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Abcd1 KO
Product ID:
C001777
Strain:
C57BL/6JCya
Status:
Description:
The ABCD1 (ATP-binding cassette subfamily D member 1) gene, located on the X chromosome (Xq28), encodes a peroxisomal transmembrane protein responsible for transporting very long-chain fatty acids (VLCFAs) into peroxisomes for β-oxidation. Widely expressed but particularly prominent in the brain, adrenal glands, and liver, ABCD1 is critical for maintaining lipid homeostasis. Mutations in ABCD1 cause X-linked adrenoleukodystrophy (X-ALD), a neurodegenerative disorder characterized by VLCFA accumulation, demyelination, adrenal insufficiency, and progressive neurological decline. Clinical manifestations vary widely, ranging from asymptomatic carriers to a severe, fatal childhood form. Primarily affecting males (with an estimated incidence of ~1 in 17,000 newborns), X-ALD has been included in newborn screening programs in many U.S. states [1-2]. The correlation between specific mutations and symptoms remains unclear, and VLCFA measurement cannot reliably predict disease-specific outcomes such as adrenal insufficiency or neurological decline. Current therapeutic approaches focus on gene repair or mitigating secondary effects like oxidative stress [3].
The Abcd1 KO mouse, a gene knockout model generated by deleting exon 2 of the mouse Abcd1 gene (homologous to human ABCD1), serves as a valuable tool for studying the pathogenesis of X-ALD and developing therapeutic interventions.
The ABCD1 (ATP-binding cassette subfamily D member 1) gene, located on the X chromosome (Xq28), encodes a peroxisomal transmembrane protein responsible for transporting very long-chain fatty acids (VLCFAs) into peroxisomes for β-oxidation. Widely expressed but particularly prominent in the brain, adrenal glands, and liver, ABCD1 is critical for maintaining lipid homeostasis. Mutations in ABCD1 cause X-linked adrenoleukodystrophy (X-ALD), a neurodegenerative disorder characterized by VLCFA accumulation, demyelination, adrenal insufficiency, and progressive neurological decline. Clinical manifestations vary widely, ranging from asymptomatic carriers to a severe, fatal childhood form. Primarily affecting males (with an estimated incidence of ~1 in 17,000 newborns), X-ALD has been included in newborn screening programs in many U.S. states [1-2]. The correlation between specific mutations and symptoms remains unclear, and VLCFA measurement cannot reliably predict disease-specific outcomes such as adrenal insufficiency or neurological decline. Current therapeutic approaches focus on gene repair or mitigating secondary effects like oxidative stress [3].
The Abcd1 KO mouse, a gene knockout model generated by deleting exon 2 of the mouse Abcd1 gene (homologous to human ABCD1), serves as a valuable tool for studying the pathogenesis of X-ALD and developing therapeutic interventions.
B6-huTFRC/huSNCA(3'UTR)
Product ID:
C001873
Strain:
C57BL/6NCya
Status:
Description:
The Transferrin receptor (TFRC) gene encodes Transferrin Receptor 1 (TFR1), a protein that is expressed at low levels in most normal cells but shows increased expression in highly proliferative cells, such as basal epidermal cells, intestinal epithelium, and certain activated immune cells. Brain capillary endothelial cells, which constitute the blood-brain barrier (BBB), also express this receptor at high levels [1]. TFR1 plays a critical role in maintaining iron metabolism and homeostasis by facilitating receptor-mediated endocytosis of iron-bound transferrin (Tf) via Tf cycling, thereby promoting iron uptake [2]. Cellular iron deficiency can lead to apoptosis, while cellular transformation requires substantial iron to sustain proliferation, with iron overload contributing to tumor progression. The high expression of TFR1 in many tumors makes it a potential tumor marker, offering a target for therapies to inhibit tumor growth and metastasis [1]. Moreover, TFR1 is implicated in anemia and iron metabolism disorders. Studies have shown that elevated TFR1 expression in cardiomyocytes is associated with exacerbated inflammation in myocarditis patients [3]. Various clinical drugs targeting TFR1 are currently under development, including antisense oligonucleotides (ASOs), antibody-drug conjugates (ADCs), and antibody-oligonucleotide conjugates, applicable to diseases such as cancer, anemia, and neurodegenerative disorders. Research indicates that enhancing antibody transport across the blood-brain barrier via TFR1, by forming specific bispecific antibodies with anti-β-amyloid antibodies, can improve therapeutic outcomes in Alzheimer's patients [4-5]. As research progresses, TFR1 is expected to become an effective clinical target for multiple diseases and a synergistic target for drug delivery across the blood-brain barrier (BBB).
Parkinson's disease (PD) is a neurodegenerative disease with a high prevalence mainly in the middle-aged and elderly population. It is the second most common neurodegenerative disease after Alzheimer's disease (AD). The main clinical symptoms include resting tremors, limb stiffness, bradykinesia, loss of voluntary movement, etc. The typical pathological process of PD is the formation of Lewy bodies (LB) in the central nervous system (CNS), which results in the gradual death and loss of dopaminergic neurons, leading to the disease [6-7]. The main components of Lewy bodies are insoluble aggregates of abnormal α-synuclein (α-syn), and the SNCA gene, which encodes α-synuclein, is one of the key causative genes in Parkinson's disease. Mutations in this gene cause overexpression of α-syn, leading to the formation of Lewy bodies, ultimately leading to PD [8]. In addition, SNCA mutations are also associated with diseases such as dementia with Lewy bodies (DLB) and multiple system atrophy (MSA).
