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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-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-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-hTGFBI
Product ID:
C001546
Strain:
C57BL/6JCya
Status:
Description:
Corneal dystrophy (CD) refers to a group of primary hereditary progressive corneal diseases. The typical clinical presentation involves gradual loss of corneal transparency in both eyes, often leading to recurrent corneal erosions and visual impairment. The TGFBI gene (also known as BIGH3) encodes an extracellular matrix protein called keratoepithelin (KE protein), which plays a role in cell growth, differentiation, wound healing, cell adhesion, migration, apoptosis, proliferation, and tumorigenesis [1]. Mutations in the TGFBI gene are associated with various types of corneal dystrophy. Abnormal accumulation of mutated TGFBI deposits in the corneal epithelium and stroma progressively affects corneal transparency, leading to visual impairment.
Currently, therapeutic pipelines targeting the TGFBI gene have entered preclinical research stages. For instance, SiSaf Ltd. is developing a siRNA drug pipeline called SIS-201-CD, which aims to treat the disease by specifically inhibiting abnormal TGFBI expression. Most gene therapies target human genes, but considering the genetic differences between animals and humans, humanizing mouse genes can accelerate the development of TGFBI-targeted gene therapies for clinical use. This strain is a mouse Tgfbi gene humanized model and can be used for research on CD. The homozygous B6-hTGFBI mice are viable and fertile. In addition, based on the independently developed TurboKnockout fusion BAC recombination technology, Cyagen can also generate hot mutation models based on this strain and provide customized services for specific mutations to meet the experimental needs in pharmacology and other fields related to CD.
Corneal dystrophy (CD) refers to a group of primary hereditary progressive corneal diseases. The typical clinical presentation involves gradual loss of corneal transparency in both eyes, often leading to recurrent corneal erosions and visual impairment. The TGFBI gene (also known as BIGH3) encodes an extracellular matrix protein called keratoepithelin (KE protein), which plays a role in cell growth, differentiation, wound healing, cell adhesion, migration, apoptosis, proliferation, and tumorigenesis [1]. Mutations in the TGFBI gene are associated with various types of corneal dystrophy. Abnormal accumulation of mutated TGFBI deposits in the corneal epithelium and stroma progressively affects corneal transparency, leading to visual impairment.
Currently, therapeutic pipelines targeting the TGFBI gene have entered preclinical research stages. For instance, SiSaf Ltd. is developing a siRNA drug pipeline called SIS-201-CD, which aims to treat the disease by specifically inhibiting abnormal TGFBI expression. Most gene therapies target human genes, but considering the genetic differences between animals and humans, humanizing mouse genes can accelerate the development of TGFBI-targeted gene therapies for clinical use. This strain is a mouse Tgfbi gene humanized model and can be used for research on CD. The homozygous B6-hTGFBI mice are viable and fertile. In addition, based on the independently developed TurboKnockout fusion BAC recombination technology, Cyagen can also generate hot mutation models based on this strain and provide customized services for specific mutations to meet the experimental needs in pharmacology and other fields related to CD.
B6-htau/hGLP-1R
Product ID:
I001221
Strain:
C57BL/6Cya
Status:
Description:
The tau protein, a microtubule-associated protein encoded by MAPT is primarily localized to neuronal axons and plays a critical role in microtubule stability and assembly. By binding to microtubules, tau protein helps to maintain neuronal cell shape. Mutations in MAPT can promote tau aggregation, leading to pathological tau protein accumulation and death of glutamatergic cortical neurons [1]. Additionally, certain MAPT mutations can affect pre-mRNA exon splicing, altering the ratio of 3R to 4R tau protein isoforms and increasing the relative production of 4R-tau protein, which is more prone to fibril formation [2].
