SEQUAGEL MD SSCP STOP SOLUTION
- Known as:
- SEQUAGEL MD SSCP STOP SOLUTION
- Catalog number:
- EC-848-1.2ML
- Product Quantity:
- 1.2ML
- Category:
- -
- Supplier:
- AGC
- Gene target:
- SEQUAGEL SSCP STOP SOLUTION
Related genes to: SEQUAGEL MD SSCP STOP SOLUTION
- Gene:
- MAP6 NIH gene
- Name:
- microtubule associated protein 6
- Previous symbol:
- -
- Synonyms:
- KIAA1878, STOP, FLJ41346, MAP6-N
- Chromosome:
- 11q13.5
- Locus Type:
- gene with protein product
- Date approved:
- 1998-02-26
- Date modifiied:
- 2015-11-16
Related products to: SEQUAGEL MD SSCP STOP SOLUTION
Related articles to: SEQUAGEL MD SSCP STOP SOLUTION
- Kv3.3 voltage-gated K (Kv) channels are highly expressed in cerebellar Purkinje neurons and some hippocampal neurons, aligning with the motor and cognitive impairments observed in spinocerebellar ataxia 13 (SCA13) caused by Kv3.3 mutations. Despite their functional significance, the mechanisms governing Kv3.3 subcellular localization remain poorly understood. Here we report microtubule-associated protein 6 (MAP6) regulates Kv3.3 axon-dendrite targeting. MAP6 deletion reduces Kv3.3 levels in the processes of Purkinje neurons. Mechanistically, MAP6's 1st and 2nd Mn modules directly bind the external surface of the Kv3.3 N-terminal T1 tetramer, while its 3rd Mn module indirectly associates with Cav2 Ca channels. In Purkinje neurons, shRNA-mediated MAP6 knockdown decreases somatodendritic levels of both Kv3.3 and Cav2.1 (associated with SCA6). Notably, expression of Mn1/2-GFP selectively reduces Kv3.3, but not Cav2.1, levels. Purkinje neuron burst firing is reduced in both conditions. These findings uncover a MAP6-dependent mechanism for targeting two key ion channels linked to SCAs. - Source: PubMed
Publication date: 2026/04/30
Ma DiNalinakshan NandithaMarshall Alec HJukkola PeterBosc ChristopheGory-Fauré SylvieAndrieux AnnieWester Jason CGu Chen - Microtubule-associated Protein 6 (MAP6) is critical for maintaining microtubule stability and synaptic plasticity, and its dysfunction is a key driver of cognitive impairment. However, the molecular mechanisms linking MAP6 deletion to cognitive deficits remain unclear. Here, we generated a novel Map6 knockout (KO, Map6) mouse model using CRISPR/Cas9-mediated genome editing. Behavioral tests confirmed that Map6 mice exhibited prominent cognitive impairments, primarily in long-term memory and spatial learning. Hippocampal transcriptome profiling identified marked downregulation of neurotensin (Nts) in Map6 mice, which was validated at both mRNA and protein levels. Rescue experiments demonstrated that direct microinjection of neurotensin (NTS) peptide into the hippocampal CA1 subregion significantly improved cognitive deficits in Map6 mice. Electrophysiological recordings further confirmed that NTS restored impaired long-term potentiation (LTP)-a cellular substrate of learning and memory-in the hippocampal CA1 of Map6 mice. Additionally, chemogenetic activation of CA1 NTS-positive (CA1) neurons reversed these synaptic and behavioral phenotypes. Collectively, we delineate a novel pathway wherein MAP6 deletion induces cognitive impairment by suppressing hippocampal NTS expression and secretion, and both exogenous NTS supplementation and NTS signaling activation reverse Map6 deletion-induced synaptic and behavioral deficits. These findings identify NTS as a critical downstream effector of MAP6 in cognitive regulation, offering a potential therapeutic target for cognitive impairment. - Source: PubMed
Publication date: 2026/03/11
