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)
- Spontaneous isomerization of aspartate and deamidation of asparagine residues into isoaspartate (isoAsp) constitute major non-enzymatic post-translational modifications that alter protein structure, stability, and turnover. The repair enzyme protein L-isoaspartate O-methyltransferase (PCMT1) catalyzes methylation of isoAsp residues, thereby preventing their accumulation and preserving proteome integrity. Although PCMT1 has been studied extensively in cytoplasm and nucleus, its relationship to endoplasmic reticulum (ER) proteostasis remains poorly understood. Here, we investigated dynamics of aspartate isomerization within the cell, focusing on isoAsp accumulation and the regulation of PCMT1 localization under physiological and stress conditions. Using immunofluorescence, subcellular fractionation, and methylation assays, we detected isoAsp-modified proteins within the ER-enriched fractions of HeLa cells. We found that ER stress induction enhanced formation of isoAsp-containing proteins, with MG132 treatment producing the highest accumulation. PCMT1 expression increased under both stress conditions, accompanied by distinct subcellular redistribution between the cytoplasmic and nuclear compartments. These observations indicate that ER-folded proteins are susceptible to spontaneous aspartate isomerization, and that PCMT1 activity dynamically responds to proteostatic stress. Our findings provide the first experimental evidence linking isoAsp formation within the ER to PCMT1-mediated protein repair, thereby integrating chemical instability with cellular quality-control pathways. This study establishes a structural and cellular framework for understanding the dynamics of aspartate isomerization in the cell and underscores significance of PCMT1 in maintaining proteostasis under stress conditions. - Source: PubMed
Biterge Burcu - 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