The GLP-1 receptor (GLP-1R) gene encodes a protein that serves as the receptor for the glucagon-like peptide 1 (GLP-1) hormone, belonging to the glucagon receptor subfamily within the class B G-protein-coupled receptors (GPCRs). G proteins are a class of intracellular signal transduction proteins typically associated with seven-transmembrane receptors (GPCRs). When a GPCR binds to its ligand, it activates the G protein, causing it to dissociate from the Gβγ subunit and initiate downstream effects through interactions with membrane-bound effector molecules. This signaling process is known as canonical G protein signaling. GLP-1R is a multi-transmembrane protein characterized by a typical seven-transmembrane core domain and a relatively large extracellular domain, which can stimulate glucose-induced insulin secretion [3]. GLP-1R is a cell surface receptor protein widely expressed in tissues such as the brain, small intestine, heart, and lungs. It internalizes in response to GLP-1 and GLP-1 analogs and plays a crucial role in the insulin secretion signaling cascade. Additionally, data from animal models indicate its neuroprotective effects [4-5]. Polymorphisms of this gene are closely associated with diabetes. The GLP1R protein is an important drug target for treating type 2 diabetes and stroke. Glucagon-like peptide-1 receptor agonists (GLP-1RAs) are a new class of antidiabetic drugs in recent years. They activate GLP1R to enhance insulin secretion, suppress glucagon secretion, delay gastric emptying, and reduce food intake through central appetite suppression, lowering blood glucose and weight loss [6].
The B6-htau/hGLP-1R mouse is obtained by mating B6-htau mice (Catalog No.: C001410) with B6-hGLP-1R mice (Catalog No.: C001421). This model can be used for research on neurodegenerative diseases such as frontotemporal dementia (FTD) and Alzheimer's disease (AD), as well as metabolic diseases such as obesity and type 2 diabetes. It is also useful for developing GLP-1 receptor agonist (GLP-1RA) drugs or for the preclinical evaluation of the potential therapeutic effects of GLP-1RA drugs in tauopathy-related diseases like Alzheimer's disease (AD).
The tau protein, a microtubule-associated protein encoded by MAPT is primarily localized to neuronal axons and plays a critical role in microtubule stability and assembly. By binding to microtubules, tau protein helps to maintain neuronal cell shape. Mutations in MAPT can promote tau aggregation, leading to pathological tau protein accumulation and death of glutamatergic cortical neurons [1]. Additionally, certain MAPT mutations can affect pre-mRNA exon splicing, altering the ratio of 3R to 4R tau protein isoforms and increasing the relative production of 4R-tau protein, which is more prone to fibril formation [2].
The GLP-1 receptor (GLP-1R) gene encodes a protein that serves as the receptor for the glucagon-like peptide 1 (GLP-1) hormone, belonging to the glucagon receptor subfamily within the class B G-protein-coupled receptors (GPCRs). G proteins are a class of intracellular signal transduction proteins typically associated with seven-transmembrane receptors (GPCRs). When a GPCR binds to its ligand, it activates the G protein, causing it to dissociate from the Gβγ subunit and initiate downstream effects through interactions with membrane-bound effector molecules. This signaling process is known as canonical G protein signaling. GLP-1R is a multi-transmembrane protein characterized by a typical seven-transmembrane core domain and a relatively large extracellular domain, which can stimulate glucose-induced insulin secretion [3]. GLP-1R is a cell surface receptor protein widely expressed in tissues such as the brain, small intestine, heart, and lungs. It internalizes in response to GLP-1 and GLP-1 analogs and plays a crucial role in the insulin secretion signaling cascade. Additionally, data from animal models indicate its neuroprotective effects [4-5]. Polymorphisms of this gene are closely associated with diabetes. The GLP1R protein is an important drug target for treating type 2 diabetes and stroke. Glucagon-like peptide-1 receptor agonists (GLP-1RAs) are a new class of antidiabetic drugs in recent years. They activate GLP1R to enhance insulin secretion, suppress glucagon secretion, delay gastric emptying, and reduce food intake through central appetite suppression, lowering blood glucose and weight loss [6].
The B6-htau/hGLP-1R mouse is obtained by mating B6-htau mice (Catalog No.: C001410) with B6-hGLP-1R mice (Catalog No.: C001421). This model can be used for research on neurodegenerative diseases such as frontotemporal dementia (FTD) and Alzheimer's disease (AD), as well as metabolic diseases such as obesity and type 2 diabetes. It is also useful for developing GLP-1 receptor agonist (GLP-1RA) drugs or for the preclinical evaluation of the potential therapeutic effects of GLP-1RA drugs in tauopathy-related diseases like Alzheimer's disease (AD).