B6-huTFRC/huSNCA(3'UTR) mice are a dual-gene humanized model generated by crossing B6-huTFRC mice (Catalog No.: C001860) with B6-hSNCA (3'UTR) mice (Catalog No.: C001698). This model can be used for research on neurodegenerative diseases such as Parkinson's disease (PD), dementia with Lewy bodies (DLB), and multiple system atrophy (MSA), as well as iron metabolism disorders and tumorigenesis and development. It is also applicable for the development of TFRC/SNCA-targeted drugs.
The Transferrin receptor (TFRC) gene encodes Transferrin Receptor 1 (TFR1), a protein that is expressed at low levels in most normal cells but shows increased expression in highly proliferative cells, such as basal epidermal cells, intestinal epithelium, and certain activated immune cells. Brain capillary endothelial cells, which constitute the blood-brain barrier (BBB), also express this receptor at high levels [1]. TFR1 plays a critical role in maintaining iron metabolism and homeostasis by facilitating receptor-mediated endocytosis of iron-bound transferrin (Tf) via Tf cycling, thereby promoting iron uptake [2]. Cellular iron deficiency can lead to apoptosis, while cellular transformation requires substantial iron to sustain proliferation, with iron overload contributing to tumor progression. The high expression of TFR1 in many tumors makes it a potential tumor marker, offering a target for therapies to inhibit tumor growth and metastasis [1]. Moreover, TFR1 is implicated in anemia and iron metabolism disorders. Studies have shown that elevated TFR1 expression in cardiomyocytes is associated with exacerbated inflammation in myocarditis patients [3]. Various clinical drugs targeting TFR1 are currently under development, including antisense oligonucleotides (ASOs), antibody-drug conjugates (ADCs), and antibody-oligonucleotide conjugates, applicable to diseases such as cancer, anemia, and neurodegenerative disorders. Research indicates that enhancing antibody transport across the blood-brain barrier via TFR1, by forming specific bispecific antibodies with anti-β-amyloid antibodies, can improve therapeutic outcomes in Alzheimer's patients [4-5]. As research progresses, TFR1 is expected to become an effective clinical target for multiple diseases and a synergistic target for drug delivery across the blood-brain barrier (BBB).
Parkinson's disease (PD) is a neurodegenerative disease with a high prevalence mainly in the middle-aged and elderly population. It is the second most common neurodegenerative disease after Alzheimer's disease (AD). The main clinical symptoms include resting tremors, limb stiffness, bradykinesia, loss of voluntary movement, etc. The typical pathological process of PD is the formation of Lewy bodies (LB) in the central nervous system (CNS), which results in the gradual death and loss of dopaminergic neurons, leading to the disease [6-7]. The main components of Lewy bodies are insoluble aggregates of abnormal α-synuclein (α-syn), and the SNCA gene, which encodes α-synuclein, is one of the key causative genes in Parkinson's disease. Mutations in this gene cause overexpression of α-syn, leading to the formation of Lewy bodies, ultimately leading to PD [8]. In addition, SNCA mutations are also associated with diseases such as dementia with Lewy bodies (DLB) and multiple system atrophy (MSA).
B6-huTFRC/huSNCA(3'UTR) mice are a dual-gene humanized model generated by crossing B6-huTFRC mice (Catalog No.: C001860) with B6-hSNCA (3'UTR) mice (Catalog No.: C001698). This model can be used for research on neurodegenerative diseases such as Parkinson's disease (PD), dementia with Lewy bodies (DLB), and multiple system atrophy (MSA), as well as iron metabolism disorders and tumorigenesis and development. It is also applicable for the development of TFRC/SNCA-targeted drugs.
B6-hMECP2*T158M
Product ID:
C001569
Strain:
C57BL/6NCya
Status:
Description:
Rett syndrome (RTT) is an X-linked dominant neurodevelopmental disorder primarily affecting female infants and young children, with an incidence of approximately 1 in 10,000 to 15,000 females. Characteristic clinical features include intellectual disability, loss of language skills, stereotypic hand movements, and gait disturbances. Affected individuals typically experience a period of normal development, followed by deceleration in head circumference growth between 6 to 18 months of age, and subsequent regression of acquired motor and cognitive abilities. Overt impairments in cognition and motor function generally emerge within 1 to 2 years. Mutations in the methyl-CpG-binding protein 2 (MECP2) gene are responsible for over 90% of RTT cases. MECP2 is a nuclear protein that binds methylated DNA to modulate gene transcription. MECP2 gene duplications lead to MECP2 duplication syndrome (MDS), while MECP2 deficiency disrupts central nervous system maturation, adversely affecting learning and memory, culminating in the clinical manifestations of RTT.
