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3 件の結果が “23435” で取得されました
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B6-hTARDBP
製品ID :
C001418
系統:
C57BL/6JCya
状況:
説明:
Amyotrophic lateral sclerosis (ALS), also known as Lou Gehrig's disease, is a fatal progressive neurodegenerative disease characterized by the degeneration and death of motor neurons in the central nervous system. This loss of motor neurons leads to progressive muscle weakness and atrophy, ultimately culminating in the complete loss of voluntary muscle control. Consequently, ALS can induce speech, swallowing, and respiratory difficulties [1]. Critically, unlike Alzheimer's disease, ALS does not necessarily impact higher-order cognitive functions. Remarkably, patients in advanced stages of the disease can maintain clear thinking and retain their premorbid memory, personality, and intelligence. Several genes have been identified as causative factors in ALS, including SOD1, ALS2, TARDBP, and FUS. Among them, TARDBP (TAR DNA-binding protein) is a gene encoding a protein involved in diverse cellular functions, including facilitating nuclear protein import, regulating circadian rhythms, and maintaining protein stability [2]. Mutations in the TARDBP gene are linked to ALS. These mutations can lead to abnormal TDP-43 protein accumulation and its mislocalization to the cytoplasm, a key pathological hallmark of the disease [3].
TARDBP-targeted therapy is mainly based on monoclonal antibody drugs, most of which are still in the preclinical stage of development. Oligonucleotides such as ASO and gene therapy have also been reported in the literature. These drugs are mainly used for the treatment of neurodegenerative diseases such as amyotrophic lateral sclerosis (ALS) and frontotemporal dementia (FTD). TARDBP is a new and popular target for the treatment of ALS. Preclinical disease research models are mainly transgenic (TG) or point mutation (PM) mice. To advance TARDBP-targeted drug therapies, especially gene and oligonucleotide therapies, Cyagen has independently developed a mouse Tardbp gene humanized model, which replaces the mouse Tardbp gene with the human TARDBP gene through gene editing technology. It can be used to study neurodegenerative diseases such as amyotrophic lateral sclerosis and frontotemporal dementia. The homozygous B6-hTARDBP mice are viable and fertile. In addition, based on the technological innovation of TurboKnockout fusion BAC recombination, Cyagen can also provide popular point mutation disease models based on this model and can provide customized services according to different point mutations to meet the needs of researchers for amyotrophic lateral sclerosis and frontotemporal dementia.
Amyotrophic lateral sclerosis (ALS), also known as Lou Gehrig's disease, is a fatal progressive neurodegenerative disease characterized by the degeneration and death of motor neurons in the central nervous system. This loss of motor neurons leads to progressive muscle weakness and atrophy, ultimately culminating in the complete loss of voluntary muscle control. Consequently, ALS can induce speech, swallowing, and respiratory difficulties [1]. Critically, unlike Alzheimer's disease, ALS does not necessarily impact higher-order cognitive functions. Remarkably, patients in advanced stages of the disease can maintain clear thinking and retain their premorbid memory, personality, and intelligence. Several genes have been identified as causative factors in ALS, including SOD1, ALS2, TARDBP, and FUS. Among them, TARDBP (TAR DNA-binding protein) is a gene encoding a protein involved in diverse cellular functions, including facilitating nuclear protein import, regulating circadian rhythms, and maintaining protein stability [2]. Mutations in the TARDBP gene are linked to ALS. These mutations can lead to abnormal TDP-43 protein accumulation and its mislocalization to the cytoplasm, a key pathological hallmark of the disease [3].
TARDBP-targeted therapy is mainly based on monoclonal antibody drugs, most of which are still in the preclinical stage of development. Oligonucleotides such as ASO and gene therapy have also been reported in the literature. These drugs are mainly used for the treatment of neurodegenerative diseases such as amyotrophic lateral sclerosis (ALS) and frontotemporal dementia (FTD). TARDBP is a new and popular target for the treatment of ALS. Preclinical disease research models are mainly transgenic (TG) or point mutation (PM) mice. To advance TARDBP-targeted drug therapies, especially gene and oligonucleotide therapies, Cyagen has independently developed a mouse Tardbp gene humanized model, which replaces the mouse Tardbp gene with the human TARDBP gene through gene editing technology. It can be used to study neurodegenerative diseases such as amyotrophic lateral sclerosis and frontotemporal dementia. The homozygous B6-hTARDBP mice are viable and fertile. In addition, based on the technological innovation of TurboKnockout fusion BAC recombination, Cyagen can also provide popular point mutation disease models based on this model and can provide customized services according to different point mutations to meet the needs of researchers for amyotrophic lateral sclerosis and frontotemporal dementia.
huTARDBP-Q331K/M337V/A382T
製品ID :
C001963
系統:
C57BL/6JCya
状況:
説明:
TAR DNA-binding protein 43 (TARDBP/TDP43) is a crucial protein involved in RNA processing, transport, and metabolism. Its aggregation in the cytoplasm is a key pathological feature of several neurodegenerative diseases, including Amyotrophic Lateral Sclerosis (ALS) and Frontotemporal Dementia (FTD). TDP43 is a multifunctional nuclear protein and is the main component of ubiquitin-positive cytoplasmic inclusions found in residual motor neurons of sporadic and familial ALS, with cytoplasmic TDP43 inclusions observed in almost all ALS cases [1]. TDP43 is typically localized in the cell nucleus but can shuttle between the nucleus and cytoplasm to perform various functions, including regulating RNA splicing, transport, and homeostasis. Both cytoplasmic mislocalization and nuclear loss of TDP43 are associated with ALS and FTD, and the proper function of TDP43 is ensured by strictly controlled nucleocytoplasmic transport, which regulates its expression levels and correct cellular localization [2].
