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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.
B6-hIL-17A
Product ID:
C001510
Strain:
C57BL/6NCya
Status:
Description:
Interleukin 17A (IL-17A) is a signature cytokine of the T helper 17 (Th17) subset of CD4+ T cells and one of the six members (IL-17A~IL-17F) of the IL-17 family. IL-17A is primarily produced by Th17 cells and can also be produced by other immune cells under certain conditions, including CD8+ T cells, γδT cells, natural killer T (NKT) cells, monocytes, neutrophils, and microglia [1]. IL-17A mediates downstream pathways that induce the production of inflammatory molecules, chemokines, antimicrobial peptides, and remodeling proteins, which have important effects on host defense, cell transport, immune regulation, and tissue repair, especially in inducing innate immune defense. In healthy skin, commensal microorganisms induce the production of IL-17A to provide antifungal protection. When the skin barrier is damaged, IL-17A promotes epithelial cell proliferation and can clear pathogenic factors, promoting tissue repair and wound healing [2]. IL-17A usually protects the body when it is acutely injured, but when a wound requires long-term healing and becomes a chronic injury, the role of IL-17A may transform into wound erosion or excessive proliferation, ultimately leading to loss of function [3].
IL-17A plays a key role in various infectious diseases, inflammations, autoimmune diseases, and cancers. Its high expression level is associated with chronic inflammatory diseases such as rheumatoid arthritis, psoriasis, and multiple sclerosis. Lung injury caused by severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) is largely the result of the promotion of inflammatory reactions by cytokines such as IL-17A. Dysregulation of IL-17 signaling promotes pathogenic inflammation. IL-17A has a pathogenic role in mediating the important inflammatory pathway of psoriasis. The IL-23/Th17/IL-17A pathway is a key link in its pathogenesis, and inhibiting the expression of IL-17A can effectively alleviate psoriasis [4]. IL-17A is also associated with the course of ankylosing spondylitis (AS), and IL-17A inhibitors can effectively treat AS [5]. In addition, studies have shown that IL-17A is involved in the pathogenesis of neurodegenerative diseases in the central nervous system, and its expression level is related to the severity and progression of the disease [3].
B6-hIL-17A mice are humanized mouse models that express human IL-17A protein. They were constructed by using gene editing technology to replace the sequence encoding the endogenous extracellular domain of the mouse Il17a gene with the corresponding sequence from the human IL17A gene while retaining the mouse signal peptide. This strain can be used for mechanism research and preclinical evaluation of therapeutic drugs for various chronic inflammatory diseases such as rheumatoid arthritis, psoriasis, and multiple sclerosis. The homozygotes are viable and fertile.
Interleukin 17A (IL-17A) is a signature cytokine of the T helper 17 (Th17) subset of CD4+ T cells and one of the six members (IL-17A~IL-17F) of the IL-17 family. IL-17A is primarily produced by Th17 cells and can also be produced by other immune cells under certain conditions, including CD8+ T cells, γδT cells, natural killer T (NKT) cells, monocytes, neutrophils, and microglia [1]. IL-17A mediates downstream pathways that induce the production of inflammatory molecules, chemokines, antimicrobial peptides, and remodeling proteins, which have important effects on host defense, cell transport, immune regulation, and tissue repair, especially in inducing innate immune defense. In healthy skin, commensal microorganisms induce the production of IL-17A to provide antifungal protection. When the skin barrier is damaged, IL-17A promotes epithelial cell proliferation and can clear pathogenic factors, promoting tissue repair and wound healing [2]. IL-17A usually protects the body when it is acutely injured, but when a wound requires long-term healing and becomes a chronic injury, the role of IL-17A may transform into wound erosion or excessive proliferation, ultimately leading to loss of function [3].