Current therapeutic strategies for RTT primarily revolve around gene supplementation using adeno-associated virus (AAV) vectors to deliver functional human MECP2 genes to compensate for the endogenous deficiency. However, the substantial size of the MECP2 gene surpasses the packaging capacity of most viral vectors, and overexpression of MECP2 poses a risk of severe neurological complications. These challenges have significantly impeded the progress of gene supplementation therapies. Consequently, the focus has shifted towards DNA/RNA editing approaches aimed at correcting MECP2 mutations and restoring physiological levels of MECP2 protein expression. Notably, several research groups have successfully employed CRISPR-based gene editing technologies to rectify MECP2 mutations in induced pluripotent stem cells (iPSCs) or patient-derived cells ex vivo [1-2]. Given the pivotal role of animal models in preclinical research, the development of humanized mouse models expressing the human MECP2 gene is crucial. These models facilitate the transition of gene therapy candidates—encompassing small nucleic acids, CRISPR-based editors, base editors, and RNA editing technologies—into clinical stages [3-4].
This strain is a humanized MECP2 gene mouse model, generated by replacing the endogenous mouse Mecp2 gene with the human MECP2 gene harboring the T158M mutation through embryonic stem cell targeting techniques. This mutation represents the most common human RTT-associated missense mutation in MECP2. Studies have shown that mice carrying this mutation recapitulate many clinical features of RTT [5].
Rett syndrome (RTT) is an X-linked dominant neurodevelopmental disorder primarily affecting female infants and young children, with an incidence of approximately 1 in 10,000 to 15,000 females. Characteristic clinical features include intellectual disability, loss of language skills, stereotypic hand movements, and gait disturbances. Affected individuals typically experience a period of normal development, followed by deceleration in head circumference growth between 6 to 18 months of age, and subsequent regression of acquired motor and cognitive abilities. Overt impairments in cognition and motor function generally emerge within 1 to 2 years. Mutations in the methyl-CpG-binding protein 2 (MECP2) gene are responsible for over 90% of RTT cases. MECP2 is a nuclear protein that binds methylated DNA to modulate gene transcription. MECP2 gene duplications lead to MECP2 duplication syndrome (MDS), while MECP2 deficiency disrupts central nervous system maturation, adversely affecting learning and memory, culminating in the clinical manifestations of RTT.
Current therapeutic strategies for RTT primarily revolve around gene supplementation using adeno-associated virus (AAV) vectors to deliver functional human MECP2 genes to compensate for the endogenous deficiency. However, the substantial size of the MECP2 gene surpasses the packaging capacity of most viral vectors, and overexpression of MECP2 poses a risk of severe neurological complications. These challenges have significantly impeded the progress of gene supplementation therapies. Consequently, the focus has shifted towards DNA/RNA editing approaches aimed at correcting MECP2 mutations and restoring physiological levels of MECP2 protein expression. Notably, several research groups have successfully employed CRISPR-based gene editing technologies to rectify MECP2 mutations in induced pluripotent stem cells (iPSCs) or patient-derived cells ex vivo [1-2]. Given the pivotal role of animal models in preclinical research, the development of humanized mouse models expressing the human MECP2 gene is crucial. These models facilitate the transition of gene therapy candidates—encompassing small nucleic acids, CRISPR-based editors, base editors, and RNA editing technologies—into clinical stages [3-4].
This strain is a humanized MECP2 gene mouse model, generated by replacing the endogenous mouse Mecp2 gene with the human MECP2 gene harboring the T158M mutation through embryonic stem cell targeting techniques. This mutation represents the most common human RTT-associated missense mutation in MECP2. Studies have shown that mice carrying this mutation recapitulate many clinical features of RTT [5].
B6-hIGHMBP2
Product ID:
C001437
Strain:
C57BL/6NCya
Status:
Description:
The IGHMBP2 (Immunoglobulin mu binding protein 2) gene encodes an ATP-dependent helicase that is expressed throughout the body and contains a helicase structural domain, a single-stranded nucleic acid binding domain, and one zinc finger motif. It is involved in the regulation of DNA replication, mRNA splicing, transcription, and translation. Mutations in IGHMBP2 can lead to two different types of diseases: spinal muscular atrophy with respiratory distress type 1 (SMARD1) and Charcot-Marie-Tooth disease type 2S (CMT2S).
Spinal muscular atrophy with respiratory distress type 1 (SMARD1) is a rare autosomal recessive motor neuron disease, with its main clinical symptom being diaphragmatic paralysis leading to respiratory distress, occurring mostly in infants aged 6 to 12 months. In addition, SMARD1 can also cause severe muscle atrophy that progresses from the distal to the proximal limbs, intrauterine growth retardation, weak crying, and sensory and autonomic nervous system defects [1]. Restrictive cardiomyopathy may be one of the phenotypes of SMARD1 [2]. Charcot-Marie-Tooth disease type 2S (CMT2S) is a rare hereditary neurological disease and is a subtype of Charcot-Marie-Tooth disease type 2 (CMT2). CMT2 is a group of hereditary peripheral neuropathies characterized by abnormal fibers or axons extending from the nerve cell body to muscles or sensory organs, reducing the strength of nerve impulses. The clinical characteristics of CMT2S include symmetrical distal limb weakness and muscle atrophy, with severe peripheral nerve damage.
Currently, ASO drugs and AAV-based gene therapy have emerged in the IGHMBP2-targeted drug pipeline for the treatment of SMARD1 and CMT2. Gene therapy is expected to become one of the most promising treatments for these diseases. However, since most ASO, AAV-based gene therapy, etc., act on the human IGHMBP2 gene, considering the differences between animals and humans in genes, humanizing the mouse gene will help promote the further clinical translation of therapies targeting IGHMBP2. This strain is a mouse Ighmbp2 gene humanized model and can be used for research on SMARD1 and CMT2S. The homozygous B6-hIGHMBP2 mice are viable and fertile. In addition, based on the independently developed TurboKnockout fusion BAC recombination technology, Cyagen can also generate hot mutation models based on this strain and provide customized services for specific mutations to meet the experimental needs in pharmacology and other fields related to SMARD1 and CMT2S.
