PCBD1 predesign siRNA
- Known as:
- PCBD1 predesign small interfearing RNA
- Catalog number:
- RI13828
- Category:
- -
- Supplier:
- Abgen
- Gene target:
- PCBD1 predesign siRNA
Related genes to: PCBD1 predesign siRNA
- Gene:
- PCBD1 NIH gene
- Name:
- pterin-4 alpha-carbinolamine dehydratase 1
- Previous symbol:
- DCOH, PCBD
- Synonyms:
- PCD
- Chromosome:
- 10q22.1
- Locus Type:
- gene with protein product
- Date approved:
- 1993-06-08
- Date modifiied:
- 2016-10-05
Related products to: PCBD1 predesign siRNA
3 Target siRNA's & 1 negative control duplex. Standard purity, 2 nmol each4-alpha-hydroxy-tetrahydropterin dehydratase,Bos taurus,Bovine,DCoH,Dimerization cofactor of hepatocyte nuclear factor 1-alpha,Dimerization cofactor of HNF1,PCBD1,PCD,Phenylalanine hydroxylase-stimula4-alpha-hydroxy-tetrahydropterin dehydratase,cDcoH,Chicken,DCoH,DCOH,Dimerization cofactor of hepatocyte nuclear factor 1-alpha,Dimerization cofactor of HNF1,Gallus gallus,PCBD,PCBD1,PCD,Phenylalanine4-alpha-hydroxy-tetrahydropterin dehydratase,DCoH,DCOH,Dimerization cofactor of hepatocyte nuclear factor 1-alpha,Dimerization cofactor of HNF1,Homo sapiens,Human,PCBD,PCBD1,PCD,Phenylalanine hydroxyl4-alpha-hydroxy-tetrahydropterin dehydratase,DCoH,Dcoh,Dimerization cofactor of hepatocyte nuclear factor 1-alpha,Dimerization cofactor of HNF1,Mouse,Mus musculus,Pcbd,Pcbd1,PCD,Phenylalanine hydroxyl4-alpha-hydroxy-tetrahydropterin dehydratase,DCoH,Dcoh,Dimerization cofactor of hepatocyte nuclear factor 1-alpha,Dimerization cofactor of HNF1,Pcbd,Pcbd1,PCD,Phenylalanine hydroxylase-stimulating pro5x SiRNA Buffer5x SiRNA Buffer5x SiRNA BufferA1BG predesign siRNAA1BG predesign siRNAAAAS predesign siRNAAAAS predesign siRNAAADAC predesign siRNAAADAC predesign siRNA Related articles to: PCBD1 predesign siRNA
- Moderate-to-vigorous physical activity (MVPA) lowers the risk of type 2 diabetes (T2D). Identifying protein modules that mediate this association may help dissect these biological underpinnings, but they remain incompletely characterized. - Source: PubMed
Publication date: 2026/09/09
Wang ZhenqianSu Chen-YangLu JiawenHasebe MasashiMejia-Garcia AlejandroTsao Hsuan MeganHu JingyiLu TianyuanZhou Sirui - Gastric adenocarcinoma (STAD) exhibits extensive intratumoral heterogeneity that contributes to tumor progression and therapeutic resistance. In this study, we integrated single-cell RNA sequencing and bulk transcriptomic analyses to characterize malignant epithelial subtypes in STAD. Among seven identified tumor subtypes, the OLFM4-associated C3 subtype exhibited enriched palmitoylation-related signatures and altered metabolic activities, particularly glycolysis-related pathways. Functional enrichment analyses further supported the enrichment of multiple energy metabolism pathways. To evaluate the association between OLFM4 and metabolic regulation, recombinant OLFM4 treatment and siRNA-mediated OLFM4 knockdown were performed in gastric cancer cell lines. OLFM4 upregulation increased the expression of ZDHHC2 and GLUT1, accompanied by enhanced glucose uptake and elevated ATP production, whereas OLFM4 silencing reduced ZDHHC2 and GLUT1 expression. In addition, a prognostic risk model derived from C3 subtype-associated genes (MUC16, RALA, and PCBD1) effectively stratified STAD patients and was associated with immune checkpoint expression and immune infiltration. Collectively, our findings identify an OLFM4-associated gastric cancer cell state with palmitoylation-related signatures and altered metabolic activities, highlighting its potential relevance to metabolic heterogeneity in gastric adenocarcinoma. - Source: PubMed
Publication date: 2026/06/15
