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Alb-Cre+/hMYC-IRES-EGFP+
Product ID:
C001339
Strain:
C57BL/6JCya
Status:
Description:
The MYC oncogene family comprises regulatory genes and proto-oncogenes that encode transcription factors, involved in various cellular processes such as the cell cycle, apoptosis, DNA repair, and metabolism. Members include c-Myc (MYC), l-Myc (MYCL), and n-Myc (MYCN). c-Myc (MYC) is a basic helix-loop-helix leucine zipper (bHLHZip) transcription factor, which forms heterodimers with Max protein to bind DNA and regulate the expression of approximately 15% of genes, thereby participating in key cellular processes such as cell proliferation, apoptosis, DNA repair, and metabolism. In many cancers, c-Myc is overexpressed, leading to uncontrolled cell proliferation and tumor growth, such as in Burkitt's lymphoma where c-Myc gene rearrangement is common. Dysregulation of the MYC oncogene plays a crucial role in tumorigenesis, predominantly through transcriptional dysregulation resulting in overexpression of c-Myc protein.
Alb-Cre+/hMYC-IRES-EGFP+ mice are generated by crossing H11-CAG-LSL-hMYC-IRES-EGFP mice (Catalog Number: C001338), which conditionally express the human c-Myc oncogene, with Alb-Cre mice that express Cre recombinase specifically in hepatocytes under the control of the Alb promoter. The Cre-mediated recombination results in the deletion of the transcriptional stop sequence (Loxp-Stop-Loxp, LSL) in H11-CAG-LSL-hMYC-IRES-EGFP mice, leading to overexpression of the MYC oncogene in the liver and subsequent carcinogenesis. This model, therefore, spontaneously develops liver cancer with an early onset.
The MYC oncogene family comprises regulatory genes and proto-oncogenes that encode transcription factors, involved in various cellular processes such as the cell cycle, apoptosis, DNA repair, and metabolism. Members include c-Myc (MYC), l-Myc (MYCL), and n-Myc (MYCN). c-Myc (MYC) is a basic helix-loop-helix leucine zipper (bHLHZip) transcription factor, which forms heterodimers with Max protein to bind DNA and regulate the expression of approximately 15% of genes, thereby participating in key cellular processes such as cell proliferation, apoptosis, DNA repair, and metabolism. In many cancers, c-Myc is overexpressed, leading to uncontrolled cell proliferation and tumor growth, such as in Burkitt's lymphoma where c-Myc gene rearrangement is common. Dysregulation of the MYC oncogene plays a crucial role in tumorigenesis, predominantly through transcriptional dysregulation resulting in overexpression of c-Myc protein.
Alb-Cre+/hMYC-IRES-EGFP+ mice are generated by crossing H11-CAG-LSL-hMYC-IRES-EGFP mice (Catalog Number: C001338), which conditionally express the human c-Myc oncogene, with Alb-Cre mice that express Cre recombinase specifically in hepatocytes under the control of the Alb promoter. The Cre-mediated recombination results in the deletion of the transcriptional stop sequence (Loxp-Stop-Loxp, LSL) in H11-CAG-LSL-hMYC-IRES-EGFP mice, leading to overexpression of the MYC oncogene in the liver and subsequent carcinogenesis. This model, therefore, spontaneously develops liver cancer with an early onset.
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.
Abca4/Rdh8-DKO
Product ID:
C001968
Strain:
C57BL/6JCya
Status:
Description:
The Abca4/Rdh8-DKO mouse is a dual-gene knockout model obtained by mating Rdh8-KO mice (catalog No.: C001969) with Abca4-KO mice (catalog No.: C002024). This model can be used to investigate the pathogenic mechanisms and therapeutic strategies of diseases, including Stargardt disease (STGD) and age‑related macular degeneration (AMD), and facilitates the evaluation of synergistic effects of polygenic therapies.
