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B6-hCCR8
Product ID:
C001808
Strain:
C57BL/6NCya
Status:
Description:
The CCR8 gene encodes the C-C chemokine receptor type 8, a 41 kDa G-protein coupled receptor with seven transmembrane regions. This protein functions as a receptor for the chemokine CCL1 (also known as I-309) and is involved in cell migration, particularly for various immune cell types, and thymic cell apoptosis. CCR8 expression is notably found in the thymus and is also highly expressed on subsets of CD4+ memory T lymphocytes (including Th2 effector and regulatory T cells or Tregs), natural killer T (NKT) cells, macrophages, monocytes, and monocyte-derived dendritic cells [1]. Its expression is particularly relevant in inflammatory settings, where it guides immune cells to sites of inflammation and infection, such as in the lungs in asthma, and in the skin in atopic dermatitis [2]. Associated diseases and conditions include allergic disorders (like asthma and atopic dermatitis) due to its role in promoting Th2-biased immune responses, various cancers (e.g., malignant melanoma, hepatocellular carcinoma, cutaneous T-cell lymphomas) where it is highly expressed on tumor-infiltrating Tregs contributing to an immunosuppressive tumor microenvironment, and chronic inflammatory conditions such as chronic obstructive pulmonary disease (COPD) and potentially multiple sclerosis (MS) [3]. CCR8 also acts as an alternative co-receptor for HIV-1 infection [4].
The B6-hCCR8 mouse is a humanized model, constructed by replacing the coding sequences of the endogenous mouse Ccr8 gene with the coding sequences of the human CCR8 gene. B6-hCCR8 mice can be used for research into the pathogenesis of allergic disorders, various cancers, chronic inflammatory conditions, and HIV-1 infection, as well as for the screening, development, and safety evaluation of CCR8-targeted drugs.
The CCR8 gene encodes the C-C chemokine receptor type 8, a 41 kDa G-protein coupled receptor with seven transmembrane regions. This protein functions as a receptor for the chemokine CCL1 (also known as I-309) and is involved in cell migration, particularly for various immune cell types, and thymic cell apoptosis. CCR8 expression is notably found in the thymus and is also highly expressed on subsets of CD4+ memory T lymphocytes (including Th2 effector and regulatory T cells or Tregs), natural killer T (NKT) cells, macrophages, monocytes, and monocyte-derived dendritic cells [1]. Its expression is particularly relevant in inflammatory settings, where it guides immune cells to sites of inflammation and infection, such as in the lungs in asthma, and in the skin in atopic dermatitis [2]. Associated diseases and conditions include allergic disorders (like asthma and atopic dermatitis) due to its role in promoting Th2-biased immune responses, various cancers (e.g., malignant melanoma, hepatocellular carcinoma, cutaneous T-cell lymphomas) where it is highly expressed on tumor-infiltrating Tregs contributing to an immunosuppressive tumor microenvironment, and chronic inflammatory conditions such as chronic obstructive pulmonary disease (COPD) and potentially multiple sclerosis (MS) [3]. CCR8 also acts as an alternative co-receptor for HIV-1 infection [4].
The B6-hCCR8 mouse is a humanized model, constructed by replacing the coding sequences of the endogenous mouse Ccr8 gene with the coding sequences of the human CCR8 gene. B6-hCCR8 mice can be used for research into the pathogenesis of allergic disorders, various cancers, chronic inflammatory conditions, and HIV-1 infection, as well as for the screening, development, and safety evaluation of CCR8-targeted drugs.
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.
B6-H11-hBDCA2 (hCLEC4C)
Product ID:
C001693
Strain:
C57BL/6NCya
Status:
Description:
The CLEC4C gene, also known as BDCA-2 or CD303, encodes a type II transmembrane C-type lectin receptor predominantly expressed by plasmacytoid dendritic cells (pDCs) [1]. This receptor plays a critical role in pDC biology and serves as a key marker for this cell type [2]. The CLEC4C protein, featuring a carbohydrate recognition domain, is implicated in the capture and subsequent processing of antigens, potentially through the recognition of specific glycans and immunoglobulin G [1]. Functionally, CLEC4C acts as a signaling receptor within pDCs, and its engagement can negatively regulate the production of type I interferons, thereby modulating immune responses [2]. Notably, dysregulation of CLEC4C expression and pDC function has been associated with the pathogenesis of autoimmune disorders, including systemic lupus erythematosus (SLE), as well as in the context of certain hematological malignancies [3]. Litifilimab is a monoclonal antibody that targets CLEC4C and is under investigation for the treatment of SLE and other interferonopathies [4].