IL-17A plays a key role in various infectious diseases, inflammations, autoimmune diseases, and cancers. Its high expression level is associated with chronic inflammatory diseases such as rheumatoid arthritis, psoriasis, and multiple sclerosis. Lung injury caused by severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) is largely the result of the promotion of inflammatory reactions by cytokines such as IL-17A. Dysregulation of IL-17 signaling promotes pathogenic inflammation. IL-17A has a pathogenic role in mediating the important inflammatory pathway of psoriasis. The IL-23/Th17/IL-17A pathway is a key link in its pathogenesis, and inhibiting the expression of IL-17A can effectively alleviate psoriasis [4]. IL-17A is also associated with the course of ankylosing spondylitis (AS), and IL-17A inhibitors can effectively treat AS [5]. In addition, studies have shown that IL-17A is involved in the pathogenesis of neurodegenerative diseases in the central nervous system, and its expression level is related to the severity and progression of the disease [3].
B6-hIL-17A mice are humanized mouse models that express human IL-17A protein. They were constructed by using gene editing technology to replace the sequence encoding the endogenous extracellular domain of the mouse Il17a gene with the corresponding sequence from the human IL17A gene while retaining the mouse signal peptide. This strain can be used for mechanism research and preclinical evaluation of therapeutic drugs for various chronic inflammatory diseases such as rheumatoid arthritis, psoriasis, and multiple sclerosis. The homozygotes are viable and fertile.
B6-hTREM1
Product ID:
C001790
Strain:
C57BL/6NCya
Status:
Description:
The Triggering Receptor Expressed on Myeloid Cells 1 (TREM1) gene encodes a transmembrane protein, also known as CD354, primarily expressed on myeloid cells such as neutrophils, monocytes, and macrophages, with expression also observed in dendritic cells, microglia, osteoclasts, platelets, and even some epithelial and endothelial cells [1]. Upon activation, the TREM1 protein amplifies inflammatory responses, often synergizing with Toll-like receptor (TLR) and NOD-like receptor (NLR) signaling pathways. This leads to the robust production and release of pro-inflammatory cytokines and chemokines, enhanced degranulation, phagocytosis, and respiratory burst in neutrophils and macrophages, and even promotes dendritic cell maturation [2]. A soluble form of TREM1 (sTREM1) also exists, which can act as a decoy receptor to modulate inflammation and serves as a biomarker for various inflammatory conditions [3]. Dysregulated TREM1 activity is implicated in a wide range of diseases, including infectious diseases like sepsis and pneumonia, chronic inflammatory conditions such as inflammatory bowel disease, atherosclerosis, rheumatoid arthritis, and various cancers (e.g., glioma, hepatocellular carcinoma, lung adenocarcinoma, breast, colon, and pancreatic cancers), as well as neurodegenerative disorders like Parkinson's and Alzheimer's disease, and kidney-related diseases [2-5].
The B6-hTREM1 mouse is a humanized model, constructed by replacing the mouse Trem1 signal peptide (aa. 1-20) and endogenous extracellular domain (aa. 21-202) with the human TREM1 signal peptide (aa. 1-20) and extracellular domain (aa. 21-205), while preserving the murine aa. 203-230. B6-hTREM1 mice can be used for research into the pathogenesis of various inflammatory diseases, cancers, neurodegenerative diseases, and kidney-related diseases, as well as for the screening, development, and safety evaluation of TREM1-targeted drugs.
The Triggering Receptor Expressed on Myeloid Cells 1 (TREM1) gene encodes a transmembrane protein, also known as CD354, primarily expressed on myeloid cells such as neutrophils, monocytes, and macrophages, with expression also observed in dendritic cells, microglia, osteoclasts, platelets, and even some epithelial and endothelial cells [1]. Upon activation, the TREM1 protein amplifies inflammatory responses, often synergizing with Toll-like receptor (TLR) and NOD-like receptor (NLR) signaling pathways. This leads to the robust production and release of pro-inflammatory cytokines and chemokines, enhanced degranulation, phagocytosis, and respiratory burst in neutrophils and macrophages, and even promotes dendritic cell maturation [2]. A soluble form of TREM1 (sTREM1) also exists, which can act as a decoy receptor to modulate inflammation and serves as a biomarker for various inflammatory conditions [3]. Dysregulated TREM1 activity is implicated in a wide range of diseases, including infectious diseases like sepsis and pneumonia, chronic inflammatory conditions such as inflammatory bowel disease, atherosclerosis, rheumatoid arthritis, and various cancers (e.g., glioma, hepatocellular carcinoma, lung adenocarcinoma, breast, colon, and pancreatic cancers), as well as neurodegenerative disorders like Parkinson's and Alzheimer's disease, and kidney-related diseases [2-5].
