HSPA1L Mouse Monoclonal Antibody
- Known as:
- HSPA1L Mouse Monoclonal Antibody
- Catalog number:
- BIN-003305-M02
- Product Quantity:
- 0.1mg
- Category:
- -
- Supplier:
- Zyagen
- Gene target:
- HSPA1L Mouse Monoclonal Antibody
Related genes to: HSPA1L Mouse Monoclonal Antibody
- Gene:
- HSPA1L NIH gene
- Name:
- heat shock protein family A (Hsp70) member 1 like
- Previous symbol:
- -
- Synonyms:
- HSP70-HOM, hum70t
- Chromosome:
- 6p21.33
- Locus Type:
- gene with protein product
- Date approved:
- 1989-05-12
- Date modifiied:
- 2016-10-05
Related products to: HSPA1L Mouse Monoclonal Antibody
Related articles to: HSPA1L Mouse Monoclonal Antibody
- Diabetic nephropathy (DN) is the most common complication of diabetes, with immune-mediated inflammation playing a significant role in its pathophysiology. The complement system, a key proinflammatory factor, is implicated in DN. This study was aimed at identifying diagnostic biomarkers related to the complement system in DN using bioinformatics methods. We analyzed three datasets (GSE96804, GSE104948, and GSE1009) from public databases, employing differential expression analysis and machine learning to identify complement system-related genes (CSRGs) as potential biomarkers. A diagnostic nomogram was constructed based on these genes, and immune microenvironment differences between the DN and control groups were explored. Gene interaction networks, enrichment analysis, and drug predictions were also conducted. Mendelian randomization (MR) was used to examine the causal links between identified biomarkers and DN. Our analysis identified five biomarkers (CKB, ANXA1, HSPA1L, CYP27B1, and XYLT1) associated with DN. A diagnostic nomogram based on these biomarkers showed high accuracy (model correction slope close to 1 and AUC close to 1). Immune infiltration analysis revealed significant differences in immune cell subsets between the DN and control groups. Gene set variation analysis (GSVA) indicated that the oxidative phosphorylation (OXPHOS) pathway was activated in CKB, HSPA1L, CYP27B1, and XYLT1 while inhibited in ANXA1. MR confirmed HSPA1L as a risk factor for DN (OR = 1.625, 95% CI: 1.272-2.076, p = 9.96e - 05). In conclusion, these five CSRGs may play significant roles in DN progression, providing a foundation for further research into DN pathogenesis and potential molecular markers for clinical diagnosis. - Source: PubMed
Wei LifangLi YeLu YuhuiXu MinminYu YueLi LijieLin MinFan LifeiCai Jing - Alzheimer's disease (AD) is a progressive disorder characterized by cognitive decline. Physical exercise and audiovisual stimulation have gained increasing concern for their potential to mitigate AD pathology. However, the therapeutic advantages of combining these interventions and the precise molecular mechanisms underlying these strategies need further demonstration. - Source: PubMed
Publication date: 2026/05/29
Jia JunXie GuominZheng WuXu ChunshuangXia YuxinHu QiaoxiaXiang BinbinZhou XinkaiChen AnqiChen XiaopingWang QinwenZhou YingsongXu Shujun - Photoaging is an extrinsic skin aging process caused by chronic ultraviolet (UV) radiation. A core pathological feature of photoaging is excessive oxidative stress, which can further induce ferroptosis. The HSP70 family plays a critical role in this stress response by protecting the key antioxidant enzyme GPX4. In this study, we established UV-induced photoaging models in cultured cells and 3D skin organoids. UPLC-MS/MS analysis of Chenpi transdermal permeate (prepared by in vitro transdermal penetration of Chenpi extract through mouse skin) identified hesperidin as the primary bioactive compound of Chenpi (dried peel of the plant Blanco after the aging process). The efficacy of hesperidin was validated in human keratinocytes (HaCaTs), fibroblasts (HSFs), and skin organoids. Mechanistically, transcriptomic and metabolomics analysis indicated that ferroptosis is a key pathway through which hesperidin ameliorates photoaging. Limited proteolysis mass spectrometry (LiP-MS), transcriptomics, and molecular dynamics simulation results demonstrated that hesperidin directly binds to the molecular chaperone HSPA1L. By upregulating HSPA1L expression, hesperidin enhanced the stability of GPX4 and suppressed UV-triggered ferroptosis. Our findings identify the HSPA1L/GPX4 axis as a critical redox regulatory pathway targeted by hesperidin, providing a mechanistic foundation for anti-photoaging therapies. - Source: PubMed
Publication date: 2026/04/14
Guo XiaoyuWu MengyaoLi YunxingHe JianlangMa YongjieSu TaizhiLi ChangzhengWang Jian - (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 heat shock protein 70 (Hsp70) family is essential for maintaining protein homeostasis and mediating responses to environmental stresses; however, comprehensive characterizations of this family in the mandarin fish (Siniperca chuatsi) are presently absent. Through comparative genomic analysis, a total of 178 Hsp70 genes were identified across nine vertebrate species (human, mouse, and seven teleost fishes), including 17 unique members within the mandarin fish genome. Phylogenetic and gene structure analyses demonstrated that the mandarin fish Hsp70 family has remained highly conserved throughout teleost evolution, marked by lineage-specific expansions (notably in hspa1, hspa4, hspa8, and hspa12) and selective gene loss (e.g., the absence of hspa2 and hspa6). Specifically, tandem duplication was observed for hspa8.1 and hspa8.2, at the same time, two pairs of syntenic genes (hspa4a/hspa4b and hyou1/hspa8b) were found. Ka/Ks analysis further indicated that this gene family has mainly evolved under purifying selection. Transcriptomic profiling showed that hspa8.1 was constantly expressed across all examined tissues. In addition, under thermal stress and Aeromonas hydrophila infection, Hsp70 genes in mandarin fish exhibited divergent expression patterns: certain members contribute to basal homeostasis (e.g., hspa8.1), whereas others demonstrate specialized responses to heat/cold adaptation (e.g., hspa5) or pathogen infection (e.g., hspa1l). Respectively, these findings together provide a thorough understanding of the composition, evolutionary trajectory, and stress-responsive dynamics of the Hsp70 family, establishing a foundational molecular basis for understanding the environmental adaptation of mandarin fish. - Source: PubMed
Publication date: 2026/04/21
Liu YufeiYao XiaoliGao JinhuaIsmaeel HossamChen XiaowuZhao Jinliang