B6-H11-hCLEC4C mice are humanized models generated by gene editing technology, in which the human CLEC4C genomic DNA was inserted at the H11 safe harbor. This modification does not affect the expression of the mouse homologous gene Clec4b1. This model can be used to study the pathological mechanisms and therapeutic methods of autoimmune disorders and hematological malignancies, as well as the screening and development of CLEC4C-targeted drugs, and preclinical efficacy and safety evaluations.
The CLEC4C gene, also known as BDCA-2 or CD303, encodes a type II transmembrane C-type lectin receptor predominantly expressed by plasmacytoid dendritic cells (pDCs) [1]. This receptor plays a critical role in pDC biology and serves as a key marker for this cell type [2]. The CLEC4C protein, featuring a carbohydrate recognition domain, is implicated in the capture and subsequent processing of antigens, potentially through the recognition of specific glycans and immunoglobulin G [1]. Functionally, CLEC4C acts as a signaling receptor within pDCs, and its engagement can negatively regulate the production of type I interferons, thereby modulating immune responses [2]. Notably, dysregulation of CLEC4C expression and pDC function has been associated with the pathogenesis of autoimmune disorders, including systemic lupus erythematosus (SLE), as well as in the context of certain hematological malignancies [3]. Litifilimab is a monoclonal antibody that targets CLEC4C and is under investigation for the treatment of SLE and other interferonopathies [4].
B6-H11-hCLEC4C mice are humanized models generated by gene editing technology, in which the human CLEC4C genomic DNA was inserted at the H11 safe harbor. This modification does not affect the expression of the mouse homologous gene Clec4b1. This model can be used to study the pathological mechanisms and therapeutic methods of autoimmune disorders and hematological malignancies, as well as the screening and development of CLEC4C-targeted drugs, and preclinical efficacy and safety evaluations.
B6-hTTN
Product ID:
C001819
Strain:
C57BL/6NCya
Status:
Description:
The TTN gene provides instructions for making titin, the largest known protein in the human body, essential for the structure, flexibility, and stability of sarcomeres, the fundamental contractile units of muscle [1]. Titin is primarily expressed in striated muscle, including skeletal muscle and cardiac muscle, where it acts as a molecular spring and scaffold, interacting with other muscle proteins like actin and myosin to maintain sarcomere integrity during muscle contraction and relaxation [2]. The TTN gene undergoes extensive alternative splicing, leading to the production of various titin isoforms with differing elastic properties, which contributes to the diverse mechanical characteristics of different muscle types. Mutations in TTN are a leading cause of various muscle and heart disorders, collectively known as titinopathies. These include familial dilated cardiomyopathy (DCM), a common cause of heart failure characterized by weakening and enlargement of the heart, often due to truncating variants in TTN. Other associated conditions include early-onset myopathy with fatal cardiomyopathy, centronuclear myopathy, limb-girdle muscular dystrophy, and tibial muscular dystrophy [3].
The B6-hTTN mouse is a humanized model constructed via gene-editing technology. The sequence from the ATG start codon to the TAA stop codon of mouse Ttn will be replaced with the sequence from the ATG start codon to the TAA stop codon of human TTN. B6-hTTN mice can be used to study the pathogenesis of hereditary muscle diseases such as familial dilated cardiomyopathy (DCM), early-onset myopathy, and muscular dystrophy, as well as for the screening, development, and safety evaluation of TTN-targeted drugs.