The B6-hTREM1 mouse is a humanized model, constructed by replacing the mouse Trem1 signal peptide (aa. 1-20) and endogenous extracellular domain (aa. 21-202) with the human TREM1 signal peptide (aa. 1-20) and extracellular domain (aa. 21-205), while preserving the murine aa. 203-230. B6-hTREM1 mice can be used for research into the pathogenesis of various inflammatory diseases, cancers, neurodegenerative diseases, and kidney-related diseases, as well as for the screening, development, and safety evaluation of TREM1-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-hKHK
Product ID:
C001642
Strain:
C57BL/6NCya
Status:
Description:
The KHK gene encodes ketohexokinase, an enzyme mainly expressed in the liver, kidneys, and small intestine, and plays a crucial role in fructose metabolism. KHK catalyzes the phosphorylation of fructose into fructose-1-phosphate, which is the first step in the fructose metabolic pathway, enabling its conversion into intermediate products that can enter the glycolytic or gluconeogenic pathways. This gene generates two isoforms (KHK-A and KHK-C). Among them, KHK-C has higher catalytic activity and is mainly expressed in the liver, while KHK-A is widely distributed in various tissues, but its function is not fully understood. The expression and activity of KHK are closely related to fructose intake. Excessive fructose intake will lead to the upregulation of KHK activity, which triggers metabolic disorders, such as metabolic dysfunction-associated steatotic liver disease (MASLD), insulin resistance, and obesity [1]. The excessive activation of KHK-C is closely associated with fructose-induced metabolic dysfunction, and blocking KHK-C can significantly ameliorate metabolic abnormalities in fructose-sensitive mice [2]. In addition, fructose metabolism may play an important role in cancer and other proliferative diseases, providing signaling cues that sustain the proliferation of cancer cells. Many cancer cells overexpress KHK. Moreover, the genetic disorder (essential fructosuria) caused by loss-of-function mutations in KHK is clinically asymptomatic and harmless, which further supports the view that inhibiting KHK in cancer patients may be well tolerated [3]. Therefore, KHK has emerged as a potential target for treating metabolic diseases and cancer. Inhibitors targeting KHK are currently under development and have shown the potential to improve metabolic syndrome and inhibit tumor progression.
The B6-hKHK mice are a humanized model constructed through gene editing technology, in which the sequence of the mouse Khk gene is replaced in situ with the corresponding sequence of the human KHK gene. Homozygous B6-hKHK mice are viable and fertile. This model can be used for the study of the pathological mechanisms and treatment methods of metabolic diseases such as metabolic dysfunction-associated steatotic liver disease (MASLD), insulin resistance, and obesity, as well as cancer. It can also be applied to the screening, research and development, and safety evaluation of KHK-targeted drugs.
The KHK gene encodes ketohexokinase, an enzyme mainly expressed in the liver, kidneys, and small intestine, and plays a crucial role in fructose metabolism. KHK catalyzes the phosphorylation of fructose into fructose-1-phosphate, which is the first step in the fructose metabolic pathway, enabling its conversion into intermediate products that can enter the glycolytic or gluconeogenic pathways. This gene generates two isoforms (KHK-A and KHK-C). Among them, KHK-C has higher catalytic activity and is mainly expressed in the liver, while KHK-A is widely distributed in various tissues, but its function is not fully understood. The expression and activity of KHK are closely related to fructose intake. Excessive fructose intake will lead to the upregulation of KHK activity, which triggers metabolic disorders, such as metabolic dysfunction-associated steatotic liver disease (MASLD), insulin resistance, and obesity [1]. The excessive activation of KHK-C is closely associated with fructose-induced metabolic dysfunction, and blocking KHK-C can significantly ameliorate metabolic abnormalities in fructose-sensitive mice [2]. In addition, fructose metabolism may play an important role in cancer and other proliferative diseases, providing signaling cues that sustain the proliferation of cancer cells. Many cancer cells overexpress KHK. Moreover, the genetic disorder (essential fructosuria) caused by loss-of-function mutations in KHK is clinically asymptomatic and harmless, which further supports the view that inhibiting KHK in cancer patients may be well tolerated [3]. Therefore, KHK has emerged as a potential target for treating metabolic diseases and cancer. Inhibitors targeting KHK are currently under development and have shown the potential to improve metabolic syndrome and inhibit tumor progression.
