Rat Anti-Mouse CD107a
- Known as:
- Rat Antibody toMouse CD107a
- Catalog number:
- 129-10090
- Product Quantity:
- 25
- Category:
- -
- Supplier:
- Ray Biotech
- Gene target:
- Rat Anti-Mouse CD107a
Related genes to: Rat Anti-Mouse CD107a
- Gene:
- LAMP1 NIH gene
- Name:
- lysosomal associated membrane protein 1
- Previous symbol:
- -
- Synonyms:
- CD107a
- Chromosome:
- 13q34
- Locus Type:
- gene with protein product
- Date approved:
- 1990-07-15
- Date modifiied:
- 2016-01-14
Related products to: Rat Anti-Mouse CD107a
Related articles to: Rat Anti-Mouse CD107a
- Recent studies reveal that inorganic nanoparticles (NPs) can alter allergic skin reactions in a contact hypersensitivity (CHS) mouse model. Specifically, negatively charged silica (SiO) NPs suppressed the response whereas manganese doped titanium dioxide (mTiO) exacerbated it. Mast cells are critically important in transducing the CHS response. In this study we investigated the effect of SiO and mTiO NPs on bone marrow derived mast cell (BMMC) activation markers, degranulation and cytokine release. Sensitized BMMC were exposed to NPs alone or NPs plus antigen. Cytokines (IL-6, IL-13, TNF-α) and degranulation (β-hexosaminidase) studies were performed. Flow cytometry was used to follow cell surface activation markers including FcεRI, CD63 (LAMP-3), and CD107a (LAMP-1). Transmission Electron Microscopy (TEM) studies were preformed to assess NP endocytosis. Results found that mTiO NPs were cytotoxic to BMMC in a dose- and time-dependent manner. SiO NPs showed minimal cytotoxicity up to 100 µg/ml. In the absence of antigen the NPs had limited effect on sensitized BMMC degranulation or cytokine release. However, in the presence of antigen, 30 min co-culture studies (NP plus antigen) showed that SiO NPs protect against degranulation, and they suppressed the expression of cell surface activation markers whereas mTiO NPs exacerbated these. - Source: PubMed
Publication date: 2026/05/21
Pineda Jessica PerezDeLouise Lisa A - The small GTP-binding protein Arl8b is established as a regulator of lysosome positioning and fusion, yet its role in lysosome biogenesis remains unclear. Here, we investigate the role of Arl8b in the trafficking of newly synthesized LAMP1 to lysosomes using the Retention Using Selective Hook (RUSH) assay. We find that Arl8b localizes to post-endocytic LAMP1-containing vesicles prior to fusion with acidic lysosomes. Arl8b depletion leads to Rab11a-dependent recycling of LAMP1 to the plasma membrane, impairing its lysosomal delivery. Mechanistically, Arl8b recruits the Rab11a GAP, TBC1D9B, to LAMP1-positive membranes, and TBC1D9B depletion similarly disrupts LAMP1 sorting. Notably, TBC1D9B knockdown also impairs the retrieval of cation-independent mannose-6-phosphate receptor (CI-M6PR) from Rab11a- and Rab14-positive endosomes to the trans-Golgi network, impairing pro-cathepsin trafficking and cargo degradation. These findings reveal that Arl8b-mediated recruitment of Rab GAP TBC1D9B is crucial for inactivation of the Rab11a recycling pathway, leading to efficient sorting of lysosomal cargo to their functional location. - Source: PubMed
Publication date: 2026/05/21
Chouhan PriyaPhogat YogitaWalia KshitizDebnath SaikatChoubey SandeepGupta MedhaTuli AmitSharma Mahak - Intracerebral hemorrhage (ICH) is a neurological disorder characterized by a high mortality rate for which there is currently no definitive cure. Research has demonstrated that adipose-derived mesenchymal stem cells (ASCs) exhibit considerable potential in treating ICH. However, the advanced age of ICH patients and the necessary cell expansion before transplantation therapy could result in the senescence of ASCs, thereby compromising their viability and therapeutic efficacy. This study aims to investigate whether FGF21 (fibroblast growth factor 21) can rejuvenate aged ASCs by enhancing macroautophagy/autophagy flux and subsequently enhance the therapeutic efficacy of ICH. We demonstrated that the autophagy flux of aged ASCs was significantly decreased and FGF21 treatment significantly reversed the senescence phenotype and increased the viability of aged ASCs. Mechanistically, our findings suggested that FGF21 rejuvenates aged ASCs by augmenting autophagy flux, a process partly mediated by TFE3 (transcription factor E3) nuclear translocation. The FGF21-induced TFE3 nuclear translocation was partially facilitated potentially via the FGFR1-SIRT1-MTOR pathway. In addition, FGF21 enhanced the potential of senescent ASCs to differentiate into neurons. In the in vivo study, we further verified that FGF21 could enhance the therapeutic effect of ASCs on acute ICH rats. In conclusion, these results indicated that FGF21 could restore ASC viability by upregulating TFE3-mediated autophagy flux in part through the FGFR1-SIRT1-MTOR signaling pathway, enhanced the potential to improve the differentiation