The TTN gene provides instructions for making titin, the largest known protein in the human body, essential for the structure, flexibility, and stability of sarcomeres, the fundamental contractile units of muscle [1]. Titin is primarily expressed in striated muscle, including skeletal muscle and cardiac muscle, where it acts as a molecular spring and scaffold, interacting with other muscle proteins like actin and myosin to maintain sarcomere integrity during muscle contraction and relaxation [2]. The TTN gene undergoes extensive alternative splicing, leading to the production of various titin isoforms with differing elastic properties, which contributes to the diverse mechanical characteristics of different muscle types. Mutations in TTN are a leading cause of various muscle and heart disorders, collectively known as titinopathies. These include familial dilated cardiomyopathy (DCM), a common cause of heart failure characterized by weakening and enlargement of the heart, often due to truncating variants in TTN. Other associated conditions include early-onset myopathy with fatal cardiomyopathy, centronuclear myopathy, limb-girdle muscular dystrophy, and tibial muscular dystrophy [3].
The B6-hTTN mouse is a humanized model constructed via gene-editing technology. The sequence from the ATG start codon to the TAA stop codon of mouse Ttn will be replaced with the sequence from the ATG start codon to the TAA stop codon of human TTN. B6-hTTN mice can be used to study the pathogenesis of hereditary muscle diseases such as familial dilated cardiomyopathy (DCM), early-onset myopathy, and muscular dystrophy, as well as for the screening, development, and safety evaluation of TTN-targeted drugs.
B6-hTL1A/hIL23A
Product ID:
C001837
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 IL23A gene encodes the p19 subunit, a component of interleukin-23 (IL-23), which forms a heterodimer with the p40 subunit (encoded by IL12B) to generate the functional IL-23 cytokine [1]. Primarily expressed by activated dendritic cells, macrophages, and monocytes, IL-23 signals through the IL-23 receptor (IL-23R) complex, activating the JAK-STAT pathway to promote Th17 cell differentiation and maintain IL-17 production. This process drives inflammatory responses and mucosal immunity against extracellular pathogens [6-7]. Genetic polymorphisms within IL23A are strongly associated with autoimmune and inflammatory diseases, including psoriasis, Crohn's disease, and inflammatory bowel disease, due to dysregulated Th17 activity and chronic inflammation [6-7]. Monoclonal antibodies targeting IL-23, such as risankizumab and guselkumab, selectively block the p19 subunit, demonstrating therapeutic efficacy in psoriasis and inflammatory bowel diseases by suppressing pathogenic IL-17/Th17 pathways [8]. While IL-23 plays a role in protective immunity, its overactivation contributes to tissue damage in autoimmune settings, highlighting its dual function in immune regulation and disease pathogenesis [6-9].
B6-hTL1A/hIL23A mice are humanized models generated by crossing B6-hTL1A (TNFSF15) mice (Catalog No.: C001603) with B6-hIL23A mice (Catalog No.: C001618). These mice are suitable for studying the pathological mechanisms and therapeutic strategies of allergic and inflammatory diseases, immune-related disorders, and cancer, as well as for the screening, development, and preclinical evaluation of TL1A/IL23A-targeted drugs.
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 IL23A gene encodes the p19 subunit, a component of interleukin-23 (IL-23), which forms a heterodimer with the p40 subunit (encoded by IL12B) to generate the functional IL-23 cytokine [1]. Primarily expressed by activated dendritic cells, macrophages, and monocytes, IL-23 signals through the IL-23 receptor (IL-23R) complex, activating the JAK-STAT pathway to promote Th17 cell differentiation and maintain IL-17 production. This process drives inflammatory responses and mucosal immunity against extracellular pathogens [6-7]. Genetic polymorphisms within IL23A are strongly associated with autoimmune and inflammatory diseases, including psoriasis, Crohn's disease, and inflammatory bowel disease, due to dysregulated Th17 activity and chronic inflammation [6-7]. Monoclonal antibodies targeting IL-23, such as risankizumab and guselkumab, selectively block the p19 subunit, demonstrating therapeutic efficacy in psoriasis and inflammatory bowel diseases by suppressing pathogenic IL-17/Th17 pathways [8]. While IL-23 plays a role in protective immunity, its overactivation contributes to tissue damage in autoimmune settings, highlighting its dual function in immune regulation and disease pathogenesis [6-9].