B6-huOX40 (huTNFRSF4)
Product ID:
C001805
Strain:
C57BL/6NCya
Status:
Description:
The TNFRSF4 gene encodes the protein OX40 (also known as CD134 or Tumor Necrosis Factor Receptor Superfamily Member 4), a cell-surface receptor belonging to the TNF-receptor superfamily. Its gene expression is primarily found on activated T cells (both CD4+ helper and CD8+ T cells), and also on other immune and non-immune cells, becoming upregulated following T cell activation, distinguishing it from constitutively expressed co-stimulatory molecules. The encoded protein acts as a co-stimulatory molecule, functioning as a receptor for its ligand, TNFSF4 (OX40L or CD252), which is expressed on antigen-presenting cells (APCs) [1]. The primary function of the OX40/OX40L axis is to deliver a crucial co-stimulatory signal that promotes T cell proliferation, enhances their survival (by suppressing apoptosis via pathways like NF-κB activation), and supports their differentiation into long-term effector and memory T cells, thus playing a vital role in sustaining the adaptive immune response [2]. Dysregulation of this pathway is implicated in various associated diseases, including autoimmune disorders such as systemic lupus erythematosus (SLE), rheumatoid arthritis, and Graves' disease, as well as cancers (e.g., in tumor-infiltrating lymphocytes, and some leukemias and carcinomas), where it's a target for immunotherapy, and Immunodeficiency 16 (IMD16), a primary immunodeficiency caused by loss-of-function variants [3-4].
B6-huOX40 (huTNFRSF4) mouse is a humanized model generated using gene editing technology, in which the mouse Tnfrsf4 endogenous extracellular domain is replaced with the human TNFRSF4 extracellular domain. The murine signal peptide was preserved. This model can be used for studying the pathological mechanisms and therapeutic approaches of autoimmune disorders, such as systemic lupus erythematosus (SLE), rheumatoid arthritis, and Graves' disease, as well as cancers and Immunodeficiency 16 (IMD16). It can also be used for the development of TNFRSF4-targeted drugs.
The TNFRSF4 gene encodes the protein OX40 (also known as CD134 or Tumor Necrosis Factor Receptor Superfamily Member 4), a cell-surface receptor belonging to the TNF-receptor superfamily. Its gene expression is primarily found on activated T cells (both CD4+ helper and CD8+ T cells), and also on other immune and non-immune cells, becoming upregulated following T cell activation, distinguishing it from constitutively expressed co-stimulatory molecules. The encoded protein acts as a co-stimulatory molecule, functioning as a receptor for its ligand, TNFSF4 (OX40L or CD252), which is expressed on antigen-presenting cells (APCs) [1]. The primary function of the OX40/OX40L axis is to deliver a crucial co-stimulatory signal that promotes T cell proliferation, enhances their survival (by suppressing apoptosis via pathways like NF-κB activation), and supports their differentiation into long-term effector and memory T cells, thus playing a vital role in sustaining the adaptive immune response [2]. Dysregulation of this pathway is implicated in various associated diseases, including autoimmune disorders such as systemic lupus erythematosus (SLE), rheumatoid arthritis, and Graves' disease, as well as cancers (e.g., in tumor-infiltrating lymphocytes, and some leukemias and carcinomas), where it's a target for immunotherapy, and Immunodeficiency 16 (IMD16), a primary immunodeficiency caused by loss-of-function variants [3-4].
B6-huOX40 (huTNFRSF4) mouse is a humanized model generated using gene editing technology, in which the mouse Tnfrsf4 endogenous extracellular domain is replaced with the human TNFRSF4 extracellular domain. The murine signal peptide was preserved. This model can be used for studying the pathological mechanisms and therapeutic approaches of autoimmune disorders, such as systemic lupus erythematosus (SLE), rheumatoid arthritis, and Graves' disease, as well as cancers and Immunodeficiency 16 (IMD16). It can also be used for the development of TNFRSF4-targeted drugs.
B6-hIL2RB
Product ID:
C001820
Strain:
C57BL/6NCya
Status:
Description:
The IL2RB gene, located on human chromosome 22, encodes the Interleukin-2 receptor subunit beta protein. This protein is a key component of the high-affinity receptors for both Interleukin-2 (IL-2) and Interleukin-15 (IL-15). Structurally, it is a single-pass type I membrane protein with an extracellular domain, a transmembrane region, and an intracellular domain containing motifs essential for signaling, primarily through the JAK/STAT pathway [1]. Its expression is significant in hematopoietic tissues and is upregulated upon T-cell activation, playing a critical role in the proliferation and differentiation of lymphocytes. The function of the IL-2Rβ chain is to transmit signals from IL-2 or IL-15 binding into the cell, driving immune responses. Consequently, the protein is prominently expressed on immune cells such as T-lymphocytes and Natural Killer (NK) cells, with expression also observed on activated B-lymphocytes [2]. Mutations or dysregulation of the IL2RB gene are associated with severe immunodeficiencies (though less commonly than mutations in its partner subunit IL2RG) and are implicated in the pathogenesis of certain leukemias and lymphomas, often due to constitutive activation of its downstream signaling pathways [3].