Chen GongWei WeipingLi DanHan ShanshanSchäfer MichaelHuang Xiaoyan - The production of complex biologics in Chinese hamster ovary (CHO) cells is constrained by the lack of selection systems capable of coordinating multiple transgenes. Conventional single-marker systems have low saturable thresholds that limit enrichment efficiency, while multi-auxotrophic platforms often impose metabolic burdens. Here, we present a rationally designed tyrosine-auxotrophic system that overcomes these limitations by establishing a high-threshold cooperative selection mechanism. This is achieved through the reconstruction of an essential pathway comprising pterin-4α carbinolamine dehydratase 1 (PCBD1), phenylalanine hydroxylase (PAH), and quinoid dihydropteridine reductase (QDPR). We generated a triple-knockout CHO host via CRISPR/Cas9, wherein survival under tyrosine deprivation became strictly dependent on the balanced co-expression of all three rescue genes. This architecture creates a selection pressure that is not saturable by any single gene, enabling efficient co-enrichment. Applied to monoclonal antibody (mAb) production, the system enriched triple-positive populations to 97.49%, resulting in significantly enhanced homogeneity and coordinated upregulation of antibody chain expression. Optimized pools achieved titers of 0.35 g/L in fed-batch and 1.60 g/L in perfusion cultures without tyrosine feeding. Consequently, pathway reconstitution rewired central metabolism, reducing byproducts and enhancing biosynthesis. This antibiotic-free multi-marker platform establishes a new paradigm for stringent multigene co-expression, advancing CHO cell engineering for next-generation biologics. - Source: PubMed
Publication date: 2026/03/09
Cao LeiNa DaoyuanCheng JunZhao LiangYe QianTan Wen-Song - Understanding the role of plasma proteins in the pathophysiology of epilepsy is crucial for uncovering novel biological mechanisms and therapeutic targets. Mendelian randomization (MR) provides a valuable tool for dissecting potentially causal associations between circulating proteins and disease risk. This study aimed to systematically assess potential causal relationships between the plasma proteome and epilepsy. - Source: PubMed
Publication date: 2025/10/30
Fu JingfengWu WeiShen Shangren - CHO cells dominate monoclonal antibody (mAb) production in fed-batch biomanufacturing, where tyrosine supply is limited by low solubility in neutral media and the complexities of alkaline tyrosine feeds. Existing studies confirm overexpressing pterin-4α-carbinolamine dehydratase 1 (PCBD1) and phenylalanine hydroxylase (PAH) restores tyrosine prototrophy and matches non-engineered cells' production in tyrosine-supplemented cultures. However, these studies focus on enzyme regulation without resolving feeding-phase supply challenges in high-density scenarios. To address this, this study verified that recombinant CHO (rCHO) cells rely strongly on exogenous tyrosine for growth and production. Multi-level expression analysis further confirmed low PCBD1/PAH levels restrict endogenous tyrosine synthesis, and identified quinoid dihydropteridine reductase (QDPR)-a key tetrahydrobiopterin (BH4) regeneration enzyme-as a previously unrecognized bottleneck, particularly in tyrosine-limited conditions. By co-overexpressing QDPR in high PCBD1/PAHexpressing cells to remodel the tyrosine biosynthesis pathway, a novel fed-batch strategy was established: basal medium with 3.0 mM tyrosine and tyrosine-free singlefeeding medium. Results showed this strategy, effective in high-density fed-batch settings, enabled rCHO cells to reach a final mAb titer of 4.24 g/L, representing a 32.50% increase compared to cells overexpressing only PCBD1 and PAH, and a 10.70 % increase compared to the conventional strategy. In summary, the strategy offers a simplified nutrient alternative by eliminating alkaline tyrosine feeds, highlighting holistic metabolic pathway optimization's importance in biomanufacturing and targeted value for high-density, tyrosine-limited CHO cell-based mAb production. - Source: PubMed
Publication date: 2025/10/10
Cao LeiZhao LiangYe QianTan Wen-Song