B6-hTL1A/hIL23A mice are humanized models generated by crossing B6-hTL1A (TNFSF15) mice (Catalog No.: C001603) with B6-hIL23A mice (Catalog No.: C001618). These mice are suitable for studying the pathological mechanisms and therapeutic strategies of allergic and inflammatory diseases, immune-related disorders, and cancer, as well as for the screening, development, and preclinical evaluation of TL1A/IL23A-targeted drugs.
B6-hIL13/hIL23A
Product ID:
C001772
Strain:
C57BL/6NCya
Status:
Description:
Interleukin-13, encoded by the IL13 gene, is a key type 2 immune response cytokine, predominantly expressed by activated Th2 helper T cells, type 2 innate lymphoid cells (ILC2s), and mast cells, and central to type 2 immune responses elicited by allergens or other stimuli [1]. The IL-13 protein, a ~13 kDa molecule with a four-helix bundle structure, mediates its biological effects by binding to the cell surface receptor IL-13Rα1 and recruiting the IL-4Rα chain to form a functional receptor complex, thereby activating the downstream JAK/STAT6 signaling pathway [2]. Key functions of IL-13 include promoting B cell maturation and plasma cell differentiation, inducing IgE isotype switching, and suppressing the pro-inflammatory activity of macrophages, leading to reduced production of pro-inflammatory cytokines and chemokines [3]. Furthermore, IL-13 induces goblet cell hyperplasia, promotes mucus secretion, and contributes to airway remodeling and fibrosis [4]. Numerous studies have established the critical role of IL-13 in the pathogenesis of various diseases, including asthma, allergic rhinitis, atopic dermatitis, and eosinophilic esophagitis [1-4]. Consequently, targeting IL-13 and its signaling pathways has become a significant therapeutic strategy for these conditions; for example, the monoclonal antibody Dupilumab, which simultaneously blocks IL-4 and IL-13 signaling, has demonstrated substantial efficacy in treating diverse type 2 inflammation-related diseases [5]. Thus, IL-13 represents a promising therapeutic target for allergic and inflammatory disorders.
The IL23A gene encodes the p19 subunit, a component of interleukin-23 (IL-23), which forms a heterodimer with the p40 subunit (encoded by IL12B) to generate the functional IL-23 cytokine. Primarily expressed by activated dendritic cells, macrophages, and monocytes, IL-23 signals through the IL-23 receptor (IL-23R) complex, activating the JAK-STAT pathway to promote Th17 cell differentiation and maintain IL-17 production. This process drives inflammatory responses and mucosal immunity against extracellular pathogens [6-7]. Genetic polymorphisms within IL23A are strongly associated with autoimmune and inflammatory diseases, including psoriasis, Crohn's disease, and inflammatory bowel disease, due to dysregulated Th17 activity and chronic inflammation [6-7]. Monoclonal antibodies targeting IL-23, such as risankizumab and guselkumab, selectively block the p19 subunit, demonstrating therapeutic efficacy in psoriasis and inflammatory bowel diseases by suppressing pathogenic IL-17/Th17 pathways [8]. While IL-23 plays a role in protective immunity, its overactivation contributes to tissue damage in autoimmune settings, highlighting its dual function in immune regulation and disease pathogenesis [6-9].
B6-hIL13/hIL23A mice are humanized models generated by crossing B6-hIL13 mice (Product No.: C001634) with B6-hIL23A mice (Product No.: C001618). These mice are suitable for studying the pathological mechanisms and therapeutic strategies of allergic and inflammatory diseases, immune-related disorders, and cancer, as well as for the screening, development, and preclinical evaluation of IL13/IL23A-targeted drugs.
