Hsp90b1
- Known as:
- Hsp90b1
- Catalog number:
- 064015A
- Product Quantity:
- 250ul
- Category:
- -
- Supplier:
- ABM
- Gene target:
- Hsp90b1
Related genes to: Hsp90b1
- Gene:
- HSP90B1 NIH gene
- Name:
- heat shock protein 90 beta family member 1
- Previous symbol:
- TRA1
- Synonyms:
- GP96, GRP94
- Chromosome:
- 12q23.3
- Locus Type:
- gene with protein product
- Date approved:
- 1991-07-03
- Date modifiied:
- 2016-10-11
Related products to: Hsp90b1
anti-HSP90B1 GRP94anti-HSP90B1 GRP94 (2H3)anti-HSP90B1 GRP94 (2H3) type: Primary antibodies host: Mouseanti-HSP90B1 GRP94 (C-Terminus)Anti-HSP90B1 (2H3), Mouse Monoclonal to HSP90B1, Isotype IgG2a, Host Mouseanti-HSP90B1 / GRP94anti-HSP90B1 / GRP94anti-HSP90B1 / GRP94 (2H3)anti-HSP90B1 / GRP94 (C-Terminus)anti-HSP90B1 / GRP94 (Internal)Anti-HSP90B1, Goat Polyclonal to HSP90B1, Isotype , Host GoatAnti-HSP90B1, Rabbit Polyclonal to HSP90B1, Isotype , Host Rabbitanti-HSP90B1, Rabbit polyclonal to HSP90B1, Isotype IgG, Host Rabbitanti-HSP90B1, Rabbit polyclonal to HSP90B1, Isotype IgG, Host RabbitAnti-Human mouse rat HSP90 beta (hsp90B1) peptide IgG, aff pure Related articles to: Hsp90b1
- Signal Regulatory Protein Alpha (SIRPA) functions as an inhibitory receptor to suppress phagocytosis of macrophages and promote tumor immune evasion. Recent studies revealed that SIRPA deficiency reprogrammed tumor-associated macrophages toward an antitumor phenotype, and SIRPA functioned independently of CD47. However, the exact role and signaling pathways by which SIRPA macrophages were induced and exerted their functions in glioblastoma have not been fully elucidated. - Source: PubMed
Publication date: 2026/05/11
Yin NanhengZhang ZhichengXia FeiyuZhang XiaopeiLi ZengyangZhong TaoPan JiaxinLiang GengHuang DelongDai XiaoxiaoDong Jun - Acute pancreatitis is a systemic inflammatory response that has the potential to affect numerous organs, resulting in persistent multiorgan failure and necrosis of the pancreas. According to previous studies, the development and occurrence of acute pancreatitis are linked to ferroptosis and immune responses. We assessed and validated the function of ferroptosis-related genes in acute pancreatitis and their association with inferred immune infiltration using bioinformatic analyses. Ferroptosis-related differentially expressed genes were identified using the Gene Expression Omnibus databases (GSE109227, GSE121038, and GSE183158) in conjunction with our transcriptome sequencing data. The involvement of ferroptosis-related differentially expressed genes was clarified through gene ontology, differential gene correlation, and gene set enrichment analysis. CIBERSORT analysis was used to evaluate and internally validate the immune microenvironment in acute pancreatitis. Comparative analysis of sequencing data from the pancreatic and liver tissues revealed 13 ferroptosis-related differentially expressed genes in acute pancreatitis. Gene ontology analysis primarily identified enrichment for iron ions, protein phosphatase, and actin filament binding. Gene set enrichment analysis predominantly highlighted the interleukin-18 and interleukin-23 pathways. Hub genes in the protein-protein interaction network included Egfr, Fads1, Hsp90b1, Krt18, Lcn2, Myh9, Pdia6, and Sqle. We identified 80 miRNAs, 67 transcription factors, and 24 potential drugs or molecular compounds associated with acute pancreatitis pathology. Quantitative reverse transcription polymerase chain reaction performed on caerulein-induced acute pancreatitis mouse models confirmed significant downregulation of Fads1, Hsp90b1, Pdia6, Sqle, and Cisd1 mRNA levels while showing significant upregulation of Osbpl9, Myh9, and Zfp36 mRNA levels. These findings suggested that these genes may represent candidate genes associated with AP and ferroptosis. Thirteen ferroptosis-related differentially expressed genes were discovered within the framework of acute pancreatitis, and their association with immune cell infiltration was studied. Future investigations should explore the possibility of Fads1, Hsp90b1, Pdia6, Sqle, Cisd1, Osbpl9, Myh9, and Zfp36 as novel therapeutic targets. - Source: PubMed
Publication date: 2026/04/29
Liu HuiYue MengliChen ShangsiLiu Pi - (pea aphid) is a major pest of Fabaceae (legume) crops, causing direct feeding damage and transmitting plant diseases. Conventional control relies on broad-spectrum insecticides and natural enemies, both of which can harm non-target organisms and ecosystems. RNA interference (RNAi) offers a promising, species-specific alternative by silencing essential genes double-stranded RNA (dsRNA). This study targeted two heat shock protein Genes-Heat Shock 70 kDa Protein 1-Like () and Heat Shock Protein 90 kDa beta (Grp94) Member 1 ()-key players in protein folding, quality control, and stress response within the Unfolded Protein Response () pathway. These chaperones stabilize proteins, assist in folding newly synthesized polypeptides, and target misfolded proteins for