The IGHMBP2 (Immunoglobulin mu binding protein 2) gene encodes an ATP-dependent helicase that is expressed throughout the body and contains a helicase structural domain, a single-stranded nucleic acid binding domain, and one zinc finger motif. It is involved in the regulation of DNA replication, mRNA splicing, transcription, and translation. Mutations in IGHMBP2 can lead to two different types of diseases: spinal muscular atrophy with respiratory distress type 1 (SMARD1) and Charcot-Marie-Tooth disease type 2S (CMT2S).
Spinal muscular atrophy with respiratory distress type 1 (SMARD1) is a rare autosomal recessive motor neuron disease, with its main clinical symptom being diaphragmatic paralysis leading to respiratory distress, occurring mostly in infants aged 6 to 12 months. In addition, SMARD1 can also cause severe muscle atrophy that progresses from the distal to the proximal limbs, intrauterine growth retardation, weak crying, and sensory and autonomic nervous system defects [1]. Restrictive cardiomyopathy may be one of the phenotypes of SMARD1 [2]. Charcot-Marie-Tooth disease type 2S (CMT2S) is a rare hereditary neurological disease and is a subtype of Charcot-Marie-Tooth disease type 2 (CMT2). CMT2 is a group of hereditary peripheral neuropathies characterized by abnormal fibers or axons extending from the nerve cell body to muscles or sensory organs, reducing the strength of nerve impulses. The clinical characteristics of CMT2S include symmetrical distal limb weakness and muscle atrophy, with severe peripheral nerve damage.
Currently, ASO drugs and AAV-based gene therapy have emerged in the IGHMBP2-targeted drug pipeline for the treatment of SMARD1 and CMT2. Gene therapy is expected to become one of the most promising treatments for these diseases. However, since most ASO, AAV-based gene therapy, etc., act on the human IGHMBP2 gene, considering the differences between animals and humans in genes, humanizing the mouse gene will help promote the further clinical translation of therapies targeting IGHMBP2. This strain is a mouse Ighmbp2 gene humanized model and can be used for research on SMARD1 and CMT2S. The homozygous B6-hIGHMBP2 mice are viable and fertile. In addition, based on the independently developed TurboKnockout fusion BAC recombination technology, Cyagen can also generate hot mutation models based on this strain and provide customized services for specific mutations to meet the experimental needs in pharmacology and other fields related to SMARD1 and CMT2S.
B6-hSNCA (3'UTR)
Product ID:
C001698
Strain:
C57BL/6NCya
Status:
Description:
Parkinson's disease (PD) is a neurodegenerative disease with a high prevalence mainly in the middle-aged and elderly population. It is the second most common neurodegenerative disease after Alzheimer's disease (AD). The main clinical symptoms include resting tremors, limb stiffness, bradykinesia, loss of voluntary movement, etc. The typical pathological process of PD is the formation of Lewy bodies (LB) in the central nervous system (CNS), which results in the gradual death and loss of dopaminergic neurons, leading to the disease [1-2]. The main components of Lewy bodies are insoluble aggregates of abnormal α-synuclein (α-syn), and the SNCA gene, which encodes α-synuclein, is one of the key causative genes in Parkinson's disease. Mutations in this gene cause overexpression of α-syn, leading to Lewy bodies' formation, ultimately leading to PD [3]. In addition, SNCA mutations are also associated with diseases such as dementia with Lewy bodies (DLB) and multiple system atrophy (MSA).
The B6-hSNCA (3'UTR) mouse is a humanized model constructed by replacing the mouse Snca gene in situ with the human SNCA gene, in which the sequences from ATG start codon to downstream of 3'UTR of the endogenous mouse Snca gene are replaced with the sequences from ATG start codon to downstream of 3'UTR of the human SNCA gene. The homozygous B6-hSNCA (3'UTR) mice are viable and fertile and can be used for studies on Parkinson's disease (PD), Dementia with Lewy Bodies (DLB) and Multiple System Atrophy (MSA), and pathogenesis of neurodegenerative diseases, as well as for SNCA-targeted drug development.
Parkinson's disease (PD) is a neurodegenerative disease with a high prevalence mainly in the middle-aged and elderly population. It is the second most common neurodegenerative disease after Alzheimer's disease (AD). The main clinical symptoms include resting tremors, limb stiffness, bradykinesia, loss of voluntary movement, etc. The typical pathological process of PD is the formation of Lewy bodies (LB) in the central nervous system (CNS), which results in the gradual death and loss of dopaminergic neurons, leading to the disease [1-2]. The main components of Lewy bodies are insoluble aggregates of abnormal α-synuclein (α-syn), and the SNCA gene, which encodes α-synuclein, is one of the key causative genes in Parkinson's disease. Mutations in this gene cause overexpression of α-syn, leading to Lewy bodies' formation, ultimately leading to PD [3]. In addition, SNCA mutations are also associated with diseases such as dementia with Lewy bodies (DLB) and multiple system atrophy (MSA).