Interleukin-13, encoded by the IL13 gene, is a key type 2 immune response cytokine, predominantly expressed by activated Th2 helper T cells, type 2 innate lymphoid cells (ILC2s), and mast cells, and central to type 2 immune responses elicited by allergens or other stimuli [1]. The IL-13 protein, a ~13 kDa molecule with a four-helix bundle structure, mediates its biological effects by binding to the cell surface receptor IL-13Rα1 and recruiting the IL-4Rα chain to form a functional receptor complex, thereby activating the downstream JAK/STAT6 signaling pathway [2]. Key functions of IL-13 include promoting B cell maturation and plasma cell differentiation, inducing IgE isotype switching, and suppressing the pro-inflammatory activity of macrophages, leading to reduced production of pro-inflammatory cytokines and chemokines [3]. Furthermore, IL-13 induces goblet cell hyperplasia, promotes mucus secretion, and contributes to airway remodeling and fibrosis [4]. Numerous studies have established the critical role of IL-13 in the pathogenesis of various diseases, including asthma, allergic rhinitis, atopic dermatitis, and eosinophilic esophagitis [1-4]. Consequently, targeting IL-13 and its signaling pathways has become a significant therapeutic strategy for these conditions; for example, the monoclonal antibody Dupilumab, which simultaneously blocks IL-4 and IL-13 signaling, has demonstrated substantial efficacy in treating diverse type 2 inflammation-related diseases [5]. Thus, IL-13 represents a promising therapeutic target for allergic and inflammatory disorders.
The IL23A gene encodes the p19 subunit, a component of interleukin-23 (IL-23), which forms a heterodimer with the p40 subunit (encoded by IL12B) to generate the functional IL-23 cytokine. Primarily expressed by activated dendritic cells, macrophages, and monocytes, IL-23 signals through the IL-23 receptor (IL-23R) complex, activating the JAK-STAT pathway to promote Th17 cell differentiation and maintain IL-17 production. This process drives inflammatory responses and mucosal immunity against extracellular pathogens [6-7]. Genetic polymorphisms within IL23A are strongly associated with autoimmune and inflammatory diseases, including psoriasis, Crohn's disease, and inflammatory bowel disease, due to dysregulated Th17 activity and chronic inflammation [6-7]. Monoclonal antibodies targeting IL-23, such as risankizumab and guselkumab, selectively block the p19 subunit, demonstrating therapeutic efficacy in psoriasis and inflammatory bowel diseases by suppressing pathogenic IL-17/Th17 pathways [8]. While IL-23 plays a role in protective immunity, its overactivation contributes to tissue damage in autoimmune settings, highlighting its dual function in immune regulation and disease pathogenesis [6-9].
B6-hIL13/hIL23A mice are humanized models generated by crossing B6-hIL13 mice (Product No.: C001634) with B6-hIL23A mice (Product No.: C001618). These mice are suitable for studying the pathological mechanisms and therapeutic strategies of allergic and inflammatory diseases, immune-related disorders, and cancer, as well as for the screening, development, and preclinical evaluation of IL13/IL23A-targeted drugs.
B6-hCOL7A1
Product ID:
C001428
Strain:
C57BL/6NCya
Status:
Description:
Epidermolysis bullosa (EB) is a hereditary skin disease characterized by the formation of blisters and bullae on the skin and mucous membranes after minor trauma or friction. Common clinical symptoms include blisters, blood blisters, and erosion on the skin. According to the different sites of onset, hereditary EB can be divided into three types: Epidermolysis Bullosa Simplex (EBS), Junctional Epidermolysis Bullosa (JEB), and Dystrophic Epidermolysis Bullosa (DEB). Mutations in the COL7A1 gene cause Dystrophic Epidermolysis Bullosa (DEB), and the different clinical phenotypes presented by DEB are related to the mutation sites and forms of the COL7A1 gene. The COL7A1 gene encodes type VII collagen, which forms anchoring fibrils that bind dermal tissue to epidermal tissue. Functional anchoring fibril deficiency caused by COL7A1 mutations makes the patient’s skin extremely fragile and easily blistered or torn due to minor friction or trauma. At present, 324 pathogenic mutations of the COL7A1 gene related to DEB have been found, including nonsense, missense, deletion, insertion, splicing, and regulation [1].