degradation. Silencing these genes was hypothesized to cause accumulation of misfolded proteins, triggering Endoplasmic Reticulum (ER) stress, overload, and ultimately apoptosis, leading to aphid mortality. Total RNA was extracted from adult pea aphids, reverse-transcribed to cDNA, and used to synthesize gene-specific dsRNAs for and . These dsRNAs were encapsulated in Branched-Amphiphilic Peptide Capsules (BAPCs) and delivered orally at concentrations of 10 ng/μL and 100 ng/μL artificial diet feeding. Survival was monitored every 6 hours for 48 hours on dsRNA diet, followed by transfer to healthy faba bean leaves. Preliminary studies indicated positive correlations between gene knockdown and elevated mortality. Results demonstrated significantly reduced survival in treated groups compared to controls at both concentrations (Kaplan-Meier survival analysis, log-rank p<0.001), supporting the induction of apoptosis. This approach highlights the potential of -targeted RNAi for eco-friendly, targeted pest control. - Source: PubMed
Publication date: 2026/01/06
Davies GriffinBalthazor James - The developmental pace and sex ratio of preimplantation embryos have major implications for pregnancy outcome and herd replacement. We asked whether selecting embryos that develop faster preferentially captures distinct molecular and metabolic states and inadvertently affects the sex ratio in bovine in vitro produced (IVP) blastocysts. Hatching-stage blastocysts (pool of blastocysts undergoing and having completed the hatching process) developed on Day 7 and Day 8 of in vitro culture (IVC) were analyzed by RNA-sequencing, alongside assessments of lipid content, mitochondrial activity, and reactive oxygen species (ROS). Sexing was performed via Y-chromosome multiplex PCR, and candidate genes were quantified by qPCR in individually sexed hatching-stage embryos. RNA-sequencing identified 192 differentially expressed genes. Notably, significantly higher expression of pregnancy recognition factors (IFNT2, IFNT3) and the trophoblast marker TKDP1, along with glycolytic, lipid transport genes was observed on Day 8. In contrast, hatching-stage blastocysts from Day 7 displayed upregulation of oxidative phosphorylation genes. Mitochondrial activity and ROS levels were comparable between groups, but Day 7 embryos contained significantly more lipids. Interestingly, sexing analysis revealed a significant male bias among these blastocysts on Day 7 (66.7%) and Day 8 (58.5%). Candidate gene expression analysis revealed sexually dimorphic regulation of UQCRC2 and developmental day-dependent regulation of ENO1, UQCRC2, HSP90B1, and APOA1. Collectively, these findings indicate that hatching-stage blastocysts developed on Day 7 and Day 8 of IVC represent distinct physiological states and demonstrate that selecting embryos for rapid development can inadvertently skew sex ratios and molecular profiles in bovine IVP embryos. - Source: PubMed
Publication date: 2026/04/24
Baddela Vijay SimhaFersterer TheresPöhland Ralfde Andrade Melo-Sterza FabianaLudwig Carolin L MBecker DoreenKühn ChristaVanselow Jens - Heat shock protein Gp96 (also known as Grp94 or endoplasmin) is the endoplasmic reticulum (ER)-resident paralog of the Hsp90 family and a central regulator of ER proteostasis and immune receptor biogenesis in mammalian cells. By controlling the folding, quality control, and trafficking of a restricted yet functionally critical set of client proteins, including Toll-like receptors, integrins, and immunoglobulins, Gp96 plays an essential role in innate immunity and inflammatory signaling. In the context of malaria, accumulating evidence suggests that host-derived Gp96 is involved in immune activation and disease severity, notably through its extracellular release under conditions of cellular stress, where it functions as a danger-associated molecular pattern (DAMP). Elevated circulating Gp96 levels have been associated with severe malaria phenotypes, supporting its potential value as a biomarker of host stress and immune dysregulation. In parallel, expresses its own ER-resident Hsp90 homolog, PfGp96, which retains the conserved domain architecture of Hsp90 while exhibiting parasite-specific adaptations, including divergence in ER retention motifs. However, the biological functions, client repertoire, and essentiality of PfGp96 remain poorly defined, and direct evidence supporting its validation as a drug target is currently limited. This review critically synthesizes current knowledge on Gp96 and PfGp96, emphasizing experimentally validated functions, host-parasite interface dynamics, and unresolved knowledge gaps. We discuss the opportunities and challenges of targeting Gp96-related pathways for biomarker development and therapeutic intervention in malaria, while outlining key priorities for future functional and translational research. - Source: PubMed
Publication date: 2026/03/26
Djoumoi DjibabaDiouara Abou Abdallah MalickDiop MamadouNguer Cheikh MomarMbengue BabacarThiam Fatou