The B6-hSNCA (3'UTR) mouse is a humanized model constructed by replacing the mouse Snca gene in situ with the human SNCA gene, in which the sequences from ATG start codon to downstream of 3'UTR of the endogenous mouse Snca gene are replaced with the sequences from ATG start codon to downstream of 3'UTR of the human SNCA gene. The homozygous B6-hSNCA (3'UTR) mice are viable and fertile and can be used for studies on Parkinson's disease (PD), Dementia with Lewy Bodies (DLB) and Multiple System Atrophy (MSA), and pathogenesis of neurodegenerative diseases, as well as for SNCA-targeted drug development.
B6-hSNCA
Product ID:
C001427
Strain:
C57BL/6NCya
Status:
Description:
Parkinson's disease (PD) is a degenerative disease of the nervous system that occurs mostly in middle-aged and elderly people and is the second most common neurodegenerative disease after Alzheimer's disease (AD). Clinical symptoms of PD are characterized by resting tremors, limb stiffness, bradykinesia, and lack of voluntary movement. The typical pathology of PD is characterized by the formation of Lewy bodies (LB) in the central nervous system (CNS). This process leads to the progressive death and loss of dopaminergic neurons, ultimately resulting in the development of Parkinson's disease. Lewy bodies are mainly composed of insoluble aggregates of abnormal α-synuclein (α-syn).
The SNCA gene, one of the key pathogenic genes in Parkinson's disease, encodes α-syn. Mutations in SNCA can cause overexpression of α-syn, which leads to the formation of Lewy bodies and ultimately PD. Therefore, the SNCA gene is considered an effective drug target for the treatment of PD [1].
Gene therapy is one of the ways to treat PD, among which the development prospects of SNCA-targeted drugs are particularly prominent. The drug pipelines targeting SNCA are widely laid out, and ASO, siRNA, and CRISPR therapies have emerged [2].
This strain is a mouse Snca gene humanized model and can be used for research on PD. The homozygous B6-hSNCA mice are viable and fertile. Leveraging its proprietary TurboKnockout fusion BAC recombination technology, Cyagen can also generate hot mutation models based on this strain and provide customized services for specific mutations to meet the experimental needs in pharmacology and other fields related to PD.
Parkinson's disease (PD) is a degenerative disease of the nervous system that occurs mostly in middle-aged and elderly people and is the second most common neurodegenerative disease after Alzheimer's disease (AD). Clinical symptoms of PD are characterized by resting tremors, limb stiffness, bradykinesia, and lack of voluntary movement. The typical pathology of PD is characterized by the formation of Lewy bodies (LB) in the central nervous system (CNS). This process leads to the progressive death and loss of dopaminergic neurons, ultimately resulting in the development of Parkinson's disease. Lewy bodies are mainly composed of insoluble aggregates of abnormal α-synuclein (α-syn).
The SNCA gene, one of the key pathogenic genes in Parkinson's disease, encodes α-syn. Mutations in SNCA can cause overexpression of α-syn, which leads to the formation of Lewy bodies and ultimately PD. Therefore, the SNCA gene is considered an effective drug target for the treatment of PD [1].
Gene therapy is one of the ways to treat PD, among which the development prospects of SNCA-targeted drugs are particularly prominent. The drug pipelines targeting SNCA are widely laid out, and ASO, siRNA, and CRISPR therapies have emerged [2].
This strain is a mouse Snca gene humanized model and can be used for research on PD. The homozygous B6-hSNCA mice are viable and fertile. Leveraging its proprietary TurboKnockout fusion BAC recombination technology, Cyagen can also generate hot mutation models based on this strain and provide customized services for specific mutations to meet the experimental needs in pharmacology and other fields related to PD.
B6-hTARDBP
Product ID:
C001418
Strain:
C57BL/6JCya
Status:
Description:
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.
B6-hMECP2
Product ID:
C001568
Strain:
C57BL/6NCya
Status:
Description:
Rett syndrome (RTT) is an X-linked dominant neurodevelopmental disorder that occurs predominantly in female infants and young children. The incidence is approximately 1 in 10,000–15,000 females. Clinical features include intellectual disability, loss of language function, stereotyped hand movements, and gait abnormalities. Affected children typically have a period of normal development followed by stagnation of head circumference growth at 6–18 months of age, and regression of acquired skills. Overt cognitive and motor impairments develop 1–2 years later. Mutations in the methyl-CpG-binding protein 2 (MECP2) gene account for >90% of RTT cases. MECP2 is a nuclear protein that binds to methylated DNA to regulate gene transcription. MECP2 duplications cause MECP2 duplication syndrome (MDS), while functional deficiency of MECP2 impairs the production of this nuclear protein, leading to central nervous system functional maturation disorders that affect learning and memory functions, resulting in RTT.
Treatment for RTT focuses mainly on gene supplementation therapy based on adeno-associated virus (AAV) vectors. This involves delivering human MECP2 genes via AAV vectors to compensate for the deficiency of MECP2 genes in patients. However, the large size of the MECP2 gene exceeds the delivery capacity of most vectors, and over-expression of the MECP2 gene can also lead to serious neurological diseases. These limitations have hindered the development of this therapy. Therefore, DNA/RNA editing to repair MECP2 gene mutations and restore normal expression of MECP2 protein has received widespread attention. Currently, multiple research groups have used CRISPR-based gene editing technology to repair mutations in the MECP2 gene in induced pluripotent stem cells (iPSCs) or ex vivo patient cells [1-2]. Animal studies are an essential part of preclinical research. RTT therapies based on small nucleic acids, CRISPR gene editing technology, base editors, and RNA editing technology target the human MECP2 gene. Humanized mouse models can help advance gene therapy drug pipelines into clinical stages [3-4].