The current DEB treatment pipeline is mainly based on gene therapy and small nucleic acid drugs, including ASO drugs, siRNA drugs, and gene therapy based on CRISPR and AAV vector delivery. Among them, COL7A1 is the most important therapeutic target. B-Vec, developed by Krystal Biotech delivers functional COL7A1 genes to skin cells of DEB patients with COL7A1 mutations through HSV-1 vectors to produce functional proteins to promote wound healing and was the first approved gene therapy drug for the DEB [2-5]. In addition, since most ASO, siRNA, and CRISPR-based therapies target human COL7A1 genes, considering the genetic differences between animals and humans, humanizing mouse genes will help promote further clinical translation of therapies targeting COL7A1. This strain is a mouse Col7a1 gene humanized model and can be used for research on DEB. The homozygous B6-hCOL7A1 mice are viable and fertile [6-7]. 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 EB.
Epidermolysis bullosa (EB) is a hereditary skin disease characterized by the formation of blisters and bullae on the skin and mucous membranes after minor trauma or friction. Common clinical symptoms include blisters, blood blisters, and erosion on the skin. According to the different sites of onset, hereditary EB can be divided into three types: Epidermolysis Bullosa Simplex (EBS), Junctional Epidermolysis Bullosa (JEB), and Dystrophic Epidermolysis Bullosa (DEB). Mutations in the COL7A1 gene cause Dystrophic Epidermolysis Bullosa (DEB), and the different clinical phenotypes presented by DEB are related to the mutation sites and forms of the COL7A1 gene. The COL7A1 gene encodes type VII collagen, which forms anchoring fibrils that bind dermal tissue to epidermal tissue. Functional anchoring fibril deficiency caused by COL7A1 mutations makes the patient’s skin extremely fragile and easily blistered or torn due to minor friction or trauma. At present, 324 pathogenic mutations of the COL7A1 gene related to DEB have been found, including nonsense, missense, deletion, insertion, splicing, and regulation [1].
The current DEB treatment pipeline is mainly based on gene therapy and small nucleic acid drugs, including ASO drugs, siRNA drugs, and gene therapy based on CRISPR and AAV vector delivery. Among them, COL7A1 is the most important therapeutic target. B-Vec, developed by Krystal Biotech delivers functional COL7A1 genes to skin cells of DEB patients with COL7A1 mutations through HSV-1 vectors to produce functional proteins to promote wound healing and was the first approved gene therapy drug for the DEB [2-5]. In addition, since most ASO, siRNA, and CRISPR-based therapies target human COL7A1 genes, considering the genetic differences between animals and humans, humanizing mouse genes will help promote further clinical translation of therapies targeting COL7A1. This strain is a mouse Col7a1 gene humanized model and can be used for research on DEB. The homozygous B6-hCOL7A1 mice are viable and fertile [6-7]. 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 EB.
B6-hATP7B
Product ID:
I001130
Strain:
C57BL/6NCya
Status:
Description:
Hepatolenticular degeneration (HLD), also known as Wilson disease (WD), is an autosomal recessive copper transport disorder that can lead to liver failure. The incidence rate is about 1:30,000 [1]. The clinical manifestations of HLD mainly include chronic liver damage, and neurological and psychiatric symptoms, and can occasionally cause acute liver failure and hemolytic anemia. Its typical manifestation is the combination of liver disease and movement disorders in adolescence or early adulthood, but there is a large variation in phenotypic differences among patients, and up to 60% of patients have neurological or psychiatric symptoms [2]. Studies have shown that mutations in the ATP7B gene are associated with HLD. The characteristic feature is that with the loss of functional ATP7B protein, the clearance of excess copper is affected, leading to copper accumulation to toxic levels, damaging tissues and organs such as the liver and brain [1, 3-4]. The copper ion transport ATPase β-peptide encoded by the ATP7B gene is a member of the P-type cation transport ATPase family. This family uses the energy stored in ATP to transport metals into and out of cells. The ATP7B protein consists of multiple transmembrane domains, an ATPase consensus sequence, a hinge domain, a phosphorylation site, and at least two putative copper-binding sites [5]. This protein mainly exists in the liver, with small amounts found in the kidneys and brain. Its function as a copper transport ATPase plays a role in transporting copper from the liver to other parts of the body.
