CD222
- Known as:
- CD222
- Catalog number:
- 11-315-M001
- Product Quantity:
- 1.0 mg
- Category:
- -
- Supplier:
- Exbio
- Gene target:
- CD222
Related genes to: CD222
- Gene:
- IGF2R NIH gene
- Name:
- insulin like growth factor 2 receptor
- Previous symbol:
- -
- Synonyms:
- CD222, MPRI, MPR1, CIMPR, M6P-R, CI-M6PR, CI-MPR, MPR300
- Chromosome:
- 6q25.3
- Locus Type:
- gene with protein product
- Date approved:
- 1988-07-07
- Date modifiied:
- 2019-04-23
Related products to: CD222
Antibodies: Mouse Monoclonal to CD222 _ IGF2 receptor _ CIMPR, Species Reactivity: Human, Non-Human Primates, Clone: MEM-238, Isotype: IgG1Antibodies: Mouse Monoclonal to CD222 _ IGF2 receptor _ CIMPR, Species Reactivity: Human, Non-Human Primates, Clone: MEM-238, Isotype: IgG1Antibodies: Mouse Monoclonal to CD222 _ IGF2 receptor _ CIMPR, Species Reactivity: Human, Non-Human Primates, Clone: MEM-238, Isotype: IgG1Antibodies: Mouse Monoclonal to CD222 _ IGF2 receptor _ CIMPR, Species Reactivity: Human, Non-Human Primates, Clone: MEM-238, Isotype: IgG1Antibodies: Mouse Monoclonal to CD222 _ IGF2 receptor _ CIMPR, Species Reactivity: Human, Non-Human Primates, Clone: MEM-238, Isotype: IgG1Antibodies: Mouse Monoclonal to CD222 _ IGF2 receptor _ CIMPR, Species Reactivity: Human, Non-Human Primates, Clone: MEM-238, Isotype: IgG1Antibodies: Mouse Monoclonal to CD222 _ IGF2 receptor _ CIMPR, Species Reactivity: Human, Non-Human Primates, Clone: MEM-238, Isotype: IgG1Antibodies: Mouse Monoclonal to CD222 _ IGF2 receptor _ CIMPR, Species Reactivity: Human, Non-Human Primates, Clone: MEM-238, Isotype: IgG1Antibodies: Mouse Monoclonal to CD222 _ IGF2 receptor _ CIMPR, Species Reactivity: Human, Non-Human Primates, Clone: MEM-238, Isotype: IgG1Antibodies: Mouse Monoclonal to CD222 _ IGF2 receptor _ CIMPR, Species Reactivity: Human, Non-Human Primates, Clone: MEM-238, Isotype: IgG1CD222 IGF2R antibody Ab host: RabbitCD222 IGF2R antibody Ab host: RabbitCD222 IGF2R antibody Ab host: RabbitCD222 IGF2R antibody Ab host: RabbitCD222 IGF2R antibody Ab host: Rabbit Related articles to: CD222
- Lysosomal storage disorders (LSDs) are intractable rare diseases caused by lysosomal dysfunction due mainly to defects in lysosomal enzyme genes. For many lysosomal enzymes to be transported correctly into lysosomes, their mannose-6-phosphate (M6P) labeling by GlcNAc-1 phosphotransferase (GNPT) is crucial. M6P-modified lysosomal enzymes are captured by M6P receptors and transported to lysosomes. The M6P-dependent pathway is utilized not only for newly synthesized lysosomal enzymes but also for the intracellular transport of exogenously administered lysosomal enzymes to lysosomes. In this study, we performed gene knockouts targeting the M6PR and IGF2R genes, which encode the M6P receptors. Cells with a double knockout of these genes secrete M6P-modified proteins into the culture supernatant (dKO sup), and we investigated its potential for therapeutic application. I-cell disease (mucolipidosis II, ML-II) arises from GNPT deficiency and is a disorder in which dozens of lysosomal enzymes are deficient within the cell. Treating ML II cells with the dKO sup restored lysosomal enzyme activity, reduced inclusion bodies, and improved autophagic function. ML II patient-derived fibroblasts exhibited increased lysosomal enzyme activities, normalized morphology, and improved cryo-viability with the treatment. NPC2 protein is not a lysosomal enzyme but functions cooperatively with NPC1 protein to mediate cholesterol transport in lysosomes. NPC2 deficiency causes Niemann-Pick disease type C2, and the dKO sup restored the cellular function of the disease by supplementing the NPC2 protein. These results indicate that M6PR/IGF2R double-deficient cells provide a simple platform for supplying M6P-modified proteins that can be applied to the treatment of a broad range of LSDs. - Source: PubMed
Publication date: 2026/08/28