This strain is a humanized MECP2 gene mouse model that can be used for RTT research. Homozygous B6-hMECP2 mice are viable and fertile. Additionally, based on the independently developed TurboKnockout fusion BAC recombination technology, Cyagen can also generate hot mutation models based on this strain (B6-hMECP2*T158M, Catalog Number: C001569) and provide customized services for specific mutations to meet experimental needs in pharmacology and other RTT-related fields.
Rett syndrome (RTT) is an X-linked dominant neurodevelopmental disorder that occurs predominantly in female infants and young children. The incidence is approximately 1 in 10,000–15,000 females. Clinical features include intellectual disability, loss of language function, stereotyped hand movements, and gait abnormalities. Affected children typically have a period of normal development followed by stagnation of head circumference growth at 6–18 months of age, and regression of acquired skills. Overt cognitive and motor impairments develop 1–2 years later. Mutations in the methyl-CpG-binding protein 2 (MECP2) gene account for >90% of RTT cases. MECP2 is a nuclear protein that binds to methylated DNA to regulate gene transcription. MECP2 duplications cause MECP2 duplication syndrome (MDS), while functional deficiency of MECP2 impairs the production of this nuclear protein, leading to central nervous system functional maturation disorders that affect learning and memory functions, resulting in RTT.
Treatment for RTT focuses mainly on gene supplementation therapy based on adeno-associated virus (AAV) vectors. This involves delivering human MECP2 genes via AAV vectors to compensate for the deficiency of MECP2 genes in patients. However, the large size of the MECP2 gene exceeds the delivery capacity of most vectors, and over-expression of the MECP2 gene can also lead to serious neurological diseases. These limitations have hindered the development of this therapy. Therefore, DNA/RNA editing to repair MECP2 gene mutations and restore normal expression of MECP2 protein has received widespread attention. Currently, multiple research groups have used CRISPR-based gene editing technology to repair mutations in the MECP2 gene in induced pluripotent stem cells (iPSCs) or ex vivo patient cells [1-2]. Animal studies are an essential part of preclinical research. RTT therapies based on small nucleic acids, CRISPR gene editing technology, base editors, and RNA editing technology target the human MECP2 gene. Humanized mouse models can help advance gene therapy drug pipelines into clinical stages [3-4].
This strain is a humanized MECP2 gene mouse model that can be used for RTT research. Homozygous B6-hMECP2 mice are viable and fertile. Additionally, based on the independently developed TurboKnockout fusion BAC recombination technology, Cyagen can also generate hot mutation models based on this strain (B6-hMECP2*T158M, Catalog Number: C001569) and provide customized services for specific mutations to meet experimental needs in pharmacology and other RTT-related fields.
B6-hTFRC/hDMD (E8-30)
Product ID:
C001596
Strain:
C57BL/6NCya
Status:
Description:
The Transferrin receptor (TFRC) gene encodes Transferrin Receptor 1 (TFR1), a protein that is expressed at low levels in most normal cells but shows increased expression in highly proliferative cells, such as basal epidermal cells, intestinal epithelium, and certain activated immune cells. Brain capillary endothelial cells, which constitute the blood-brain barrier (BBB), also express this receptor at high levels [1]. TFR1 plays a critical role in maintaining iron metabolism and homeostasis by facilitating receptor-mediated endocytosis of iron-bound transferrin (Tf) via Tf cycling, thereby promoting iron uptake [2]. Cellular iron deficiency can lead to apoptosis, while cellular transformation requires substantial iron to sustain proliferation, with iron overload contributing to tumor progression. The high expression of TFR1 in many tumors makes it a potential tumor marker, offering a target for therapies to inhibit tumor growth and metastasis [1]. Moreover, TFR1 is implicated in anemia and iron metabolism disorders. Studies have shown that elevated TFR1 expression in cardiomyocytes is associated with exacerbated inflammation in myocarditis patients [3]. Various clinical drugs targeting TFR1 are currently under development, including antisense oligonucleotides (ASOs), antibody-drug conjugates (ADCs), and antibody-oligonucleotide conjugates, applicable to diseases such as cancer, anemia, and neurodegenerative disorders. Research indicates that enhancing antibody transport across the blood-brain barrier via TFR1, by forming specific bispecific antibodies with anti-β-amyloid antibodies, can improve therapeutic outcomes in Alzheimer's patients [4-5]. As research progresses, TFR1 is expected to become an effective clinical target for multiple diseases and a synergistic target for drug delivery across the blood-brain barrier (BBB).