The synergy of the Q331K, M337V, and A382T mutations within the C-terminal glycine-rich domain of TARDBP creates a potent driver of neurodegeneration by fundamentally altering the protein's biophysical properties and cellular localization [3]. Individually, Q331K promotes the formation of toxic C-terminal fragments and disrupts RNA splicing, while M337V accelerates the kinetics of irreversible fibrillization and impairs mitochondrial transport [4]. A382T further exacerbates this pathology by promoting nucleocytoplasmic mislocalization and inducing R-loop-mediated DNA damage [5]. When combined in a humanized model, these mutations act in concert to trigger robust TDP-43 proteinopathy, characterized by the loss of essential nuclear regulatory functions and the gain of cytoplasmic aggregate toxicity. This pathological cascade directly mirrors the clinical progression of ALS and FTD, leading to selective motor neuron loss, cognitive decline, and the formation of phosphorylated inclusions that are hallmarks of the ALS-FTD spectrum.
huTARDBP-Q331K/M337V/A382T was generated by introducing the p.Q331K (CAG to AAG), p.M337V (ATG to GTG), and p.A382T (GCA to ACA) point mutations into exon 6 of the human TARDBP gene in huTARDBP mice (Catalog Number: C001418). This model serves as a valuable tool for studying neurodegenerative diseases, including amyotrophic lateral sclerosis (ALS) and frontotemporal lobar degeneration (FTLD), and can be used to investigate the effects of TDP‑43 protein aggregation in related disorders.
TAR DNA-binding protein 43 (TARDBP/TDP43) is a crucial protein involved in RNA processing, transport, and metabolism. Its aggregation in the cytoplasm is a key pathological feature of several neurodegenerative diseases, including Amyotrophic Lateral Sclerosis (ALS) and Frontotemporal Dementia (FTD). TDP43 is a multifunctional nuclear protein and is the main component of ubiquitin-positive cytoplasmic inclusions found in residual motor neurons of sporadic and familial ALS, with cytoplasmic TDP43 inclusions observed in almost all ALS cases [1]. TDP43 is typically localized in the cell nucleus but can shuttle between the nucleus and cytoplasm to perform various functions, including regulating RNA splicing, transport, and homeostasis. Both cytoplasmic mislocalization and nuclear loss of TDP43 are associated with ALS and FTD, and the proper function of TDP43 is ensured by strictly controlled nucleocytoplasmic transport, which regulates its expression levels and correct cellular localization [2].
The synergy of the Q331K, M337V, and A382T mutations within the C-terminal glycine-rich domain of TARDBP creates a potent driver of neurodegeneration by fundamentally altering the protein's biophysical properties and cellular localization [3]. Individually, Q331K promotes the formation of toxic C-terminal fragments and disrupts RNA splicing, while M337V accelerates the kinetics of irreversible fibrillization and impairs mitochondrial transport [4]. A382T further exacerbates this pathology by promoting nucleocytoplasmic mislocalization and inducing R-loop-mediated DNA damage [5]. When combined in a humanized model, these mutations act in concert to trigger robust TDP-43 proteinopathy, characterized by the loss of essential nuclear regulatory functions and the gain of cytoplasmic aggregate toxicity. This pathological cascade directly mirrors the clinical progression of ALS and FTD, leading to selective motor neuron loss, cognitive decline, and the formation of phosphorylated inclusions that are hallmarks of the ALS-FTD spectrum.
huTARDBP-Q331K/M337V/A382T was generated by introducing the p.Q331K (CAG to AAG), p.M337V (ATG to GTG), and p.A382T (GCA to ACA) point mutations into exon 6 of the human TARDBP gene in huTARDBP mice (Catalog Number: C001418). This model serves as a valuable tool for studying neurodegenerative diseases, including amyotrophic lateral sclerosis (ALS) and frontotemporal lobar degeneration (FTLD), and can be used to investigate the effects of TDP‑43 protein aggregation in related disorders.
Dmgdh-KO
製品ID :
S-KO-23435
系統:
C57BL/6JCya
状況:
説明:
Dmgdh is located on chromosome 13 of mice. Nuclease Technology will be used to design sgRNA; Dmgdh knockout mice will be obtained by applying high-throughput electroporation of fertilized eggs. After sexual maturity, sperm were collected for cryopreservation.
Dmgdh is located on chromosome 13 of mice. Nuclease Technology will be used to design sgRNA; Dmgdh knockout mice will be obtained by applying high-throughput electroporation of fertilized eggs. After sexual maturity, sperm were collected for cryopreservation.
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