The B6-hKHK mice are a humanized model constructed through gene editing technology, in which the sequence of the mouse Khk gene is replaced in situ with the corresponding sequence of the human KHK gene. Homozygous B6-hKHK mice are viable and fertile. This model can be used for the study of the pathological mechanisms and treatment methods of metabolic diseases such as metabolic dysfunction-associated steatotic liver disease (MASLD), insulin resistance, and obesity, as well as cancer. It can also be applied to the screening, research and development, and safety evaluation of KHK-targeted drugs.
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-hXDH
Product ID:
C001586
Strain:
C57BL/6NCya
Status:
Description:
Hyperuricemia is a metabolic disorder characterized by abnormally elevated levels of uric acid (UA) in the blood. Uric acid, the end product of purine metabolism, may crystallize as urate in joints, leading to gouty arthritis or form stones in the kidneys when its concentration is excessively high. The clinical manifestations of gout include hyperuricemia, recurrent acute gouty arthritis, deposition of tophi, chronic tophaceous arthritis, and joint deformities. It commonly affects the kidneys, causing chronic interstitial nephritis and uric acid nephrolithiasis [1-3]. By 2020, the global prevalence of hyperuricemia and gout surpassed 1.1 billion cases. In China, the number of patients is projected to reach 200 million for hyperuricemia and 43.25 million for gout by 2024 [2-3]. With the increasing disease burden, the demand for pharmacological interventions for hyperuricemia and gout continues to grow.
Hyperuricemia is closely related to uric acid levels in the body, and current therapeutic agents mainly target the reduction of uric acid synthesis or the promotion of uric acid excretion to manage the condition. Xanthine oxidoreductase (XOR) plays a critical role in purine metabolism by catalyzing the oxidation of hypoxanthine to xanthine and subsequently to uric acid. It is thus a key regulatory point in uric acid synthesis and an important target for hyperuricemia treatment [4-5]. XOR exists in two forms: the reduced xanthine dehydrogenase (XDH) and the oxidized xanthine oxidase (XO). XDH, in its reduced state, catalyzes the conversion of hypoxanthine to xanthine and uric acid, generating reduced nicotinamide adenine dinucleotide (NADH). In contrast, XO, in its oxidized state, converts xanthine to uric acid and hydrogen peroxide. The inhibition of XO by xanthine oxidase inhibitors (XOIs) to reduce uric acid production is a widely adopted therapeutic strategy for hyperuricemia and gout [6]. However, safety concerns remain with existing XOIs, highlighting the urgent need for novel therapeutics with improved safety profiles. Small interfering RNA (siRNA) represents a promising research focus in this area.
This strain is a humanized mouse model of the Xdh gene, generated by replacing the mouse Xdh gene with the complete human XDH gene sequence, including its untranslated regions (UTRs), exons, and introns. The B6-hXDH mice express the human XDH gene and xanthine oxidase protein in a pattern similar to the endogenous Xdh gene in mice, making their genetic, protein expression, and biochemical features highly comparable to humans. This strain serves as an ideal preclinical platform for studying the pathological mechanisms of hyperuricemia and gout and for developing novel xanthine oxidase inhibitors and nucleic acid therapies.