Duchenne Muscular Dystrophy (DMD) is a severe, progressive, and disabling X-linked recessive genetic disorder characterized primarily by muscle atrophy. This disease leads to motor impairments, eventually requiring assisted ventilation, and often results in premature death. The primary cause of DMD is mutations in the DMD gene, which encodes the dystrophin protein. These mutations lead to a reduction or absence of dystrophin in muscle tissue, resulting in muscle atrophy and related complications [6]. The lack of dystrophin leads to the breakdown of the dystrophin-associated protein complex (DAPC) within the muscle membrane, disrupting the interaction between actin and the extracellular matrix, and making the muscles more susceptible to damage. This susceptibility results in the gradual loss of muscle tissue and function, potentially leading to cardiomyopathy [7]. Researchers have identified thousands of different DMD gene mutations in patients with DMD. Deletion mutations account for approximately 60%–70%, while duplication mutations account for 5%–15%. These mutations are primarily concentrated in hotspot regions of the DMD gene, specifically between exons 45-55 (47%) and exons 3-9 (7%) [6].
The B6-hTFRC/hDMD(E8-30) mouse model is a humanized model obtained by breeding B6-hTFRC(CDS) mice (Catalog No.: C001584) with B6-hDMD(E8-30) mice (Catalog No.: I001224). This model can be used for research on iron metabolism disorders, Duchenne muscular dystrophy (DMD), neurodegenerative diseases, and tumor development, aiding in the research of TFRC/DMD-targeted drugs.
The Transferrin receptor (TFRC) gene encodes Transferrin Receptor 1 (TFR1), a protein that is expressed at low levels in most normal cells but shows increased expression in highly proliferative cells, such as basal epidermal cells, intestinal epithelium, and certain activated immune cells. Brain capillary endothelial cells, which constitute the blood-brain barrier (BBB), also express this receptor at high levels [1]. TFR1 plays a critical role in maintaining iron metabolism and homeostasis by facilitating receptor-mediated endocytosis of iron-bound transferrin (Tf) via Tf cycling, thereby promoting iron uptake [2]. Cellular iron deficiency can lead to apoptosis, while cellular transformation requires substantial iron to sustain proliferation, with iron overload contributing to tumor progression. The high expression of TFR1 in many tumors makes it a potential tumor marker, offering a target for therapies to inhibit tumor growth and metastasis [1]. Moreover, TFR1 is implicated in anemia and iron metabolism disorders. Studies have shown that elevated TFR1 expression in cardiomyocytes is associated with exacerbated inflammation in myocarditis patients [3]. Various clinical drugs targeting TFR1 are currently under development, including antisense oligonucleotides (ASOs), antibody-drug conjugates (ADCs), and antibody-oligonucleotide conjugates, applicable to diseases such as cancer, anemia, and neurodegenerative disorders. Research indicates that enhancing antibody transport across the blood-brain barrier via TFR1, by forming specific bispecific antibodies with anti-β-amyloid antibodies, can improve therapeutic outcomes in Alzheimer's patients [4-5]. As research progresses, TFR1 is expected to become an effective clinical target for multiple diseases and a synergistic target for drug delivery across the blood-brain barrier (BBB).
Duchenne Muscular Dystrophy (DMD) is a severe, progressive, and disabling X-linked recessive genetic disorder characterized primarily by muscle atrophy. This disease leads to motor impairments, eventually requiring assisted ventilation, and often results in premature death. The primary cause of DMD is mutations in the DMD gene, which encodes the dystrophin protein. These mutations lead to a reduction or absence of dystrophin in muscle tissue, resulting in muscle atrophy and related complications [6]. The lack of dystrophin leads to the breakdown of the dystrophin-associated protein complex (DAPC) within the muscle membrane, disrupting the interaction between actin and the extracellular matrix, and making the muscles more susceptible to damage. This susceptibility results in the gradual loss of muscle tissue and function, potentially leading to cardiomyopathy [7]. Researchers have identified thousands of different DMD gene mutations in patients with DMD. Deletion mutations account for approximately 60%–70%, while duplication mutations account for 5%–15%. These mutations are primarily concentrated in hotspot regions of the DMD gene, specifically between exons 45-55 (47%) and exons 3-9 (7%) [6].
The B6-hTFRC/hDMD(E8-30) mouse model is a humanized model obtained by breeding B6-hTFRC(CDS) mice (Catalog No.: C001584) with B6-hDMD(E8-30) mice (Catalog No.: I001224). This model can be used for research on iron metabolism disorders, Duchenne muscular dystrophy (DMD), neurodegenerative diseases, and tumor development, aiding in the research of TFRC/DMD-targeted drugs.
B6-hTFRC/hDMD (E49-53)
Product ID:
C001595
Strain:
C57BL/6NCya
Status:
Description:
The Transferrin receptor (TFRC) gene encodes Transferrin Receptor 1 (TFR1), a protein that is expressed at low levels in most normal cells but shows increased expression in highly proliferative cells, such as basal epidermal cells, intestinal epithelium, and certain activated immune cells. Brain capillary endothelial cells, which constitute the blood-brain barrier (BBB), also express this receptor at high levels [1]. TFR1 plays a critical role in maintaining iron metabolism and homeostasis by facilitating receptor-mediated endocytosis of iron-bound transferrin (Tf) via Tf cycling, thereby promoting iron uptake [2]. Cellular iron deficiency can lead to apoptosis, while cellular transformation requires substantial iron to sustain proliferation, with iron overload contributing to tumor progression. The high expression of TFR1 in many tumors makes it a potential tumor marker, offering a target for therapies to inhibit tumor growth and metastasis [1]. Moreover, TFR1 is implicated in anemia and iron metabolism disorders. Studies have shown that elevated TFR1 expression in cardiomyocytes is associated with exacerbated inflammation in myocarditis patients [3]. Various clinical drugs targeting TFR1 are currently under development, including antisense oligonucleotides (ASOs), antibody-drug conjugates (ADCs), and antibody-oligonucleotide conjugates, applicable to diseases such as cancer, anemia, and neurodegenerative disorders. Research indicates that enhancing antibody transport across the blood-brain barrier via TFR1, by forming specific bispecific antibodies with anti-β-amyloid antibodies, can improve therapeutic outcomes in Alzheimer's patients [4-5]. As research progresses, TFR1 is expected to become an effective clinical target for multiple diseases and a synergistic target for drug delivery across the blood-brain barrier (BBB).
