TETRAN Blocking Peptide
- Known as:
- TETRAN Blocking Peptide
- Catalog number:
- 33r-1438
- Product Quantity:
- USD
- Category:
- -
- Supplier:
- Fitzgerald industries international
- Gene target:
- TETRAN Blocking Peptide
Related genes to: TETRAN Blocking Peptide
- Gene:
- MFSD10 NIH gene
- Name:
- major facilitator superfamily domain containing 10
- Previous symbol:
- -
- Synonyms:
- TETRAN, IT10C3
- Chromosome:
- 4p16.3
- Locus Type:
- gene with protein product
- Date approved:
- 2008-03-03
- Date modifiied:
- 2014-11-19
Related products to: TETRAN Blocking Peptide
Related articles to: TETRAN Blocking Peptide
- Osteoporosis (OP) is a common metabolic bone disease characterized by decreased bone mass and increased fracture risk. Recent studies suggest that oxidative phosphorylation (OXPHOS) plays a crucial role in the pathogenesis of OP. This study aims to investigate the differential expression and potential functional roles of OXPHOS-related genes in OP. - Source: PubMed
Publication date: 2025/04/16
Wang SongmaoWang YalingGan MinfengWan LeiLiu YapuXu YonghuiHou ZhenxingDeng YongkangWu Xuejian - The major facilitator superfamily (MFS) is known as the largest and most diverse superfamily containing human transporters, and these transporters are essential as they sustain the homeostasis within cellular compartments by moving substances over lipid membranes. We have identified a novel MFS protein, named Major facilitator superfamily domain containing 6 (MFSD6), and confirmed that it is phylogenetically related to the human Solute Carrier (SLC) transporter family. A homology model of MFSD6 revealed 12 predicted transmembrane segments (TMS) with the classical MFS fold between TMS 6 and 7. Immunohistological analyses showed specific MFSD6 staining in neurons of wildtype mouse brain tissue, but no expression in astrocytes. Furthermore, we explored expression and probable function(s) of MFSD6 in relation to its phylogenetically related proteins, major facilitator superfamily domain containing 8 (MFSD8) and 10 (MFSD10), which is of interest as both these proteins are involved in diseases. We showed that expression levels of and were decreased with elevated or depleted energy consumption, while that of remained unaffected. - Source: PubMed
Publication date: 2020/01/06
Bagchi SonchitaPerland EmelieHosseini KimiaLundgren JohannaAl-Walai NouraKheder SaniaFredriksson Robert - The double membrane nuclear envelope (NE), which is contiguous with the ER, contains nuclear pore complexes (NPCs) - the channels for nucleocytoplasmic transport, and the nuclear lamina (NL) - a scaffold for NE and chromatin organization. Since numerous human diseases linked to NE proteins occur in mesenchyme-derived cells, we used proteomics to characterize NE and other subcellular fractions isolated from mesenchymal stem cells and from adipocytes and myocytes. Based on spectral abundance, we calculated enrichment scores for proteins in the NE fractions. We demonstrated by quantitative immunofluorescence microscopy that five little-characterized proteins with high enrichment scores are substantially concentrated at the NE, with Itprip exposed at the outer nuclear membrane, Smpd4 enriched at the NPC, and Mfsd10, Tmx4, and Arl6ip6 likely residing in the inner nuclear membrane. These proteins provide new focal points for studying the functions of the NE. Moreover, our datasets provide a resource for evaluating additional potential NE proteins. - Source: PubMed
Cheng Li-ChunBaboo SabyasachiLindsay CoryBrusman LizaMartinez-Bartolomé SalvadorTapia OlgaZhang XiYates John RGerace Larry - The eosinophil is deeply associated with the pathogenesis of bronchial asthma and other allergic diseases. We recently identified a novel eosinophil-specific cell surface molecule, major facilitator super family domain containing 10 (Mfsd10). A monoclonal antibody (mAb) against Mfsd10 (M2) showed selective binding and neutralizing activities for eosinophils. However, the relative potency of the blockage of Mfsd10 and other eosinophil-specific molecules for the treatment of allergic diseases has not been evaluated. Therefore, in this study, the effects of M2 and an anti-Siglec-F mAb on antigen-immunized and antigen-specific Th2 cell-transferred murine eosinophilic inflammation models were comparatively investigated. - Source: PubMed
Nishimura TomoeSaeki MayumiMotoi YujiKitamura NorikoMori AkioKaminuma OsamuHiroi Takachika - Eosinophilic inflammation is the prominent feature of bronchial asthma, though the importance of eosinophils in the pathogenesis of this disease is controversial. We here established monoclonal antibodies against a newly identified cell surface molecule specifically expressed on mouse eosinophils. Eosinophils were highly purified from small intestine lamina propria and thymus as CD11c(+)Gr1(low)F4/80(+)B220(-) cells. Upon comparative microarray analysis for mRNA expressed in eosinophils and other leukocytes, major facilitator super family domain containing 10 (Mfsd10) was identified as a novel eosinophil-specific cell surface molecule. Hybridomas were established from spleen cells of rats immunized with Mfsd10-introduced Ba/F3 cells. One of three monoclonal antibodies against Mfsd10 displayed selective binding activity against eosinophils recovered in bronchoalveolar lavage fluid of ovalbumin-immunized and -challenged mice. Administration of this antibody in vivo induced a significant reduction of eosinophils recruited in the allergic lungs. Anti-Mfsd10 antibody is useful for investigating the pathophysiological roles of eosinophils with its selective binding and neutralizing activity for mouse eosinophils. - Source: PubMed
Publication date: 2012/07/20
Motoi YujiSaeki MayumiNishimura TomoeKatayama KazufumiKitamura NorikoIchikawa HitoshiMiyoshi HiroyukiKaminuma OsamuHiroi Takachika