Hyperuricemia is a metabolic disorder characterized by abnormally elevated levels of uric acid (UA) in the blood. Uric acid, the end product of purine metabolism, may crystallize as urate in joints, leading to gouty arthritis or form stones in the kidneys when its concentration is excessively high. The clinical manifestations of gout include hyperuricemia, recurrent acute gouty arthritis, deposition of tophi, chronic tophaceous arthritis, and joint deformities. It commonly affects the kidneys, causing chronic interstitial nephritis and uric acid nephrolithiasis [1-3]. By 2020, the global prevalence of hyperuricemia and gout surpassed 1.1 billion cases. In China, the number of patients is projected to reach 200 million for hyperuricemia and 43.25 million for gout by 2024 [2-3]. With the increasing disease burden, the demand for pharmacological interventions for hyperuricemia and gout continues to grow.
Hyperuricemia is closely related to uric acid levels in the body, and current therapeutic agents mainly target the reduction of uric acid synthesis or the promotion of uric acid excretion to manage the condition. Xanthine oxidoreductase (XOR) plays a critical role in purine metabolism by catalyzing the oxidation of hypoxanthine to xanthine and subsequently to uric acid. It is thus a key regulatory point in uric acid synthesis and an important target for hyperuricemia treatment [4-5]. XOR exists in two forms: the reduced xanthine dehydrogenase (XDH) and the oxidized xanthine oxidase (XO). XDH, in its reduced state, catalyzes the conversion of hypoxanthine to xanthine and uric acid, generating reduced nicotinamide adenine dinucleotide (NADH). In contrast, XO, in its oxidized state, converts xanthine to uric acid and hydrogen peroxide. The inhibition of XO by xanthine oxidase inhibitors (XOIs) to reduce uric acid production is a widely adopted therapeutic strategy for hyperuricemia and gout [6]. However, safety concerns remain with existing XOIs, highlighting the urgent need for novel therapeutics with improved safety profiles. Small interfering RNA (siRNA) represents a promising research focus in this area.
This strain is a humanized mouse model of the Xdh gene, generated by replacing the mouse Xdh gene with the complete human XDH gene sequence, including its untranslated regions (UTRs), exons, and introns. The B6-hXDH mice express the human XDH gene and xanthine oxidase protein in a pattern similar to the endogenous Xdh gene in mice, making their genetic, protein expression, and biochemical features highly comparable to humans. This strain serves as an ideal preclinical platform for studying the pathological mechanisms of hyperuricemia and gout and for developing novel xanthine oxidase inhibitors and nucleic acid therapies.
BALB/c;B6J-Rosa26-hHRAS
Product ID:
I001214
Strain:
BALB/c;B6JCya
Status:
Description:
The HRas oncogene (HRAS), also known as the Harvey Rat Sarcoma Viral Oncogene Homolog (HRAS), is a member of the Ras oncogene family, which also includes KRAS and NRAS. All members of this family are associated with the development of mammalian sarcoma retroviruses [1]. HRAS encodes the H-Ras protein, a small GTPase responsible for transmitting signals from cell surface receptors to the nucleus, regulating cell proliferation, survival, and differentiation. HRAS is primarily expressed in various tissues, including the brain, heart, and skeletal muscle, and is involved in controlling the cellular response to growth factors. As a member of the small GTPase family, HRAS acts as a molecular switch, cycling between active and inactive states to influence key cellular processes. Mutations in the HRAS gene can lead to abnormal signal transduction, commonly found in tumors of stratified epithelial tissues, such as bladder cancer, thyroid cancer, and head and neck squamous cell carcinoma. Additionally, HRAS is associated with Costello syndrome, a genetic disorder characterized by developmental delays and an increased risk of tumors [2-3].