of ASCs into neural stem cells and enhanced the therapeutic effect of ASCs transplantation in acute ICH.: FGF21: fibroblast growth factor 21; TFE3: transcription factor E3; TFEB: transcription factor EB; DMEM: Dulbecco's modified Eagle medium; RAPA: rapamycin; 3-MA: 3-methyladenine; CQ: chloroquine; DMSO: dimethyl sulfoxide; RT-qPCR: quantitative real-time PCR; pAb: polyclonal antibody; mAb: monoclonal antibody; LAMP1: lysosomal associated membrane protein 1; SQSTM1/p62: sequestosome 1; MAP1lc3/LC3: microtubule associated protein 1 light chain 3; GFAP: glial fibrillary acidic protein; MAP2: microtubule associated protein 2; SOX2: SRY-box transcription factor 2; MOI: multiplicity of infection; FGFR1: fibroblast growth factor receptor 1; SIRT1: sirtuin 1; MTOR: mechanistic target of rapamycin kinase; ROS: reactive oxygen species; siRNA: small interfering RNA; OD: optical density; SASP: senescence-related secretion phenotype; IL6: interleukin 6; IL1B/IL-1β: interleukin 1 beta; TNF/TNF-α: tumor necrosis factor; CCL2/MCP-1: C-C motif chemokine ligand 2; BDNF: brain derived neurotrophic factor; VEGF: vascular endothelial growth factor; ICH: intracerebral hemorrhage; MLPT: modified limb placement test. - Source: PubMed
Publication date: 2026/05/19
Song BeiLiu ChengyunHu JingqiongZhao XiaofangFan HaohuiLiu TingGao GuangyuZhang XinyueGuang XuekeZhou QuanWang KunLu Weilin - Enteroviruses pose a substantial global health burden, and a complete understanding of host defense mechanisms is still evolving. Through proteomic profiling of coxsackievirus B3 (CVB3)-infected cells, we identified the host factor USF2 (upstream transcription factor 2) as significantly upregulated, a process that may be associated with the viral capsid protein VP4. Here, we characterize USF2 as a novel, infection-induced restriction factor. Functional studies demonstrate that USF2 knockdown enhances viral RNA replication without affecting entry, while its overexpression suppresses replication and cytopathic effects. Mechanistically, USF2 acts as a transcriptional repressor of autophagy-related genes, thereby inhibiting autophagosome formation. Crucially, USF2 depletion promotes the release of MAP1LC3/LC3-positive extracellular vesicles carrying infectious virus, defining its role in blocking a key route of vesicle-mediated viral dissemination. USF2 exhibits broad antiviral activity against multiple enteroviruses and other RNA viruses that depend on cytoplasmic membrane remodeling. Our findings reveal that the host deploys a virus-triggered transcriptional regulator to restrict enterovirus spread by suppressing macroautophagy/autophagy-dependent viral dissemination. BafA1: bafilomycin A; CQ: chloroquine; CPE: cytopathic effect; CVB3: coxsackievirus B3; dpi: days post infection; DEGs: differentially expressed genes; EV-A71: enterovirus A71; EVs: extracellular vesicles; GFP: green fluorescent protein; LAMP1: lysosomal-associated membrane protein 1; TR: LysoTracker Red; MAP1LC3/LC3: microtubule-associated protein 1 light chain 3; MOI: multiplicity of infection; TFEB: transcription factor EB; USF2: upstream transcription factor 2; UPR: unfolded protein response; VP1: viral capsid protein 1; VP4: viral capsid protein 4. - Source: PubMed
Publication date: 2026/05/22
Liang TianmingPeng ZeyuXi RuizhiChen ShuangYin GuangWang LinWang TianyingWei Guochao - Matrix-bound nanovesicles (MBVs) are a type of small extracellular vesicle (EV) embedded in the extracellular matrix (ECM) throughout the body. MBVs have been previously isolated from various tissues and cultured cell sheets, demonstrating remarkable attributes in regenerative medicine. However, differences between MBVs and conditioned culture medium-derived EVs (liquid-EVs) have yet to be characterized, and the field currently lacks specific protein markers that can identify MBVs from other EV subtypes. Here, we isolate MBVs and liquid-EVs from bone marrow mesenchymal stem cell (MSC) sheets and define differences in size, protein, and zeta potential between these EVs. We show that there is a correlation between cell-driven ECM deposition and MBV and liquid-EV production. We also find that MBVs are smaller, contain less protein per particle, and possess lower zeta potential than liquid-EVs. Interestingly, MBVs also comprise a distinct tetraspanin profile compared to liquid-EVs, with MBVs containing more CD63 and little to no CD81. Finally, we define that CD63, LAMP1, Alix, ITGβ1, and GRP94 and their abundance, may be markers specifically used to identify MBVs from liquid-EVs. Our study paves the way for the characteristic differentiation between MBVs from liquid-EVs, elucidates their differences in biogenesis, and reveals a potential connection between EV and ECM production. - Source: PubMed
Publication date: 2026/05/08
Dos Reis Marques RenataSheth MauleeSalami Ava IKongsomros SupasekEsfandiari LeylaDewey Marley J