B6-hIL2RB mouse is a humanized model generated using gene editing technology, in which the mouse Il2rb endogenous signal peptide and extracellular domain are replaced with the human IL2RB signal peptide and extracellular domain. This model can be used for studying the pathological mechanisms and therapeutic approaches of immunodeficiencies and certain leukemias and lymphomas, as well as for the development of IL2RB-targeted drugs.
The IL2RB gene, located on human chromosome 22, encodes the Interleukin-2 receptor subunit beta protein. This protein is a key component of the high-affinity receptors for both Interleukin-2 (IL-2) and Interleukin-15 (IL-15). Structurally, it is a single-pass type I membrane protein with an extracellular domain, a transmembrane region, and an intracellular domain containing motifs essential for signaling, primarily through the JAK/STAT pathway [1]. Its expression is significant in hematopoietic tissues and is upregulated upon T-cell activation, playing a critical role in the proliferation and differentiation of lymphocytes. The function of the IL-2Rβ chain is to transmit signals from IL-2 or IL-15 binding into the cell, driving immune responses. Consequently, the protein is prominently expressed on immune cells such as T-lymphocytes and Natural Killer (NK) cells, with expression also observed on activated B-lymphocytes [2]. Mutations or dysregulation of the IL2RB gene are associated with severe immunodeficiencies (though less commonly than mutations in its partner subunit IL2RG) and are implicated in the pathogenesis of certain leukemias and lymphomas, often due to constitutive activation of its downstream signaling pathways [3].
B6-hIL2RB mouse is a humanized model generated using gene editing technology, in which the mouse Il2rb endogenous signal peptide and extracellular domain are replaced with the human IL2RB signal peptide and extracellular domain. This model can be used for studying the pathological mechanisms and therapeutic approaches of immunodeficiencies and certain leukemias and lymphomas, as well as for the development of IL2RB-targeted drugs.
B6-huKLKB1
Product ID:
C001845
Strain:
C57BL/6JCya
Status:
Description:
The KLKB1 gene provides instructions for creating prekallikrein, a protein primarily synthesized in the liver and found circulating in the blood. This protein is activated by Factor XII to form plasma kallikrein, a serine protease [1]. The function of this protein is critical for the intrinsic coagulation pathway (blood clotting) and the kallikrein-kinin system, which regulates blood pressure and inflammation [2]. The interaction of plasma kallikrein with Factor XII triggers a series of reactions that result in the release of bradykinin, a protein that promotes inflammation [3]. Mutations in the KLKB1 gene are associated with inherited conditions, most notably prekallikrein deficiency, which causes a prolonged activated partial thromboplastin time (a measure of blood clotting) but typically doesn't lead to clinical bleeding problems. More recently, mutations in the KLKB1 gene have also been linked to hereditary angioedema (HAE), a disorder characterized by episodes of severe swelling [4].
The B6-huKLKB1 mice are a humanized model constructed through gene editing technology, in which the mouse Klkb1 endogenous domain is replaced with the human KLKB1 domain. The murine signal peptide is kept. This model can be used for the study of the pathological mechanisms and treatment methods of prekallikrein deficiency and hereditary angioedema. It can also be applied to the development of KLKB1-targeted drugs.
The KLKB1 gene provides instructions for creating prekallikrein, a protein primarily synthesized in the liver and found circulating in the blood. This protein is activated by Factor XII to form plasma kallikrein, a serine protease [1]. The function of this protein is critical for the intrinsic coagulation pathway (blood clotting) and the kallikrein-kinin system, which regulates blood pressure and inflammation [2]. The interaction of plasma kallikrein with Factor XII triggers a series of reactions that result in the release of bradykinin, a protein that promotes inflammation [3]. Mutations in the KLKB1 gene are associated with inherited conditions, most notably prekallikrein deficiency, which causes a prolonged activated partial thromboplastin time (a measure of blood clotting) but typically doesn't lead to clinical bleeding problems. More recently, mutations in the KLKB1 gene have also been linked to hereditary angioedema (HAE), a disorder characterized by episodes of severe swelling [4].