The Abca4/Rdh8-DKO mouse is a dual-gene knockout model obtained by mating Rdh8-KO mice (catalog No.: C001969) with Abca4-KO mice (catalog No.: C002024). This model can be used to investigate the pathogenic mechanisms and therapeutic strategies of diseases, including Stargardt disease (STGD) and age‑related macular degeneration (AMD), and facilitates the evaluation of synergistic effects of polygenic therapies.
B6-hLPA (CKI) /Alb-cre
Product ID:
C001522
Strain:
C57BL/6NCya
Status:
Description:
Lipoprotein A (LPA) is a type of particle similar to low-density lipoprotein (LDL) that is considered one of the risk factors for cardiovascular disease (CVD), such as atherosclerosis, coronary heart disease, stroke, etc [1]. LP(a) is similar in size and lipid content to LDL (low-density lipoprotein) and also contains the lipoprotein ApoB-100. However, unlike LDL, LP(a) additionally contains a variable-length lipoprotein called Apo(a), which covalently binds to ApoB-100 through a single disulfide bond. LP(a) plays an important role in systemic lipid transport, guiding inflammatory cells into blood vessel walls and leading to smooth muscle cell proliferation. Furthermore, it is involved in wound healing and tissue repair, interacting with the components of blood vessel walls and the extracellular matrix [2]. However, LP(a) can also cause arterial narrowing by adhering to the arterial wall, accelerating the formation of blood clots, and thereby triggering a series of pathological changes related to coronary heart disease, cardiovascular disease, atherosclerosis, thrombus formation, and stroke [3].
The plasma concentration of LP(a) is closely related to genetic factors and is primarily regulated by the LPA gene. Therefore, the LPA gene is an important potential target for cardiovascular disease treatment. The LPA gene encodes a serine protease that inhibits the activity of tissue-type plasminogen activator I. Fragments of this protein, generated through protein hydrolysis, can adhere to atherosclerotic lesions in arteries, promoting blood clot formation. The LPA gene is expressed in both humans and non-human primates but is not expressed in mice. Constructing mouse models expressing the human LPA gene is of significant importance for developing lipid-lowering drugs, which can drive the development of novel therapies for cardiovascular diseases. Currently, various novel therapies targeting the transcription rate of the LPA gene are under development, including small interfering RNA (siRNA) and antisense oligonucleotides (ASO) [4].
This strain was generated by mating B6-hLPA(CKI) mice (catalog number: C001521) with Alb-Cre mice (liver-specific Cre-expressing mice), resulting in a mouse model with liver-specific overexpression of the human LPA gene. B6-hLPA(CKI)/Alb-cre mice can be used to study the relationship between the LPA gene and hyperlipidemia and related cardiovascular diseases.
Lipoprotein A (LPA) is a type of particle similar to low-density lipoprotein (LDL) that is considered one of the risk factors for cardiovascular disease (CVD), such as atherosclerosis, coronary heart disease, stroke, etc [1]. LP(a) is similar in size and lipid content to LDL (low-density lipoprotein) and also contains the lipoprotein ApoB-100. However, unlike LDL, LP(a) additionally contains a variable-length lipoprotein called Apo(a), which covalently binds to ApoB-100 through a single disulfide bond. LP(a) plays an important role in systemic lipid transport, guiding inflammatory cells into blood vessel walls and leading to smooth muscle cell proliferation. Furthermore, it is involved in wound healing and tissue repair, interacting with the components of blood vessel walls and the extracellular matrix [2]. However, LP(a) can also cause arterial narrowing by adhering to the arterial wall, accelerating the formation of blood clots, and thereby triggering a series of pathological changes related to coronary heart disease, cardiovascular disease, atherosclerosis, thrombus formation, and stroke [3].
