HSPA2 Mouse Monoclonal Antibody
- Known as:
- HSPA2 Mouse Monoclonal Antibody
- Catalog number:
- BIN-003306-M06
- Product Quantity:
- 0.1mg
- Category:
- -
- Supplier:
- Zyagen
- Gene target:
- HSPA2 Mouse Monoclonal Antibody
Ask about this productRelated genes to: HSPA2 Mouse Monoclonal Antibody
- Gene:
- HSPA2 NIH gene
- Name:
- heat shock protein family A (Hsp70) member 2
- Previous symbol:
- -
- Synonyms:
- -
- Chromosome:
- 14q23.3
- Locus Type:
- gene with protein product
- Date approved:
- 2001-06-22
- Date modifiied:
- 2016-10-05
Related products to: HSPA2 Mouse Monoclonal Antibody
Related articles to: HSPA2 Mouse Monoclonal Antibody
- The synaptonemal complex (SC) is a highly ordered proteinaceous structure that assembles between homologous chromosomes during the prophase I of meiosis. Conserved as a tripartite architecture across species, the SC plays a central role in chromosome synapsis, meiotic recombination, and faithful chromosome segregation. This review marks the 70th anniversary of the discovery of the synaptonemal complex by Montrose Moses in 1956. In mammals, the SC is composed of eight core (canonical) structural proteins: SYCP1, SYCP2, SYCP3, SYCE1, SYCE2, SYCE3, SIX6OS1, and TEX12. The archetypal SC consists of two lateral elements (SYCP2 and SYCP3), a central element (SYCE1/2/3, SIX6OS1, and TEX12), and numerous transverse filaments (SYCP1). A shared structural feature of SC components is the presence of coiled-coil domains. Although the tripartite organization of the SC is evolutionarily conserved, its constituent proteins exhibit little to no sequence homology across species. In addition to these core components, a number of proteins, including HORMAD1, HORMAD2, TRIP13, SKP1, CDCA5 (Sororin), UBE2I (UBC9), SYCP2L, HSPA2, PSMA8, and FKBP6, associate with the SC. Beyond serving as a structural scaffold essential for homolog synapsis, SC proteins interact with key recombination factors such as DMC1, RAD51, and TEX11, thereby regulating recombination progression and crossover formation. Genetic, biochemical, and structural analyses of SC components have provided important mechanistic insights into SC assembly and function, as well as their clinical relevance to non-obstructive azoospermia (NOA) and premature ovarian insufficiency (POI) in humans. - Source: PubMed
Publication date: 2026/04/30
Yang FangWang P Jeremy - 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 - The production of type I interferons (IFN-I) induced by viruses is critical for the host to resist viral infection. While emerging studies have implicated heat shock protein A2 (HSPA2) in various diseases, its specific role in antiviral immunity remains elusive. Here, using Hspa2-deficient mice and cellular models, we demonstrate that HSPA2 negatively regulates IFN-I production by targeting TANK-binding kinase 1 (TBK1). Mechanistically, HSPA2 binds to TBK1 and competes with the HECT and RLD domains containing E3 ubiquitin protein ligase 5 (HERC5) for TBK1 binding, thereby abrogating HERC5-dependent K63-linked ubiquitination of TBK1 at lysine 608 (K608), which disrupts the formation of TBK1-associated complexes and suppresses the subsequent dimerization and nuclear translocation of interferon regulatory factor 3 (IRF3), ultimately blocking IFN-I production. This study provides insights into the regulatory network governing innate immune homeostasis and identifies HSPA2 as a potential target for antiviral therapy. - Source: PubMed
Publication date: 2026/04/03
Li ChenglongLi SiruiZhang YihuaLi ManmanHong XiaowuYan Dapeng - Egg weight (EW) is a key trait in both breeding and production for poultry. Although Zi geese demonstrate good egg-laying performance, they have relatively low EW. Identifying candidate genes and pathways associated with EW in geese is essential for enhancing genetic progress. In this study, 260 female Zi geese at 30 weeks of age were monitored individually for egg number (EN) and EW. Thirty geese, showing no significant differences in body weight and EN but significant variation in EW (P < 0.05), were selected and divided into a high egg weight (HEW) group (n = 15) and a low egg weight (LEW) group (n = 15). Egg quality traits were evaluated for both groups. From each group, six geese