Jia YananLei JintaoJiang YunruiXue LitingChen TiantianWang JiaojiaoWei Hongen - Osteoarthritis (OA) is a whole-joint disorder characterized by progressive cartilage degradation and chronic synovial inflammation, in which macrophages play a central role. Using single-cell RNA sequencing of human and mouse synovial tissues, we identified a pronounced expansion of macrophages during OA progression, with nearly ubiquitous expression of the chemokine CXCL16. These CXCL16 macrophages exhibited a pro-inflammatory phenotype and were strongly associated with synovitis. To exploit this target, we developed a biomimetic nanoparticle (MAP6) by coating capsaicin-loaded poly(lactic-co-glycolic acid) (PLGA) with CXCR6-enriched M1 macrophage membranes, leveraging the specific CXCL16-CXCR6 interaction. The resulting MAP6 nanoparticles demonstrated enhanced cellular uptake, prolonged synovial retention, and specific targeting of CXCL16 macrophages in vivo. Furthermore, MAP6 treatment promoted Ca influx and NRF2 nuclear translocation, thereby suppressing pro-inflammatory cytokine expression. In a murine OA model, intra-articular administration of MAP6 markedly alleviated synovitis, reduced cartilage degradation, and suppressed the expression of catabolic factors. Collectively, this study highlights CXCL16 as a key macrophage-associated marker in OA and presents a targeted nanotherapeutic strategy capable of modulating synovial inflammation and halting disease progression. - Source: PubMed
Publication date: 2026/02/16
Yang QingjunXu YidiZhan YangLi JianpingPeng RuiYu BoZhang LeiLiang GuihongDeng PengCao HouranHan YanhongHuang ZexinPan JiankeJiang TaoYang WeiyiFeng YonghongHuang XunWu SizhiGui TaoYe Yongsheng - Pathological inclusions composed of tau are hallmarks of neurodegenerative diseases termed tauopathies, the most common of which is Alzheimer's disease. Accumulating evidence suggests that tau is involved in a multitude of physiological functions that are regulated, in part, by direct and/or transient protein interactions. Deciphering the tau interactome is critical for understanding the physiological and pathological roles of tau. This work aimed to identify potential tau interactors using the protein labeling biotin identification (BioID2) method. Advantages of this approach include in-cell interactor labeling and an enhanced likelihood of detecting transient and/or weak interactions. We identified 324 potential tau interactors spanning multiple cellular compartments and pathways. We validated tau interactions with selected candidates using two independent approaches: proximity ligation assay and co-immunoprecipitation (co-IP) which included cytoskeletal proteins (MAP2 and MAP6), nucleus-associated proteins (FUS and prune1), and synaptic proteins (synapsin-1 and neurabin-2). Importantly, this approach revealed potential novel interactors that were not clearly identified by other interaction approaches such as co-IP. Thus, this approach is a powerful tool to identify potential members of the tau interactome via labeling. This work helps expand our understanding of tau's physiological roles, which may also advance our understanding of its role in neurodegenerative diseases. - Source: PubMed
Publication date: 2025/09/05
Atwa AhmedAlhadidy Mohammed MLamp JaredCombs BenjaminKanaan Nicholas M - We previously documented that individual microtubules in the axons of cultured juvenile rodent neurons consist of a labile domain and a stable domain and that experimental depletion of tau results in selective shortening and partial stabilization of the labile domain. After first confirming these findings in adult axons, we sought to understand the mechanism that accounts for the formation and maintenance of these microtubule domains. We found that fluorescent tau and MAP6 ectopically expressed in RFL-6 fibroblasts predominantly segregate on different microtubules or different domains on the same microtubule, with the tau-rich ones becoming more labile than in control cells and the MAP6-rich ones being more stable than in control cells. These and other experimental findings, which we studied further using computational modeling with tunable parameters, indicate that these two MAPs do not merely bind to pre-existing stable and labile domains but actually create stable and labile domains on microtubules. - Source: PubMed
Publication date: 2025/01/29
Kirimtay KorayHuang WenqiangSun XiaohuanQiang LiangWang Dong VSprouse Calvin TCraig Erin MBaas Peter W