The plasma concentration of LP(a) is closely related to genetic factors and is primarily regulated by the LPA gene. Therefore, the LPA gene is an important potential target for cardiovascular disease treatment. The LPA gene encodes a serine protease that inhibits the activity of tissue-type plasminogen activator I. Fragments of this protein, generated through protein hydrolysis, can adhere to atherosclerotic lesions in arteries, promoting blood clot formation. The LPA gene is expressed in both humans and non-human primates but is not expressed in mice. Constructing mouse models expressing the human LPA gene is of significant importance for developing lipid-lowering drugs, which can drive the development of novel therapies for cardiovascular diseases. Currently, various novel therapies targeting the transcription rate of the LPA gene are under development, including small interfering RNA (siRNA) and antisense oligonucleotides (ASO) [4].
This strain was generated by mating B6-hLPA(CKI) mice (catalog number: C001521) with Alb-Cre mice (liver-specific Cre-expressing mice), resulting in a mouse model with liver-specific overexpression of the human LPA gene. B6-hLPA(CKI)/Alb-cre mice can be used to study the relationship between the LPA gene and hyperlipidemia and related cardiovascular diseases.
B6-hLPA (CKI)
Product ID:
C001521
Strain:
C57BL/6NCya
Status:
Description:
Lipoprotein A (LPA) is a type of particle similar to low-density lipoprotein (LDL) that is considered one of the risk factors for cardiovascular disease (CVD) such as atherosclerosis, coronary heart disease, stroke, etc [1]. LP(a) is similar in size and lipid content to LDL (low-density lipoprotein) and contains the lipoprotein ApoB-100. However, unlike LDL, LP(a) contains a variable-length lipoprotein called Apo(a), which covalently binds to ApoB-100 through a single disulfide bond. LP(a) plays an important role in systemic lipid transport, guiding inflammatory cells into blood vessel walls and leading to smooth muscle cell proliferation. Furthermore, it is involved in wound healing and tissue repair, interacting with the components of blood vessel walls and the extracellular matrix [2]. However, LP(a) can also cause arterial narrowing by adhering to the arterial wall, accelerating the formation of blood clots, and thereby triggering a series of pathological changes related to coronary heart disease, cardiovascular disease, atherosclerosis, thrombus formation, and stroke [3].
The plasma concentration of LP(a) is closely related to genetic factors and is primarily regulated by the LPA gene. Therefore, the LPA gene is an important potential target for cardiovascular disease treatment. The LPA gene encodes a serine protease that inhibits the activity of tissue-type plasminogen activator I. Fragments of this protein, generated through protein hydrolysis, can adhere to atherosclerotic lesions in arteries, promoting blood clot formation. The LPA gene is expressed in both humans and non-human primates but is not expressed in mice. Constructing mouse models expressing the human LPA gene is of significant importance for developing lipid-lowering drugs, which can drive the development of novel therapies for cardiovascular diseases. Currently, various novel therapies targeting the transcription rate of the LPA gene are under development, including small interfering RNA (siRNA) and antisense oligonucleotides (ASO) [4].
This strain was a conditional mouse model expressing the human LPA gene, where the ‘loxP-Stop-loxP-hLPA’ sequence was inserted into the intron 1 of the ROSA26 safe harbor locus. When this model is bred with tool mice expressing Cre recombinase, sequence recombination occurs in the Cre-positive cells and tissues of the offspring mice. After the Cre-recombinase-mediated deletion of the stop element (LSL), specific expression of the human LPA gene can be achieved. The B6-hLPA(CKI) mice can be used for research related to atherosclerosis, and thrombotic cardiovascular diseases, as well as the development, screening, and preclinical evaluation of human LPA gene-targeted drugs.
Lipoprotein A (LPA) is a type of particle similar to low-density lipoprotein (LDL) that is considered one of the risk factors for cardiovascular disease (CVD) such as atherosclerosis, coronary heart disease, stroke, etc [1]. LP(a) is similar in size and lipid content to LDL (low-density lipoprotein) and contains the lipoprotein ApoB-100. However, unlike LDL, LP(a) contains a variable-length lipoprotein called Apo(a), which covalently binds to ApoB-100 through a single disulfide bond. LP(a) plays an important role in systemic lipid transport, guiding inflammatory cells into blood vessel walls and leading to smooth muscle cell proliferation. Furthermore, it is involved in wound healing and tissue repair, interacting with the components of blood vessel walls and the extracellular matrix [2]. However, LP(a) can also cause arterial narrowing by adhering to the arterial wall, accelerating the formation of blood clots, and thereby triggering a series of pathological changes related to coronary heart disease, cardiovascular disease, atherosclerosis, thrombus formation, and stroke [3].