Early studies have shown that genotoxic carcinogens shorten the latency period and increase the incidence of malignant tumors in rasH2 mice, which carry the human HRAS (c-Ha-ras) oncogene, compared to non-transgenic mice. Therefore, rasH2 mice are ideal animal models for rapid carcinogenicity testing [4-5]. Further research has shown that F1 hybrid mice (CB6F1 background rasH2 mice) obtained by mating male C57BL/6J mice carrying the human prototype c-Ha-ras gene with female BALB/c mice are significantly more sensitive to both mutagenic and non-mutagenic carcinogens than control mice [5]. These mice are highly sensitive to the carcinogenicity of both genotoxic and non-genotoxic compounds while showing no response to non-carcinogens [6]. Between 12 to 18 months of age, rasH2 mice primarily develop spontaneous alveolar adenomas/bronchial adenomas/adenocarcinomas, splenic hemangiomas/hemangiosarcomas, and a smaller number of skin and gastric papillomas and lymphomas [4]. In the 1990s, this mouse model was officially approved by the FDA for carcinogenicity evaluations in drug safety assessments, reducing the standard two-year carcinogenicity test in common rodents to six months.
BALB/c;B6J-Rosa26-hHRAS mice are obtained by crossing Rosa26-hHRAS mice on a C57BL/6JCya background (Catalog No.: I001213) with BALB/cAnCya mice. This hybrid strain exhibits higher sensitivity to both genotoxic and non-genotoxic human carcinogens. BALB/c;B6J-Rosa26-hHRAS mice can be used for rapid in vivo testing of the carcinogenicity of genotoxic and non-genotoxic compounds, studying the impact of HRAS oncogene point mutations on tumorigenesis and development, and developing tumor prevention or suppression therapies.
The HRas oncogene (HRAS), also known as the Harvey Rat Sarcoma Viral Oncogene Homolog (HRAS), is a member of the Ras oncogene family, which also includes KRAS and NRAS. All members of this family are associated with the development of mammalian sarcoma retroviruses [1]. HRAS encodes the H-Ras protein, a small GTPase responsible for transmitting signals from cell surface receptors to the nucleus, regulating cell proliferation, survival, and differentiation. HRAS is primarily expressed in various tissues, including the brain, heart, and skeletal muscle, and is involved in controlling the cellular response to growth factors. As a member of the small GTPase family, HRAS acts as a molecular switch, cycling between active and inactive states to influence key cellular processes. Mutations in the HRAS gene can lead to abnormal signal transduction, commonly found in tumors of stratified epithelial tissues, such as bladder cancer, thyroid cancer, and head and neck squamous cell carcinoma. Additionally, HRAS is associated with Costello syndrome, a genetic disorder characterized by developmental delays and an increased risk of tumors [2-3].
Early studies have shown that genotoxic carcinogens shorten the latency period and increase the incidence of malignant tumors in rasH2 mice, which carry the human HRAS (c-Ha-ras) oncogene, compared to non-transgenic mice. Therefore, rasH2 mice are ideal animal models for rapid carcinogenicity testing [4-5]. Further research has shown that F1 hybrid mice (CB6F1 background rasH2 mice) obtained by mating male C57BL/6J mice carrying the human prototype c-Ha-ras gene with female BALB/c mice are significantly more sensitive to both mutagenic and non-mutagenic carcinogens than control mice [5]. These mice are highly sensitive to the carcinogenicity of both genotoxic and non-genotoxic compounds while showing no response to non-carcinogens [6]. Between 12 to 18 months of age, rasH2 mice primarily develop spontaneous alveolar adenomas/bronchial adenomas/adenocarcinomas, splenic hemangiomas/hemangiosarcomas, and a smaller number of skin and gastric papillomas and lymphomas [4]. In the 1990s, this mouse model was officially approved by the FDA for carcinogenicity evaluations in drug safety assessments, reducing the standard two-year carcinogenicity test in common rodents to six months.
BALB/c;B6J-Rosa26-hHRAS mice are obtained by crossing Rosa26-hHRAS mice on a C57BL/6JCya background (Catalog No.: I001213) with BALB/cAnCya mice. This hybrid strain exhibits higher sensitivity to both genotoxic and non-genotoxic human carcinogens. BALB/c;B6J-Rosa26-hHRAS mice can be used for rapid in vivo testing of the carcinogenicity of genotoxic and non-genotoxic compounds, studying the impact of HRAS oncogene point mutations on tumorigenesis and development, and developing tumor prevention or suppression therapies.
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