenchaoZeng TianLiu XueruLi MiaoChen XunZou JuanLi Yukun - The heat shock protein beta-1 (HSPB1/HSP27) is highly expressed and phosphorylated in cancer tissues. However, the precise role of HSPB1 in cancer remains unclear. In this study, we report the unexpected findings elucidating the essential role of HSPB1 in adapting amino acid deficiency by upregulating amino acid transporter SLC7A5 function. HSPB1 regulates estrogen receptor-positive (ER+) breast cancer cell proliferation in a SLC7A5-dependent manner. In response to cellular stress, which is specified as amino acid-deficient conditions, HSPB1 was phosphorylated at Ser 78 residue by stress MAPK p38. SLC7A5 is associated with phosphorylated HSPB1 for its functional activation, leading to upregulated amino acid incorporation. In addition, HSPB1 and SLC7A5 overexpression increased acetylated α-tubulin levels. SLC7A5 overexpression did not change acetyl-CoA level, but SLC7A5 knockdown decreased ATAT1 and induced HDAC6 upregulation. Furthermore, HSPB1 and SLC7A5 induced paclitaxel and tamoxifen resistance. Therefore, the HSPB1-SLC7A5 axis contributes to the acquisition of tolerance to both tamoxifen and paclitaxel in breast cancer cells, uncovering a novel therapeutic target against drug resistance in breast cancer. - Source: PubMed
Publication date: 2026/05/27
Suzuki YukakoKitayama NarumiKudo RyuheiSilwal KarishmaMatsuda ShioriOhishi MakiUeno AyanoAshitani SanaeIgarashi KaoriMasuda TakeshiIshikawa TakamasaSoga TomoyoshiSaito Yasuhiro - Glioblastoma (GBM) is the most aggressive primary brain tumor with a dismal prognosis. Ferroptosis is implicated in GBM pathogenesis. Heat shock protein B1 (HSPB1) is associated with tumor progression, yet its precise function and regulatory mechanism in GBM ferroptosis remain elusive. Differentially expressed genes were identified from the GSE151352 dataset. WGCNA was employed to identify GBM-associated modules, which were then intersected with genes from the FerrDb V2 database. HSPB1 expression and prognostic value were validated using TCGA and GEPIA databases, and clinical specimens. Functional assays (EdU, TUNEL, and Transwell) and ferroptosis indicators (lipid ROS, Fe, GSH) were assessed following HSPB1 modulation. Bioinformatics tools predicted METTL1-mediated m7G modification of HSPB1, and results were validated by RIP, dual-luciferase reporter assay, and mRNA stability assays. Transcriptional regulation of HSPB1 by HOXA5 was predicted and confirmed. A subcutaneous xenograft model was used to evaluate the METTL1-HSPB1 axis in vivo. Analysis revealed 2985 DEGs. WGCNA identified a GBM-correlated "red" module; intersection with ferroptosis genes pinpointed HSPB1. HSPB1 was significantly overexpressed in GBM, correlating with poor patient survival. HSPB1 knockdown suppressed GBM cell proliferation, migration, invasion, and induced ferroptosis. Mechanistically, METTL1 mediated m7G modification to HSPB1 mRNA to enhance its stability. Concurrently, HOXA5 bound to the HSPB1 promoter to activate its transcription. Silencing either METTL1 or HOXA5 downregulated HSPB1, inhibiting GBM malignant phenotypes. In vivo, the METTL1-HSPB1 axis promoted tumor growth. METTL1 stabilizes HSPB1 mRNA through m7G methylation, and HOXA5 transcriptionally activates HSPB1 expression. This regulation promotes GBM malignant progression. - Source: PubMed
Publication date: 2026/05/27
Li HongchaoChen YushengZhu YanyanKe ShanbaoWu Danting - Ninety-five structurally diverse chemically synthesized compounds, retrieved from the chemical library of the national research infrastructure OPENSCREEN-GR, were subjected here to a structure-agnostic bioactivity-driven screen focused on putative anti-cancer activities using a number of human cell lines derived from diverse types of cancer. Interestingly, the top four compounds that displayed a broad anti-cancer activity (with no apparent photosensitizing activity) during unbiased biological evaluation were then identified as phenoxazine derivatives. In addition to their cytotoxic activity, phenoxazine derivatives BS115 and ST61 were also found to be cytostatic by inducing a p53-independent G2/M cell cycle arrest as well as a G0/G1 arrest only in cells harboring a functional p53. A kinetics analysis using two multiplex immunoassays and siRNA-mediated knockdown of HSP27 revealed that the latter protein is a key molecule in the response of cancer cells to ST61 via its phosphorylation by p38 MAPK. The main mechanism underlying ST61's anti-cancer activity was found to involve oxidative stress, as scavenging of ST61-induced reactive oxygen species by N-acetyl-cysteine led to the abrogation of the compound's cytotoxic effect. - Source: PubMed
Publication date: 2026/05/06
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