The plasma concentration of LP(a) is closely related to genetic factors and is primarily regulated by the LPA gene. Therefore, the LPA gene is an important potential target for cardiovascular disease treatment. The LPA gene encodes a serine protease that inhibits the activity of tissue-type plasminogen activator I. Fragments of this protein, generated through protein hydrolysis, can adhere to atherosclerotic lesions in arteries, promoting blood clot formation. The LPA gene is expressed in both humans and non-human primates but is not expressed in mice. Constructing mouse models expressing the human LPA gene is of significant importance for developing lipid-lowering drugs, which can drive the development of novel therapies for cardiovascular diseases. Currently, various novel therapies targeting the transcription rate of the LPA gene are under development, including small interfering RNA (siRNA) and antisense oligonucleotides (ASO) [4].
This strain was a conditional mouse model expressing the human LPA gene, where the ‘loxP-Stop-loxP-hLPA’ sequence was inserted into the intron 1 of the ROSA26 safe harbor locus. When this model is bred with tool mice expressing Cre recombinase, sequence recombination occurs in the Cre-positive cells and tissues of the offspring mice. After the Cre-recombinase-mediated deletion of the stop element (LSL), specific expression of the human LPA gene can be achieved. The B6-hLPA(CKI) mice can be used for research related to atherosclerosis, and thrombotic cardiovascular diseases, as well as the development, screening, and preclinical evaluation of human LPA gene-targeted drugs.
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-hTTR
Product ID:
C001512
Strain:
C57BL/6NCya
Status:
Description:
Transthyretin amyloidosis (ATTR) is a protein disorder caused by the abnormal accumulation of misfolded transthyretin (TTR) protein in organs and tissues throughout the body, primarily affecting the peripheral nervous system and heart [1]. ATTR can be divided into hereditary ATTR and wild-type ATTR, with hereditary ATTR being caused by genetic mutations in the TTR gene.
The TTR gene encodes transthyretin (TTR), also known as prealbumin, which is mainly synthesized in the liver and to a lesser extent in the brain’s choroid plexus or ocular photoreceptor tissue (such as the retina). TTR is a transport protein that exists as a homotetramer in peripheral blood under normal physiological conditions and participates in the transport of thyroxine and retinol-binding protein. Mutations in the TTR gene can lead to hereditary familial amyloidosis, such as Transthyretin Cardiac Amyloidosis Myocardiopathy (ATTR-CM) and Transthyretin Amyloid Polyneuropathy (ATTR-PN). The pathogenic mechanism is that structurally unstable TTR protein tetramers develop into pathological aggregates in tissues such as the peripheral nervous system, heart, eyes, kidneys, and meninges, forming insoluble amyloid deposits, eventually leading to ATTR.
The treatments for ATTR-CM and ATTR-PN mainly involve inhibiting the production of mutant TTR mRNA or stabilizing the structure of TTR protein tetramers. At present, various drug pipelines have emerged in the field of gene therapy targeting the TTR gene, including ASO, siRNA, and CRISPR-based gene therapies. Among them, Inotersen Sodium, developed by Ionis, the leading oligonucleic acid drug (ASO) therapy company, is the first approved ASO drug for this disease. It targets the conserved sequence of the 3’ untranslated region (UTR) of TTR mRNA to induce mRNA degradation and reduce TTR synthesis in liver cells [2]. Since most ASO, siRNA, and CRISPR-based therapies target human TTR genes, considering the differences between animals and humans at the genetic level, humanizing mouse genes will help advance gene therapy drug pipelines into clinical stages. This strain is a mouse Ttr gene humanized model and can be used for research on transthyretin amyloidosis. The homozygous B6-hTTR mice are viable and fertile [3-6]. Additionally, 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 experimental needs in pharmacology.
