PCMT1 antibody (FITC)
- Known as:
- PCMT1 (anti-) (fluorecein)
- Catalog number:
- orb103199
- Product Quantity:
- 100 ug
- Category:
- -
- Supplier:
- Biorb
- Gene target:
- PCMT1 antibody (FITC)
Related genes to: PCMT1 antibody (FITC)
- Gene:
- PCMT1 NIH gene
- Name:
- protein-L-isoaspartate (D-aspartate) O-methyltransferase
- Previous symbol:
- -
- Synonyms:
- -
- Chromosome:
- 6q25.1
- Locus Type:
- gene with protein product
- Date approved:
- 1992-09-11
- Date modifiied:
- 2017-11-27
Related products to: PCMT1 antibody (FITC)
Related articles to: PCMT1 antibody (FITC)
- The C-terminal cyclic imide modification is recognized as a degron by the E3 ligase adapter cereblon (CRBN). Reliable methods to generate and measure this modification on CRBN substrates are essential for studying its biological function. In this chapter, we describe two complementary approaches for producing C-terminal cyclic imide-modified peptides and proteins: sortase-mediated transpeptidation and enzymatic conversion by protein carboxymethyltransferase (PCMT1). Additionally, we present analytical strategies, including a time-resolved Förster resonance energy transfer (TR-FRET) assay for measuring binding of substrates to CRBN in vitro and mass spectrometry methods for confirming cyclic imide formation. Together, these protocols provide practical methods for investigating the chemistry and biology of C-terminal cyclic imides. - Source: PubMed
Zhao ZhenguangFeng Ethan YangXu WenqingWoo Christina M - Neuropsychiatric symptoms in dementia (NPS) are common and among the most troubling aspects of living with dementia, yet their underlying mechanisms remain unclear. Here, we aimed to identify cerebrospinal fluid (CSF) proteins associated with NPS. - Source: PubMed
Publication date: 2026/06/30
Mei ZhenHoward NicholasHarvey Danielle J Fox EdwardSeyfried Nicholas TWingo Thomas SWingo Aliza P - Castrate resistant prostate cancer (CRPC) is often driven by constitutively active androgen receptor and AR splicing variants that become resistant to established hormonal therapy strategies such as enzalutamide. Deubiquitinating enzymes (DUBs) play crucial roles in cancer development, progression, and metastasis by epigenetic modification. Hence, targeting DUBs might prove to be a valid strategy for developing novel anti-cancer therapeutics. Here, we reveal that the deubiquitinating enzyme USP13 is up-regulated in PCa tissues and correlates with prostate cancer progression. USP13 silencing inhibits prostate cancer cell growth in vitro and in vivo. Mechanically, USP13 directly interacts with PCMT1 and removes polyubiquitination of PCMT1 to maintain its stability, which promotes PCa cell proliferation and enzalutamide resistance. Depletion of USP13 promoted PCa cells sensitive to enzalutamide. Clinically, USP13 was significantly up-regulated in prostate cancer tissues and positively associated with PCMT1 expression. Notably, inhibition of USP13 significantly decreases prostate tumor growth and improves enzalutamide treatments through PCMT1 suppression. Our studies demonstrate that inhibition of USP13 can offer a viable therapeutic option to overcome enzalutamide resistance in prostate cancer patients with USP13/PCMT1-overexpression. - Source: PubMed
Publication date: 2026/04/30
Wang ZhipengLiu XiaoqiangLi ZhongqiYuan RuizeZheng FuchunXiong SituZeng JinPang WanFu BinLi ShengXu SonghuiDeng Jun - Paclitaxel (PTX) is a first-line chemotherapeutic agent extensively employed in the management of breast cancer (BC); however, the emergence of drug resistance frequently results in unsatisfactory clinical outcomes and poor prognosis. This study aimed to investigate the pathogenic mechanisms that drive PTX resistance in BC. - Source: PubMed
Publication date: 2026/04/13
Yang NaCao JingyingJiang FengCao RenxianLiu Yiqi - Protein-l-isoaspartate -methyltransferase (PIMT), encoded by , is a repair enzyme that corrects isoaspartyl lesions, preserving protein structure and function. While indispensable for neuronal integrity, its role in red blood cells (RBCs) and transfusion outcomes is incompletely understood. Here, we show that novel erythroid-specific knockout mice display profound remodeling of one-carbon metabolism, accumulation of repair intermediates, and destabilization of glycolytic and cytoskeletal proteins, yet maintain lower lipid peroxidation and normal post-transfusion recovery. Analysis of 13,091 blood donors from the Recipient Epidemiology and Donor Evaluation Study (REDS)-III Red Blood Cell Omics (RBC Omics) study revealed that common variants associate with hemolysis phenotypes and regulate PIMT protein level, as gleaned by protein quantitative trait loci (pQTL) analyses. The nonsynonymous rs4816 (V120I) allele, enriched in donors of Asian or African ancestry, emerged as a beneficial variant: carriers exhibited lower osmotic hemolysis, altered peptide methylation flux, and higher PIMT protein levels. Recombinant expression confirmed that the I120 variant displays preserved global folding, but greater catalytic activity than the canonical V120 enzyme. Transfusion outcome data showed that genotype influences hemoglobin increments and bilirubin responses in recipients. These findings identify PIMT as a novel determinant of RBC storage biology and establish rs4816 as a protective allele, with broader implications for donor diversity, transfusion efficacy, and proteome maintenance in aging. - Source: PubMed
Publication date: 2026/04/16
Bevers ShaunIssaian Aaron VHay ArielKeele Gregory RDzieciatkowska MonikaReisz Julie AHaiman Zachary BNemkov TravisStephenson DanielMoore Amy LDeng XutaoStone MarsHansen Kirk CKleinman SteveNorris Philip JBusch Michael PPalsson Bernhard ORoubinian Nareg HJanetzko JohnVӧgeli BeatPage Grier PJones David NHenen Morkos AEisenmesser Elan ZZimring James CD'Alessandro Angelo