ACP2 ELISA kit
- Known as:
- ACP2 Enzyme-linked immunosorbent assay test reagent
- Catalog number:
- DL-ACP2-Mu
- Product Quantity:
- 96T
- Category:
- Elisa Kits
- Supplier:
- WDSTD
- Gene target:
- ACP2 ELISA kit
Related genes to: ACP2 ELISA kit
- Gene:
- ACP2 NIH gene
- Name:
- acid phosphatase 2, lysosomal
- Previous symbol:
- -
- Synonyms:
- LAP
- Chromosome:
- 11p11.2
- Locus Type:
- gene with protein product
- Date approved:
- 1986-01-01
- Date modifiied:
- 2015-08-21
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- - Source: PubMed
Publication date: 2026/04/06
Chen FangZhang JunpengXu YingWang YalinCheng Jian - Tissue acidification is a common feature of hypoxia, inflammation and solid tumor. Acidic pH regulates innate immune response in macrophages by weakening BRD4-containing transcriptional condensates. Yet how disruption of transcriptional condensates leads to gene-specific regulation of immune programs remain unclear. Here, we integrated ATAC-seq, ChIP-seq, and RNA-seq of primary murine macrophages and performed integrative epigenomics analyses to identify transcriptional regulators (TRs) with pH-sensitive regulatory potential and association to BRD4-dependent transcriptional condensates. We determined pH-dependent super-enhancers (SEs) by extended profiles of BRD4 binding and h3K27ac marks. We found RELA, IRF family, and STAT family as candidate TRs enriched at BRD4-associated, pH-sensitive SE regions. RELA and IRF3 preferentially occupied BRD4-associated and pH-sensitive SEs, and displayed markedly reduced binding under acidic conditions, aligning with BRD4 occupancy change. Correspondingly, immune-response genes within BRD4-associated, pH-sensitive SE regions, including , , , and family, were significantly higher expressed at pH 7.4 than at pH 6.5. Together, these results reveal a set of TRs involved in BRD4-associated, pH-sensitive transcriptional condensates that coordinate macrophage gene activation under physiological conditions, providing mechanistic insight into how acidic stress modulates transcriptional condensates and immune responses. - Source: PubMed
Publication date: 2025/10/30
Wang ShengyuanWu ZhongyangZhong ZheZhou XuZang Chongzhi - Mutagenesis of the tandem acyl carrier protein (ACP-ACP) domains in the non-reducing polyketide synthase Men2 revealed their distinct roles in menisporopsin A biosynthesis. ACP is essential for multiple esterifications and cyclolactonisation, whilst ACP assembles the aromatic subunits of menisporopsin A. These findings provide a foundation for engineering macrocyclic polylactone compounds. - Source: PubMed
Publication date: 2025/10/07
Deelee ThanakornWattana-Amorn Pakorn - Systemic delivery of adeno-associated virus serotype 9 (AAV9) to the central nervous system (CNS) is insufficient due to hindrance from the tight junctions of the blood-brain barrier (BBB). While peptide-display-based AAV engineering has advanced CNS-targeting capsid development, traditional strategies inserting or substituting a 7-mer peptide remain limited by low success rates and scarcity of efficient variants. To address these issues, we developed the Multiple Capsid Mutation Strategies (MCMS) library, which enhanced sequence diversity by incorporating random peptide insertions flanked by AAV9 or variant-derived residues and peptide substitutions within the VR-VIII of the AAV9 capsid protein. Following capsid selection in mice, the leading AAV variant BRC06 was identified and validated across different mouse strains. BRC06 exhibited approximately 1.9-fold higher brain transgene expression than AAV.PHP.eB in C57BL/6J mice. In BALB/c mice, BRC06 achieved a 1,482-fold brain enhancement with a 92-fold liver reduction relative to AAV9. Sequence analysis revealed that BRC06 was derived from the MCMS library's substitution strategies. Additionally, host factor screening revealed AAVR-dependent entry with accessory factors like contributing to BRC06 transduction. Our results demonstrate that the MCMS library enables efficient selection of AAV capsids with improved BBB penetration, CNS tropism, and reduced liver targeting in mice. - Source: PubMed
Publication date: 2025/06/25
Song QingkaiWu JiameiZhang QingfengWu ShufangLuo XinXu MengmengXu YinxiaWang GangYu HangChen HuiLu ZhikeMa Lijia - Lactacystin is an irreversible proteasome inhibitor isolated from Streptomyces lactacystinicus. Despite its importance for its biological activity, the biosynthesis of lactacystin remains unknown. In this study, we identified the lactacystin biosynthetic gene cluster by gene disruption and heterologous expression experiments. We also examined the functions of the genes encoding a PKS/NRPS hybrid protein (LctA), NRPS (LctB), ketosynthase-like cyclase (LctC), cytochrome P450 (LctD), MbtH-like protein (LctE), and formyltransferase (LctF) by in vivo and in vitro experiments. In particular, we demonstrated that LctF directly transferred the formyl group of 10-N-formyl tetrahydrofolate to CoA. The formyl group of formyl-CoA was then transferred to ACP1 by LctA_AT1 to form formyl-ACP1. This is the first example of an AT domain recognizing a formyl group. The formyl group is perhaps transferred to methylmalonate tethered on LctA_ACP2 to yield methylmalonyl-semialdehyde-ACP2. Then, it would be condensed with leucine bound to PCP in LctB by the C domain in LctA. Using a mimic compound, we confirmed that LctC catalyzed the formation of the cyclic α,α-disubstituted amino acid structure with concomitant release of the product from PCP. Thus, we figured out the overall biosynthesis of lactacystin including a novel role of a formyl group in a secondary metabolite. - Source: PubMed
Publication date: 2025/01/13
Tsunoda TakeshiFurumura ShunkichiYamazaki HarukaMaruyama ChitoseHamano YoshimitsuOgasawara YasushiDairi Tohru