MCP_RAT Cd46 ELISA tesk kit
- Known as:
- MCP_RAT Cd46 Enzyme-linked immunosorbent assay test tesk reagent
- Catalog number:
- gen16414
- Product Quantity:
- 1
- Category:
- Peptides
- Supplier:
- Other suppliers
- Gene target:
- MCP_RAT Cd46 ELISA tesk kit
Related genes to: MCP_RAT Cd46 ELISA tesk kit
- Gene:
- CD46 NIH gene
- Name:
- CD46 molecule
- Previous symbol:
- MIC10, MCP
- Synonyms:
- TRA2.10, MGC26544, TLX
- Chromosome:
- 1q32.2
- Locus Type:
- gene with protein product
- Date approved:
- 1988-08-31
- Date modifiied:
- 2019-04-23
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- Oncolytic viruses are promising cancer biotherapies but often show limited durability as single agents due to tumor-intrinsic resistance mechanisms. Because therapeutic efficacy is shaped by dynamic virus-tumor-stromal interactions, pharmacologic strategies that reprogram this interface may enhance virotherapy responses. Here, we investigate whether targeting tumor stress and survival pathways with triptolide and its prodrug Minnelide can enhance the oncolytic efficacy of measles virus in colorectal cancer. - Source: PubMed
Publication date: 2026/06/06
Chavez ValeryMontero MelissaTran Ngoc Huong GiangMendes Carolina MerchanBan YuguangKhurana RimpiCeccarelli MichelleMerchan Jaime R - Gram-negative bacteria release outer membrane vesicles (OMVs) that deliver various molecules, including virulence factors, allowing them to interact with their host. Recent evidence suggests that OMVs may serve as carriers for RNAs, in particular small regulatory noncoding RNAs (sRNAs). However, for these sRNAs to function effectively, they often require a protein cofactor, typically the Hfq RNA chaperone. In our previous studies, we demonstrated that Hfq, after interacting with the bacterial inner membrane, can be translocated to the periplasm and subsequently exported within OMVs, potentially in association with RNAs. In the present study, we build upon this previous work and provide evidence that RNA molecules are not only a key component of the OMV lumen, but can also be inserted into the vesicle membrane in an Hfq-dependent manner. This new finding suggests that surface-presented RNAs may be directly delivered to the host. Overall, our results reveal a previously unrecognized aspect of OMV-associated RNA and emphasizes the need to explore the role of RNAs in cell-to-cell communication, as OMV-host interplay may not be governed solely by protein-protein or protein-membrane contacts. - Source: PubMed
Mosca KevinTurbant FlorianAchouak WafaWien FrankArluison Véronique - To define CSC genetic architecture and identify implicated ocular tissues, cell types, genes, and circulating proteins. - Source: PubMed
Publication date: 2026/05/22
Chen LiyinKim Soo HyunTruong BuuRämö Joel TGorman Bryan Rvan Dijk Elon H CBrinks JoostNikopensius TiitChoi Seung HoanKajanne RistoMehtonen JuhaKaarniranta KaiSobrin LuciaKurki MitjaYzer Suzanne Wu Wen-ChihTurunen Joni ASegrè Ayellet JMercader Josep MariaHuerta AliciaDaly Mark JPalotie AarnoEllinor Patrick TBoon Camiel JfIyengar Sudha KPeachey Neal SNatarajan PradeepRossin Elizabeth J - Homeostasis of peroxisomes and their constituents maintains peroxisome function during plant growth, development, and environmental responses. Protein degradation maintains peroxisome homeostasis by eliminating misfolded or damaged proteins and precisely regulating the abundance of specific proteins. However, the mechanism by which a subset of peroxisomal proteins is transported from the peroxisome to the proteasome for degradation remains unclear. Here, we show that CELL DIVISION CONTROL PROTEIN 48 HOMOLOG A (CDC48A) and its cofactor, the plant UBX-domain containing (PUX) protein PUX10, play a critical role in the degradation of certain peroxisomal proteins in Arabidopsis thaliana. The inducible expression of a CDC48A dominant-negative mutant (CDC48A-DN) or a deficiency of PUX10 (pux10 mutant) caused the accumulation of ubiquitinated proteins and defective degradation of peroxisomal proteins, including the peroxin (PEX) PEX5, a receptor responsible for cytosolic cargo delivery to the peroxisomal matrix, and the peroxisomal matrix protein CATALASE3 (CAT3). We further reveal that PUX10 is an integral peroxisomal membrane protein that interacts with PEX5 and CAT3 via its UBA domain. Functional analysis demonstrates that CDC48A is required for peroxisomal metabolism and abundance, whereas loss of PUX10 only affects peroxisome abundance. Overall, these findings establish that the CDC48A-PUX10 complex is a key component in the ubiquitin-dependent peroxisome-associated degradation machinery, which governs the turnover of a subset of peroxisomal proteins. - Source: PubMed
Publication date: 2026/05/27
Li JingeYu ShijiaoZang XiaoxiaoWang ShuoQin ZhaoxiaMa Changle - Complement activation is a major barrier to xenotransplantation. We report detailed complement monitoring in a 58-year-old man who received a 10 gene-edited porcine heart expressing human complement regulators CD46 and CD55. Despite these transgenes and prophylactic systemic complement inhibition with C1 esterase inhibitor (C1INH), early surveillance biopsy on post-operative day (POD) 13 showed significant histologic evidence of complement deposition with C3d and C4d within capillaries and endothelial activation. In light of these findings, treatment was escalated to terminal complement inhibition using eculizumab. Post-operative complement activity was assessed via immunohistochemistry and dynamic ex vivo serum assays, including a novel bioluminescent modified Ham (bmHam) assay. Following eculizumab initiation, serum sC5b-9 dropped to undetectable levels, and bmHam cytotoxicity decreased significantly, confirming terminal pathway inhibition. Dilutional bmHam assays further demonstrated stronger complement blockade with eculizumab than with C1INH. However, repeat transplant biopsy on POD 30 biopsy showed persistence of anti-C4d+ and anti-C3c+ staining, and increased C5b-9 compared to POD13. This breakthrough was identified by the dilutional bmHam but was not detected by changes in CH50 or sC5b-9. These findings highlight the potential need for early terminal complement inhibition and integrated functional monitoring as critical components of xenotransplant management. - Source: PubMed
Cole Michael ATully AndyGalindo JavierSingh Avneesh KWaldman MerylAthale JanhaviBoudhabhay IdrisMorgand ErwanMezine FarizaGoutaudier ValentinSannier AurélieLewis BradKain JameyEro MikeRoumenina LubkaBruneval PatrickChristenson RobertTamburro LoBurke AlanDrachenburg CinthiaLoupy AlexandreAyares DavidBrodsky Robert AGriffith Bartley PMohiuddin Muhammad MGrazioli Alison