Hsp25 Polyclonal Antibody, PE
- Known as:
- Hsp25 Polyclonal Antibody, PE
- Catalog number:
- ASASPA-801PEF
- Product Quantity:
- 200 µg
- Category:
- -
- Supplier:
- Other suppliers
- Gene target:
- Hsp25 Polyclonal Antibody
Related genes to: Hsp25 Polyclonal Antibody, PE
- 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, PE
Related articles to: Hsp25 Polyclonal Antibody, PE
- 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
Kecskeméti AndrásMolvarec Attila - In summer, bovine fertility may be reduced by increased ambient temperatures which may adversely affect the developmental competence of oocytes. This study aimed to determine how in vivo melatonin treatment affected blastocyst development rates and expression profiles of genes involved in oocyte and blastocyst development in indigenous cows during summer. The non-lactating indigenous Sahiwal cows were divided into treatment (n = 25) and control (n = 19) groups. On Day 0, the treatment group received melatonin @ 18 mg/50 kg body weight, while the control group received 4 mL placebo (corn oil) intramuscularly. All cows were subjected to ovum pickup on Day 4 for blastocyst development in vitro. Results showed that the treatment group had a higher (P < 0.04) blastocyst development rate (38.41 vs. 25.29%) than the control group. Melatonin improved mRNA expression levels of SOD2, HSPB1, BCL2, MT2 and STAR in oocytes, cumulus cells, COCs (immature and mature), and blastocysts, while reducing BAX expression levels compared to the control group. In addition, mRNA expression of ADAMTS remained comparable between the treated and control groups. In conclusion, in vivo administration of melatonin enhanced the antioxidant, anti-apoptotic and steroidogenic effects of oocytes and blastocysts in indigenous cattle during summer, which in turn increased blastocyst development rate and oocyte developmental competence. - Source: PubMed
Publication date: 2026/06/15
Solanki AnupamaPandey Anand KumarJangra HiteshSaini PradeepKumar SandeepKaushik RamakantJoshi Vinay GaneshraoKumar RajeshKognole Satish - 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