Recombinant Human Biphenyl Hydrolase-Like BPHL
- Known as:
- Recombinant Human Biphenyl Hydrolase-Like BPHL
- Catalog number:
- enz-055
- Product Quantity:
- 5
- Category:
- -
- Supplier:
- Prospecbio
- Gene target:
- Recombinant Human Biphenyl Hydrolase-Like BPHL
Related genes to: Recombinant Human Biphenyl Hydrolase-Like BPHL
- Gene:
- BPHL NIH gene
- Name:
- biphenyl hydrolase like
- Previous symbol:
- MCNAA
- Synonyms:
- Bph-rp, VACVase
- Chromosome:
- 6p25.2
- Locus Type:
- gene with protein product
- Date approved:
- 1997-10-17
- Date modifiied:
- 2016-10-05
Related products to: Recombinant Human Biphenyl Hydrolase-Like BPHL
Related articles to: Recombinant Human Biphenyl Hydrolase-Like BPHL
- As a relatively common respiratory disease, chronic obstructive pulmonary disease (COPD) has a high incidence and mortality rate. Mitochondrial dysfunction has been implicated in COPD pathogenesis, but the causal genes and underlying molecular mechanisms remain unclear. - Source: PubMed
Publication date: 2026/01/17
Hong ErMao JiaKe ZhichengWu Yang - Triple-negative breast cancer (TNBC) poses a formidable clinical challenge due to its aggressive behavior and limited therapeutic avenues. Here, we delineate a novel pathway wherein BPHL governs R-loop homeostasis to sustain cancer stem cell (CSC) stemness in TNBC. Through single-cell RNA sequencing (scRNA-seq) of 26 breast cancer samples, we identified low R-loop scores as a defining feature of TNBC CSCs, marked by elevated chromosomal instability and stemness signatures. Extensive cohort analysis further confirmed that this low R-loop profile significantly correlates with poor patient prognosis and advanced tumor staging. Bioinformatics interrogation pinpointed BPHL as the pivotal regulator, a finding corroborated by the strong positive correlation between BPHL expression and lactylation markers in clinical specimens. Functional studies across multiple TNBC models revealed that BPHL overexpression expanded the CSC compartment, bolstered sphere formation, and accelerated tumor growth in vitro and in vivo. Consistent with the low R-loop phenotype, genes enriched in low R-loop TNBC cells and CSCs were linked to cell cycle progression, DNA replication/checkpoint control, and p53-associated pathways.Mechanistically, BPHL engages POLR2A, curtailing its lactylation while augmenting BARD1-mediated ubiquitination to resolve R-loops and enable β-catenin nuclear translocation, thereby perpetuating Wnt signaling. Beyond intrinsic tumor programs, low R-loop states were also associated with enhanced intercellular communication (notably MIF/MK signaling) and elevated immune checkpoint gene expression (e.g., PDCD1, CTLA4, TIGIT, LAG3). Intriguingly, in vivo BPHL depletion curbed tumorigenesis-an effect partially mitigated by RNase H overexpression but reinstated by β-catenin blockade. These insights position BPHL as a compelling target for eradicating TNBC CSCs. - Source: PubMed
Publication date: 2026/02/27
Yuan QuanZhang HanZhang NaiqianQian YaoHong ZhipengWan XueYe RongjieChen DeboFeng XiaolingYu GeNiu Ming - While cytochrome P450 enzymes and UDP-glucuronosyltransferases play predominant roles in drug metabolism, hydrolases are emerging as key players in the metabolism of both small molecules and antibody-drug conjugates or peptide-oligonucleotide conjugates. Despite their importance, the protein levels of hydrolases across tissues and their inter-individual variability remain poorly understood. Although targeted proteomics can provide high selectivity and precision in quantifying small numbers of proteins, total protein approach (TPA)-based proteomics is emerging as a superior approach for multiplexed quantification of proteins. We performed a head-to-head comparison of targeted proteomics and TPA-based proteomics for quantifying 12 clinically relevant hydrolases in human liver and intestinal S9 fractions ( = 5 each). TPA-based global proteomics offered higher precision (coefficient of variation <20%), comparable sensitivity, along with its inherent advantage of a greater protein coverage than targeted proteomics. TPA data revealed the following order of protein abundance for target proteins: CES1> EPHX1 > CES2 > BPHL > PON3 > PON1 ∼ AADAC > CTSA > DPP4 in the liver and CES2 > ADA > DPEP1 ∼ AADAC ∼ EPHX1 > ALPI > DPP4 > CTSA > BPHL ∼ CES1 in the intestine. This study highlights the utility of TPA-based global proteomics for characterizing differential tissue abundance of hydrolases and their inter-individual variability. - Source: PubMed