Duchenne Muscular Dystrophy (DMD) is a severe, progressive, and disabling X-linked recessive genetic disorder characterized primarily by muscle atrophy. This disease leads to motor impairments, eventually requiring assisted ventilation, and often results in premature death. The primary cause of DMD is mutations in the DMD gene, which encodes the dystrophin protein. These mutations lead to a reduction or absence of dystrophin in muscle tissue, resulting in muscle atrophy and related complications [6]. The lack of dystrophin leads to the breakdown of the dystrophin-associated protein complex (DAPC) within the muscle membrane, disrupting the interaction between actin and the extracellular matrix, and making the muscles more susceptible to damage. This susceptibility results in the gradual loss of muscle tissue and function, potentially leading to cardiomyopathy [7]. Researchers have identified thousands of different DMD gene mutations in patients with DMD. Deletion mutations account for approximately 60%–70%, while duplication mutations account for 5%–15%. These mutations are primarily concentrated in hotspot regions of the DMD gene, specifically between exons 45-55 (47%) and exons 3-9 (7%) [6].
The B6-hTFRC/hDMD(E49-53) mouse model is a humanized model obtained by breeding B6-hTFRC(CDS) mice (Product No.: C001584) with B6-hDMD(E49-53) mice (Product No.: C001775). This model can be used for research on iron metabolism disorders, Duchenne muscular dystrophy (DMD), neurodegenerative diseases, and tumor development, aiding in the research of TFRC/DMD-targeted drugs.
The Transferrin receptor (TFRC) gene encodes Transferrin Receptor 1 (TFR1), a protein that is expressed at low levels in most normal cells but shows increased expression in highly proliferative cells, such as basal epidermal cells, intestinal epithelium, and certain activated immune cells. Brain capillary endothelial cells, which constitute the blood-brain barrier (BBB), also express this receptor at high levels [1]. TFR1 plays a critical role in maintaining iron metabolism and homeostasis by facilitating receptor-mediated endocytosis of iron-bound transferrin (Tf) via Tf cycling, thereby promoting iron uptake [2]. Cellular iron deficiency can lead to apoptosis, while cellular transformation requires substantial iron to sustain proliferation, with iron overload contributing to tumor progression. The high expression of TFR1 in many tumors makes it a potential tumor marker, offering a target for therapies to inhibit tumor growth and metastasis [1]. Moreover, TFR1 is implicated in anemia and iron metabolism disorders. Studies have shown that elevated TFR1 expression in cardiomyocytes is associated with exacerbated inflammation in myocarditis patients [3]. Various clinical drugs targeting TFR1 are currently under development, including antisense oligonucleotides (ASOs), antibody-drug conjugates (ADCs), and antibody-oligonucleotide conjugates, applicable to diseases such as cancer, anemia, and neurodegenerative disorders. Research indicates that enhancing antibody transport across the blood-brain barrier via TFR1, by forming specific bispecific antibodies with anti-β-amyloid antibodies, can improve therapeutic outcomes in Alzheimer's patients [4-5]. As research progresses, TFR1 is expected to become an effective clinical target for multiple diseases and a synergistic target for drug delivery across the blood-brain barrier (BBB).
Duchenne Muscular Dystrophy (DMD) is a severe, progressive, and disabling X-linked recessive genetic disorder characterized primarily by muscle atrophy. This disease leads to motor impairments, eventually requiring assisted ventilation, and often results in premature death. The primary cause of DMD is mutations in the DMD gene, which encodes the dystrophin protein. These mutations lead to a reduction or absence of dystrophin in muscle tissue, resulting in muscle atrophy and related complications [6]. The lack of dystrophin leads to the breakdown of the dystrophin-associated protein complex (DAPC) within the muscle membrane, disrupting the interaction between actin and the extracellular matrix, and making the muscles more susceptible to damage. This susceptibility results in the gradual loss of muscle tissue and function, potentially leading to cardiomyopathy [7]. Researchers have identified thousands of different DMD gene mutations in patients with DMD. Deletion mutations account for approximately 60%–70%, while duplication mutations account for 5%–15%. These mutations are primarily concentrated in hotspot regions of the DMD gene, specifically between exons 45-55 (47%) and exons 3-9 (7%) [6].
The B6-hTFRC/hDMD(E49-53) mouse model is a humanized model obtained by breeding B6-hTFRC(CDS) mice (Product No.: C001584) with B6-hDMD(E49-53) mice (Product No.: C001775). This model can be used for research on iron metabolism disorders, Duchenne muscular dystrophy (DMD), neurodegenerative diseases, and tumor development, aiding in the research of TFRC/DMD-targeted drugs.
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