The B6-huKLKB1 mice are a humanized model constructed through gene editing technology, in which the mouse Klkb1 endogenous domain is replaced with the human KLKB1 domain. The murine signal peptide is kept. This model can be used for the study of the pathological mechanisms and treatment methods of prekallikrein deficiency and hereditary angioedema. It can also be applied to the development of KLKB1-targeted drugs.
B6-hTL1A/hNLRP3
Product ID:
C001690
Strain:
C57BL/6N;6JCya
Status:
Description:
TNF-like ligand 1A (TL1A), also known as TNF superfamily member 15 (TNFSF15), is a member of the tumor necrosis factor (TNF) family encoded by the TNFSF15 gene in humans. TL1A acts as a ligand for death receptor 3 (DR3) and decoy receptor 3 (DcR3), providing a stimulatory signal for downstream pathways. It regulates the proliferation, activation, and apoptosis of effector cells, as well as cytokine and chemokine production. TL1A is expressed in various immune cells, including monocytes, macrophages, dendritic cells, and T cells, as well as in non-immune cells such as synovial fibroblasts and endothelial cells. It plays a crucial role in modulating immune responses by promoting the differentiation and survival of T cells, particularly Th17 cells involved in inflammatory processes [1]. TL1A enhances IL-2 responses in anti-CD3/CD28-stimulated T cells and synergizes with IL-12 and IL-18 to augment IFN-γ release in human T and NK cells, biasing T cell differentiation toward a Th1 phenotype [2]. Dysregulation of TL1A expression is implicated in autoimmune diseases, including inflammatory bowel disease (IBD), rheumatoid arthritis (RA), primary biliary cholangitis (PBC), systemic lupus erythematosus (SLE), and ankylosing spondylitis (AS) [1]. TL1A has emerged as a promising therapeutic target, with ongoing research focused on developing monoclonal antibodies and other biologics to neutralize TL1A and reduce inflammation in autoimmune disorders. Clinical trial results suggest that TL1A inhibition can be used in the treatment of various autoimmune diseases, particularly IBD [3-5].
The Cryopyrin protein, encoded by the NOD-like receptor family pyrin domain-containing 3 (NLRP3) gene, is a core component of the inflammasome in the innate immune system. As a member of the NOD-like receptor (NLR) family, NLRP3 is predominantly expressed in leukocytes and chondrocytes. It participates in the host defense against damage and infection by recognizing pathogen-associated molecular patterns (PAMPs) or damage-associated molecular patterns (DAMPs) to activate immune responses [6]. In its inactive monomeric state, NLRP3 senses intracellular damage signals, such as abnormal protein aggregates and lipid accumulation. Upon activation, NLRP3 oligomerizes, adopting an active conformation and assembling into inflammasome complexes, subsequently activating Caspase-1 to drive the maturation and secretion of pro-inflammatory cytokines, including IL-1β and IL-18 [6-7]. Activated NLRP3 not only induces the release of inflammatory cytokines but also triggers lytic cell pyroptosis. The intracellular components released during pyroptosis can further amplify inflammatory signals, forming a positive feedback loop of autoinflammation. Moreover, IL-1β can exacerbate the inflammatory cascade by stimulating the production of inflammatory markers such as IL-6 and high-sensitivity C-reactive protein (hsCRP) [8-9]. Given NLRP3's upstream position relative to IL-1β/IL-18 and other inflammatory factors, targeting its activity can effectively block the self-reinforcing mechanism of chronic inflammation, providing a significant therapeutic strategy for inflammation-related diseases [10]. The potential therapeutic areas include Alzheimer’s disease, Parkinson’s disease (via neuroinflammation modulation), inflammatory bowel disease, metabolic dysfunction-associated steatohepatitis (MASH), gout, and obesity-related metabolic inflammation [11-12].