Fujita ToshiharuTerawaki SeigoMoriwaki TakahitoOtomo Takanobu - Targeted protein degradation (TPD) enables selective elimination of disease-related proteins, including viral proteins. Here, we evaluated the antiviral potential of an IGF2-fused lysosomal targeting chimera (iLYTAC) in ZIKV- and IAV-infected models. We first confirmed that iLYTAC efficiently mediates uptake of extracellular proteins via the IGF2-IGF2R pathway and traffics to lysosomes. In combination with anti-E-cadherin antibody, iLYTAC reduced E-cadherin levels by 2-fold, indicating functional lysosomal targeting. For antiviral application, iLYTAC combined with non-neutralizing anti-ZIKV E IgG significantly reduced viral titers (10 to 10 PFU/mL), decreased viral RNA and protein levels, and promoted lysosomal colocalization of E protein, which was abolished by lysosome inhibition. In ZIKV-infected mice, iLYTAC combined with anti-E IgG reduced viral loads across tissues and blood, alleviated organ pathology and inflammation. Similarly, in H1N1-infected A549 cells, iLYTAC with non-neutralizing anti-HA IgG reduced cytopathic effects and viral titers, while selectively degrading HA via lysosomes without affecting NP. Overall, iLYTAC converts non-neutralizing antibodies into functional degraders of viral proteins, enabling effective suppression of infection and providing a potential platform for broad-spectrum antiviral therapeutics. - Source: PubMed
Publication date: 2026/08/20
Ma SaiyaZhang JieZhou SijieLi JingMa WenminYin XianzhengWang XiaochunTong Jie - Maternal high-fat diet (HFD) contributes to developmental programming through placental adaptations; however, the effects of exposure timing before and during pregnancy remain unclear. - Source: PubMed
Publication date: 2026/08/18
Lin Yu-JuCheng Yin-HuaTsai Ni-ChinTsai Ching-ChouTain You-LinYu Hong-RenLan Kuo-Chung - Tumor necrosis factor-α (TNF-α) is a well-characterized causal mediator in the pathogenesis of acute liver failure (ALF). Despite the efficacy of TNF-α inhibitors (e.g., antibodies and Fc-fused receptor proteins) in animal models, clinic translation has not been successful so far, largely due to sustained repression of TNF-α signaling and Fc-mediated deleterious immune responses. To address these obstacles, we aim to develop a new modality targeting TNF-α by employing lysosome-targeting protein degradation technology. - Source: PubMed
Publication date: 2026/08/18
He JunjieLi XuanyiHu WenZhang YutingZhang ZhuochaoZhao SiyuHe MuyangWang JingXiao HeLi XinyingLiu ChenghuaXu FanxingMa NingQiao ChunxiaFeng JiannanChen Guojiang - Prostate cancer (PCa) is characterized by molecular heterogeneity and metabolic reprogramming, but the relationships among transcriptomic, proteomic, and metabolic signals remain incompletely defined. Here, we present a human-centered, cross-dataset analysis of public RNA, protein, and metabolomics data in PCa. We analyzed RNA and protein profiles from PC3 parental and drug-resistant cells together with an independent human matched tissue metabolomics dataset from Metabolomics Workbench (ST000784). RNA-protein overlap analysis identified seven genes that were significant at both layers, including five concordantly upregulated genes: UPP1, IGF2R, FLNC, DSP, and PLEC. Among these, UPP1 provided the most direct metabolic interpretation because it encodes uridine phosphorylase 1, an enzyme linked to pyrimidine salvage. Independent ST000784 matched prostate tissue metabolomics supported broader nucleotide metabolism remodeling, including significant changes in N-carbamoyl-L-aspartate, guanosine monophosphate, and adenosine 3,5-cyclic monophosphate. In contrast, uracil was not significantly altered and uridine 5'-monophosphate showed only a trend after multiple-testing correction. Repeated stratified cross-validation showed that UPP1-containing candidate gene sets achieved high within-layer AUC values in RNA and protein data, while nested statistical benchmark models also performed strongly. These results prioritize a UPP1-associated nucleotide remodeling hypothesis in PCa, but do not establish causal regulation of metabolite abundance or clinical diagnostic utility. Future matched multi-omics and perturbation experiments are required. - Source: PubMed
Publication date: 2026/07/31
Chen XuancaiSu WeiZhou QunQi YuchengXie JuanjuanTang YachunTang XinFu Hao