Publication date: 2025/10/13
Singh Dilip KumarAhire DeepakJones Robert SKikuchi RyotaMa BinTian YuWang TingZubair FaizanHeyward ScottKhojasteh S CyrusMurray Bernard PSmith Bill JStresser David MTaub MitchellZientek MichaelPrasad Bhagwat - Despite comprehensive studies on P450 enzymes, studies on non-P450 enzymes are rather limited and the mechanism by which the non-P450 enzymes participate in the drug metabolism is not fully understood. Thus, we aimed to analyze the interactions between ester-containing FDA-approved drugs and three non-P450 drug-metabolizing enzymes (Bche, Bphl, and Ces1), and to investigate the structural features of their active sites using computational methods. The interaction between 920 FDA approved drugs that contain a carbonyl group (ester), and three esterase enzymes, Bche, Bphl, and Ces1 were assessed by means of computational methods. Data show that Bche and Ces1 accommodates more drugs than Bphl with 478 and 341 drugs that have docking score/molecular weight ratio greater than 0.15 respectively. In addition, there are distinct structural differences between drug binding sites of three enzymes. Ces1 has multiple solvent channels that reach the binding cavity while Bche does not have any distinct solvent channel. The volume of substrate binding site of Bche's is 1256.75 Å which is the greatest among others. MD simulations show that Gln-119, Asp-70, and Pro-285 contribute most to the drug binding in Bche enzyme. In addition, His-255, Ser-122, and Asp-155 residues in Bphl and Phe-80, Leu-367 and Asp-286 residues in Ces1 are important for drug binding. Molecular dynamic simulation and docking analyses revealed that ligand binding is driven by both electrostatic hotspots and hydrophobic packing, with stronger ligands like Venetoclax and Revefencin engaging more persistent hydrogen bonds and hydrophobic contacts, highlighting key residues for structure-based drug design. This study provides new insights into the structural and functional features of non-P450 enzymes, offering potential implication for drug metabolism. - Source: PubMed
Publication date: 2025/08/22
Yildiz Muslum - Understanding the sublethal effects of insecticides on non-target insects is essential for integrated pest management (IPM). This study aimed to evaluate the differentially expressed genes (DEGs) in the testes of adults exposed to pyriproxyfen during the larval stage. Larvae (0-12 h) were fed eggs treated with pyriproxyfen (50 and 100 mg a.i. L) for 10 days. After this exposure, the larvae were fed untreated eggs until pupation. The testes from the adults were extracted for RNA extraction, library construction, and sequencing. The reads were de novo assembled, and the genes annotated based on their ORF homology. A total of 46 DEGs were identified for the 50 mg a.i. L vs. control, 47 DEGs for the 100 mg a.i. L vs. control, and 64 DEGs for 50 mg vs. 100 mg a.i. L treatments. To validate the DEGs through RT-qPCR, the genes BPHL, Large2, MLX, and Talin-1 were selected. The results indicate that the exposure of larvae to pyriproxyfen could alter the gene expression and lead to delayed effects in adults. This study provided a novel approach for assessing the sublethal effects of pyriproxyfen and contributed valuable information to enhance IPM strategies. - Source: PubMed
Publication date: 2025/05/28
Tomacheski Jefferson FogaçaGarcia Ana Silvia GimenesNakajima Rafael TakahiroPatroni Fábio Malta de SáScudeler Elton LuizNóbrega Rafael HenriqueSantos Daniela Carvalho Dos