{"product_id":"tdp-43-hexamutant-w-s-monomers-bhp11901251","title":"TDP-43 Hexamutant (W→S) Monomers","description":"\u003ch2\u003eBackground\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eTDP-43\u003c\/strong\u003e is provided as a recombinant protein reagent for \u003cstrong\u003eresearch use only\u003c\/strong\u003e. It is commonly used as a defined molecular component in biochemical and cell-free systems where controlled protein input supports mechanistic study and assay development.\u003c\/p\u003e\u003cp\u003e\u003cstrong\u003eProtein identity context:\u003c\/strong\u003e TDP-43 (source species: Human).\u003c\/p\u003e\u003cp\u003eHuman Recombinant TDP-43 (W68S, W113S, W172S, W334S, W385S, W412S) Mutant Monomers\u003c\/p\u003e\u003cp\u003eTAR DNA-binding protein 43 (TDP-43) is a ubiquitously expressed RNA\/DNA-binding protein that plays a pivotal role in RNA processing, including RNA splicing, mRNA turnover, and microRNA biogenesis. Its pathological mislocalization from the nucleus to the cytoplasm, accompanied by aggregation and post-translational modifications, is a hallmark of several neurodegenerative diseases such as amyotrophic lateral sclerosis (ALS), frontotemporal lobar degeneration (FTLD), and Alzheimer’s disease. These TDP-43 proteinopathies disrupt nucleocytoplasmic transport and mitochondrial function, contributing to neuronal dysfunction and death. Recent studies have also highlighted TDP-43’s involvement in DNA repair and chromatin remodeling, expanding its relevance in neurobiology beyond RNA processing. Notably, Pokrishevsky et al. (2024) demonstrated that when all six tryptophans are mutated to serines (trpless), this significantly reduces the protein’s ability to cross-seed SOD1 aggregation. Our TDP-43 hexamutant monomers has shown a reduced propensity to aggregate.\u003c\/p\u003e\u003ch2\u003eBiological significance and function\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eTDP-43\u003c\/strong\u003e is used in RUO research to interrogate molecular mechanisms, interaction networks, and pathway-linked phenotypes in experimental systems. This protein is frequently discussed in research themes such as \u003cstrong\u003eNeuroscience\u003c\/strong\u003e and \u003cstrong\u003eNeurodegeneration\u003c\/strong\u003e.\u003c\/p\u003e\u003ch2\u003eMolecular characteristics\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eMolecular characteristics:\u003c\/strong\u003e Key molecular attributes can influence binding behavior, stability, and assay background—especially for multimeric, disulfide-rich, or PTM-dependent proteins.\u003c\/p\u003e\u003cul\u003e\n\u003cli\u003e\n\u003cstrong\u003eSource species:\u003c\/strong\u003e Human\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eProtein length:\u003c\/strong\u003e 413 AA\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eProtein size:\u003c\/strong\u003e 44.61 kDa\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003ePurity:\u003c\/strong\u003e \u0026gt; 95% by A260\/A280\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eExpression system:\u003c\/strong\u003e E. coli\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003ePurification:\u003c\/strong\u003e Affinity Purified\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eStorage buffer:\u003c\/strong\u003e 30mM Tris pH 7.4, 100 mM NaCl\u003c\/li\u003e\n\u003c\/ul\u003e\u003cp\u003e\u003cstrong\u003ePost-translational considerations:\u003c\/strong\u003e E. coli expression typically yields a non-glycosylated recombinant form. This is often appropriate for intracellular enzymes and many binding studies, but extracellular ligands\/receptors or disulfide-rich proteins may show activity or stability differences when PTMs are required.\u003c\/p\u003e\u003ch2\u003eExpression and purification strategy\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eExpression system:\u003c\/strong\u003e E. coli. Expression host choice can influence folding and PTM state, which may affect binding or activity depending on protein class.\u003c\/p\u003e\u003cp\u003e\u003cstrong\u003ePurification strategy:\u003c\/strong\u003e Affinity Purified. Purification method and formulation help determine sample homogeneity and background in downstream biochemical assays.\u003c\/p\u003e\u003ch2\u003eResearch interpretation\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eResearch interpretation:\u003c\/strong\u003e Recombinant protein reagents can support controlled experiments such as reconstitution of molecular interactions, quantitative calibration, and mechanistic perturbation studies with defined inputs. Interpreting outcomes typically benefits from pairing the primary readout with orthogonal markers that report on pathway state, localization, and complex formation.\u003c\/p\u003e","brand":"StressMarq Biosciences Inc.","offers":[{"title":"100 ug","offer_id":53016297406829,"sku":"SPR-522B","price":495.0,"currency_code":"USD","in_stock":true},{"title":"100 ug x 2","offer_id":53016297439597,"sku":"SPR-522C","price":890.0,"currency_code":"USD","in_stock":true},{"title":"100 ug x 5","offer_id":53016297472365,"sku":"SPR-522E","price":1850.0,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0949\/7424\/7277\/files\/SPR-522_TDP-43-Hexamutant-W_E2_86_92S-Monomers-Protein-SDS-Page-1.png?v=1782160470","url":"https:\/\/www.ebiohippo.com\/products\/tdp-43-hexamutant-w-s-monomers-bhp11901251","provider":"BioHippo","version":"1.0","type":"link"}