Transthyretin amyloidosis (ATTR) is a protein disorder caused by the abnormal accumulation of misfolded transthyretin (TTR) protein in organs and tissues throughout the body, primarily affecting the peripheral nervous system and heart [1]. ATTR can be divided into hereditary ATTR and wild-type ATTR, with hereditary ATTR being caused by genetic mutations in the TTR gene.
The TTR gene encodes transthyretin (TTR), also known as prealbumin, which is mainly synthesized in the liver and to a lesser extent in the brain’s choroid plexus or ocular photoreceptor tissue (such as the retina). TTR is a transport protein that exists as a homotetramer in peripheral blood under normal physiological conditions and participates in the transport of thyroxine and retinol-binding protein. Mutations in the TTR gene can lead to hereditary familial amyloidosis, such as Transthyretin Cardiac Amyloidosis Myocardiopathy (ATTR-CM) and Transthyretin Amyloid Polyneuropathy (ATTR-PN). The pathogenic mechanism is that structurally unstable TTR protein tetramers develop into pathological aggregates in tissues such as the peripheral nervous system, heart, eyes, kidneys, and meninges, forming insoluble amyloid deposits, eventually leading to ATTR.
The treatments for ATTR-CM and ATTR-PN mainly involve inhibiting the production of mutant TTR mRNA or stabilizing the structure of TTR protein tetramers. At present, various drug pipelines have emerged in the field of gene therapy targeting the TTR gene, including ASO, siRNA, and CRISPR-based gene therapies. Among them, Inotersen Sodium, developed by Ionis, the leading oligonucleic acid drug (ASO) therapy company, is the first approved ASO drug for this disease. It targets the conserved sequence of the 3’ untranslated region (UTR) of TTR mRNA to induce mRNA degradation and reduce TTR synthesis in liver cells [2]. Since most ASO, siRNA, and CRISPR-based therapies target human TTR genes, considering the differences between animals and humans at the genetic level, humanizing mouse genes will help advance gene therapy drug pipelines into clinical stages. This strain is a mouse Ttr gene humanized model and can be used for research on transthyretin amyloidosis. The homozygous B6-hTTR mice are viable and fertile [3-6]. Additionally, 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 experimental needs in pharmacology.
B6-hINHBE/ob
Product ID:
C001600
Strain:
C57BL/6NCya;C57BL/6JCya
Status:
Description:
Inhibin βE subunit (INHBE) is a member of the transforming growth factor-β (TGF-β) superfamily, highly specifically expressed in liver cells. The precursor protein of INHBE generates the inhibin β subunit after proteolytic processing. This protein is associated with various cellular processes, including cell proliferation, apoptosis, immune response, and hormone secretion. During the development of obesity and diabetes, the expression of INHBE protein inhibits the proliferation and growth of relevant cells in the pancreas and liver. Research has found a positive correlation between INHBE expression in the liver and insulin resistance and body mass index (BMI), suggesting that INHBE may be a liver factor in altering systemic metabolic status under conditions of obesity-related insulin resistance [1]. The studies conducted by Alnylam Pharmaceuticals and the Regeneron Genetics Center (RGC), respectively, revealed the close relationship between INHBE and fat regulation. The research demonstrated that rare loss-of-function variants in INHBE may protect the liver from the impact of inflammation, abnormal blood lipids, and type 2 diabetes by promoting healthy fat storage. Patients carrying such mutations exhibit more normal fat distribution, significantly reduced abdominal fat, improved metabolic conditions, and a decreased risk of cardiovascular diseases and type 2 diabetes [2-4]. These findings suggest that INHBE is a liver-specific negative regulator of fat storage. Inhibiting the expression of INHBE genes and proteins may be a potential strategy for treating metabolic disorders related to improper fat distribution and storage. Consequently, several small nucleic acid pharmaceutical companies, including Alnylam Pharmaceuticals, Arrowhead Pharmaceuticals, and Wave Life Sciences, are currently developing RNA interference (RNAi) drugs targeting INHBE to treat obesity [5-7].