were randomly selected for serum biochemical profiling and untargeted metabolomics; four of these were further analyzed for transcriptomic data from the liver, ovary, and oviduct magnum. The results showed significant differences in albumen weight, yolk weight, and shell weight between HEW and LEW (P < 0.01). Serum biochemical analysis revealed higher levels of total cholesterol, triglycerides, estradiol, very low-density lipoprotein, and vitellogenin in the HEW group (P < 0.05). Transcriptomic analysis identified 278 differentially expressed genes (DEGs) in the liver, primarily enriched in antigen processing and presentation pathways, with ACACB, FDFT1, and HSPA2 highlighted as candidate genes. In the ovary, 18 DEGs were identified, with RBP1 as the key gene. In the oviduct magnum, 1,605 DEGs were enriched in protein processing in the endoplasmic reticulum, with HSPA8, HSP90AA1, and ST3GAL4 identified as candidate genes. Serum metabolomics revealed metabolites associated with EW, including cholesterol sulfate, l-tryptophan, indoxyl sulfate, and LysoPC(20:5(5Z,8Z,11Z,14Z,17Z)/0:0). Integrated multi-omics analysis identified ACSL5-LysoPC(20:5(5Z,8Z,11Z,14Z,17Z)/0:0) and ACSL5-L-tryptophan as key gene-metabolite pairs potentially regulating EW. These findings provide a theoretical foundation for understanding the genetic mechanisms underlying EW regulation in geese. - Source: PubMed
Publication date: 2026/03/21
Cong KexinLiu YunuoWang HechuanJiang KeYin JiaxinMiao XinyiYang WeiranXiao XiangChen ZhifengLiu Shengjun - Heat stress significantly disrupts physiological and molecular balance in poultry, leading to oxidative damage, inflammatory responses, and metabolic dysregulation. Among emerging solutions, phytogenic adaptogens have shown promise as natural agents that enhance resilience against these environmental challenges. This exploratory study examined the transcriptomic effects of Phytocee™, a proprietary phytogenic formulation, in heat-stressed broilers, alongside in silico predictions of its phytochemical interactions with longevity-associated pathways. Phytocee™ consists of a formulation of adaptogenic medicinal plants. The primary bioactive components contributing to these adaptogenic properties include hydrolyzable tannins, withanolides, and triterpenoids. Comprehensive identification, quantification, and confirmation of these phytochemicals were conducted using liquid chromatography-mass spectrometry (LC-MS), and the formulation's integrity was validated through high-performance liquid chromatography coupled with photodiode-array detection for routine quality assurance. The transcriptomic analysis demonstrated that heat stress led to the upregulation of several vital DNA repair and cell cycle regulatory genes, including FANCF, BRCA1, and EXO1. The supplementation of Phytocee™ resulted in further increases in these genes, reaching a log2 fold change of 1.32 with a significance level of < 0.013. Additionally, resilience markers against oxidative stress such as SOD2, CAT, HSP25, HSPA2, and SOD3 along with metabolic adaptation indicators like IDH3A, ATP6V0D2, RRM2, ME1, FADS2, ALDH1L2, and DHCR7 showed significant enhancement post-treatment. There was also a restoration of several downregulated protective genes, including NFKBIA and BIRC5. DIGEP-Pred 2.0 and pathway enrichment were used in the in-silico analyses, which predicted that the key Phytocee™ phytochemicals interact with FOXO, AMPK, SIRT1, and mTOR network components. Transcriptomic patterns, such as upregulated DNA repair, oxidative resilience, and metabolic genes correlatively overlapped with this prediction. Again, no model validation or functional activation was performed. This exploratory study contributes to a hypothesis-producing framework for these associations to be tested in heat-stressed broilers but has several limitations related to the correlative nature of findings, absence of confirmation at the protein level, or functional assays, such as autophagy or pathway inhibition or direct measures of thermotolerance or production. Thus, confirmatory studies are warranted to test these implied mechanistic associations. - Source: PubMed
Publication date: 2026/03/16
Shamana KEdwin RJaishree S PPrashanth DAboli GDeepak M