B6-hTL1A/hNLRP3 mice are TL1A and NLRP3 double humanized mouse models obtained by mating TL1A humanized mouse models (Catalog No. C001603) with NLRP3 humanized mouse models (Catalog No. C001616). B6-hTL1A/hNLRP3 mice express human TL1A and NLRP3 genomic sequences under the control of mouse promoters. This model is capable of reproducing human TL1A and NLRP3 and is a valuable tool for studying autoimmune diseases and inflammation-related diseases. In addition, this model also provides a powerful preclinical research platform for evaluating the efficacy and mechanism of therapeutic drugs targeting TL1A and NLRP3.
TNF-like ligand 1A (TL1A), also known as TNF superfamily member 15 (TNFSF15), is a member of the tumor necrosis factor (TNF) family encoded by the TNFSF15 gene in humans. TL1A acts as a ligand for death receptor 3 (DR3) and decoy receptor 3 (DcR3), providing a stimulatory signal for downstream pathways. It regulates the proliferation, activation, and apoptosis of effector cells, as well as cytokine and chemokine production. TL1A is expressed in various immune cells, including monocytes, macrophages, dendritic cells, and T cells, as well as in non-immune cells such as synovial fibroblasts and endothelial cells. It plays a crucial role in modulating immune responses by promoting the differentiation and survival of T cells, particularly Th17 cells involved in inflammatory processes [1]. TL1A enhances IL-2 responses in anti-CD3/CD28-stimulated T cells and synergizes with IL-12 and IL-18 to augment IFN-γ release in human T and NK cells, biasing T cell differentiation toward a Th1 phenotype [2]. Dysregulation of TL1A expression is implicated in autoimmune diseases, including inflammatory bowel disease (IBD), rheumatoid arthritis (RA), primary biliary cholangitis (PBC), systemic lupus erythematosus (SLE), and ankylosing spondylitis (AS) [1]. TL1A has emerged as a promising therapeutic target, with ongoing research focused on developing monoclonal antibodies and other biologics to neutralize TL1A and reduce inflammation in autoimmune disorders. Clinical trial results suggest that TL1A inhibition can be used in the treatment of various autoimmune diseases, particularly IBD [3-5].
The Cryopyrin protein, encoded by the NOD-like receptor family pyrin domain-containing 3 (NLRP3) gene, is a core component of the inflammasome in the innate immune system. As a member of the NOD-like receptor (NLR) family, NLRP3 is predominantly expressed in leukocytes and chondrocytes. It participates in the host defense against damage and infection by recognizing pathogen-associated molecular patterns (PAMPs) or damage-associated molecular patterns (DAMPs) to activate immune responses [6]. In its inactive monomeric state, NLRP3 senses intracellular damage signals, such as abnormal protein aggregates and lipid accumulation. Upon activation, NLRP3 oligomerizes, adopting an active conformation and assembling into inflammasome complexes, subsequently activating Caspase-1 to drive the maturation and secretion of pro-inflammatory cytokines, including IL-1β and IL-18 [6-7]. Activated NLRP3 not only induces the release of inflammatory cytokines but also triggers lytic cell pyroptosis. The intracellular components released during pyroptosis can further amplify inflammatory signals, forming a positive feedback loop of autoinflammation. Moreover, IL-1β can exacerbate the inflammatory cascade by stimulating the production of inflammatory markers such as IL-6 and high-sensitivity C-reactive protein (hsCRP) [8-9]. Given NLRP3's upstream position relative to IL-1β/IL-18 and other inflammatory factors, targeting its activity can effectively block the self-reinforcing mechanism of chronic inflammation, providing a significant therapeutic strategy for inflammation-related diseases [10]. The potential therapeutic areas include Alzheimer’s disease, Parkinson’s disease (via neuroinflammation modulation), inflammatory bowel disease, metabolic dysfunction-associated steatohepatitis (MASH), gout, and obesity-related metabolic inflammation [11-12].
B6-hTL1A/hNLRP3 mice are TL1A and NLRP3 double humanized mouse models obtained by mating TL1A humanized mouse models (Catalog No. C001603) with NLRP3 humanized mouse models (Catalog No. C001616). B6-hTL1A/hNLRP3 mice express human TL1A and NLRP3 genomic sequences under the control of mouse promoters. This model is capable of reproducing human TL1A and NLRP3 and is a valuable tool for studying autoimmune diseases and inflammation-related diseases. In addition, this model also provides a powerful preclinical research platform for evaluating the efficacy and mechanism of therapeutic drugs targeting TL1A and NLRP3.
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