The leptin (LEP) gene, also known as the OB gene, encodes the leptin protein, which is secreted into the circulation by white adipocytes and plays a major role in regulating energy homeostasis. Circulating leptin binds to leptin receptors (LEPR) in the brain, activating downstream signaling pathways that inhibit feeding and promote energy expenditure. Leptin also has multiple endocrine functions and is involved in physiopathological processes such as immune and inflammatory responses, hematopoiesis, angiogenesis, reproduction, bone formation, and wound healing [8]. Mutations in the LEP gene and its regulatory regions lead to severe obesity and morbid obesity with hypogonadism in humans and are also associated with the development of type II diabetes [9].
The B6-hINHBE/ob mouse model, generated by mating B6-hINHBE mice (Catalog Number: C001533) with Lep KO (ob/ob) mice (Catalog Number: C001368), is a metabolic disease model. It can be used for research on obesity, type II diabetes, and metabolic diseases related to improper fat distribution and storage, and for the development of human INHBE-targeted therapies.
Inhibin βE subunit (INHBE) is a member of the transforming growth factor-β (TGF-β) superfamily, highly specifically expressed in liver cells. The precursor protein of INHBE generates the inhibin β subunit after proteolytic processing. This protein is associated with various cellular processes, including cell proliferation, apoptosis, immune response, and hormone secretion. During the development of obesity and diabetes, the expression of INHBE protein inhibits the proliferation and growth of relevant cells in the pancreas and liver. Research has found a positive correlation between INHBE expression in the liver and insulin resistance and body mass index (BMI), suggesting that INHBE may be a liver factor in altering systemic metabolic status under conditions of obesity-related insulin resistance [1]. The studies conducted by Alnylam Pharmaceuticals and the Regeneron Genetics Center (RGC), respectively, revealed the close relationship between INHBE and fat regulation. The research demonstrated that rare loss-of-function variants in INHBE may protect the liver from the impact of inflammation, abnormal blood lipids, and type 2 diabetes by promoting healthy fat storage. Patients carrying such mutations exhibit more normal fat distribution, significantly reduced abdominal fat, improved metabolic conditions, and a decreased risk of cardiovascular diseases and type 2 diabetes [2-4]. These findings suggest that INHBE is a liver-specific negative regulator of fat storage. Inhibiting the expression of INHBE genes and proteins may be a potential strategy for treating metabolic disorders related to improper fat distribution and storage. Consequently, several small nucleic acid pharmaceutical companies, including Alnylam Pharmaceuticals, Arrowhead Pharmaceuticals, and Wave Life Sciences, are currently developing RNA interference (RNAi) drugs targeting INHBE to treat obesity [5-7].
The leptin (LEP) gene, also known as the OB gene, encodes the leptin protein, which is secreted into the circulation by white adipocytes and plays a major role in regulating energy homeostasis. Circulating leptin binds to leptin receptors (LEPR) in the brain, activating downstream signaling pathways that inhibit feeding and promote energy expenditure. Leptin also has multiple endocrine functions and is involved in physiopathological processes such as immune and inflammatory responses, hematopoiesis, angiogenesis, reproduction, bone formation, and wound healing [8]. Mutations in the LEP gene and its regulatory regions lead to severe obesity and morbid obesity with hypogonadism in humans and are also associated with the development of type II diabetes [9].
The B6-hINHBE/ob mouse model, generated by mating B6-hINHBE mice (Catalog Number: C001533) with Lep KO (ob/ob) mice (Catalog Number: C001368), is a metabolic disease model. It can be used for research on obesity, type II diabetes, and metabolic diseases related to improper fat distribution and storage, and for the development of human INHBE-targeted therapies.
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.
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