Hepatolenticular degeneration (HLD) treatments are mainly categorized into pharmacotherapy and surgical intervention. Pharmacotherapy is aimed at alleviating symptoms, preventing disease progression, and preventing complications, while surgery is typically liver transplantation. With the continuous exploration of the genetic etiology of Wilson’s disease, targeted gene therapy is expected to become the next "star therapy." Currently, multiple biotechnology companies and research institutions, including Prime Medicine and LogicBio Therapeutics, are developing a variety of gene editing therapies based on CRISPR/Cas9, Prime Editor, or other technologies to correct mutations in the ATP7B gene or replace the mutated ATP7B gene as a whole. These highly promising therapies are currently in preclinical studies [6-15]. Given that these gene editing therapies require precise targeting of the human ATP7B gene, humanizing mouse genes will help accelerate the entry of gene therapy into the clinical stage. This strain is a mouse Atp7b gene humanized model and can be used for HLD. The homozygous B6-hATP7B 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 to meet the experimental needs.
Hepatolenticular degeneration (HLD), also known as Wilson disease (WD), is an autosomal recessive copper transport disorder that can lead to liver failure. The incidence rate is about 1:30,000 [1]. The clinical manifestations of HLD mainly include chronic liver damage, and neurological and psychiatric symptoms, and can occasionally cause acute liver failure and hemolytic anemia. Its typical manifestation is the combination of liver disease and movement disorders in adolescence or early adulthood, but there is a large variation in phenotypic differences among patients, and up to 60% of patients have neurological or psychiatric symptoms [2]. Studies have shown that mutations in the ATP7B gene are associated with HLD. The characteristic feature is that with the loss of functional ATP7B protein, the clearance of excess copper is affected, leading to copper accumulation to toxic levels, damaging tissues and organs such as the liver and brain [1, 3-4]. The copper ion transport ATPase β-peptide encoded by the ATP7B gene is a member of the P-type cation transport ATPase family. This family uses the energy stored in ATP to transport metals into and out of cells. The ATP7B protein consists of multiple transmembrane domains, an ATPase consensus sequence, a hinge domain, a phosphorylation site, and at least two putative copper-binding sites [5]. This protein mainly exists in the liver, with small amounts found in the kidneys and brain. Its function as a copper transport ATPase plays a role in transporting copper from the liver to other parts of the body.
Hepatolenticular degeneration (HLD) treatments are mainly categorized into pharmacotherapy and surgical intervention. Pharmacotherapy is aimed at alleviating symptoms, preventing disease progression, and preventing complications, while surgery is typically liver transplantation. With the continuous exploration of the genetic etiology of Wilson’s disease, targeted gene therapy is expected to become the next "star therapy." Currently, multiple biotechnology companies and research institutions, including Prime Medicine and LogicBio Therapeutics, are developing a variety of gene editing therapies based on CRISPR/Cas9, Prime Editor, or other technologies to correct mutations in the ATP7B gene or replace the mutated ATP7B gene as a whole. These highly promising therapies are currently in preclinical studies [6-15]. Given that these gene editing therapies require precise targeting of the human ATP7B gene, humanizing mouse genes will help accelerate the entry of gene therapy into the clinical stage. This strain is a mouse Atp7b gene humanized model and can be used for HLD. The homozygous B6-hATP7B 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 to meet the experimental needs.
B6-Fgfr3*neoY367C
Product ID:
C001745
Strain:
C57BL/6NCya
Status:
Description:
The FGFR3 gene encodes Fibroblast Growth Factor Receptor 3, a transmembrane receptor tyrosine kinase that plays a crucial role in regulating cell growth, differentiation, and apoptosis. It is widely expressed in various tissues, including the brain, kidney, testis, lung, small intestine, and liver, but is particularly important in cells forming bones, especially within the growth plate of cartilage [1]. The Fdfr3*Y367C mutation, which corresponds to the human Y373C mutation (a gain-of-function mutation), leads to constitutive activation of the FGFR3 protein. This overactivity disrupts normal chondrocyte proliferation and differentiation, impairing endochondral ossification and linear bone growth [2]. As a result, this mutation is significantly associated with severe skeletal dysplasias, including Thanatophoric Dysplasia type I (TDI) and Achondroplasia (ACH), the most common form of short-limbed dwarfism, characterized by disproportionate short stature, macrocephaly, and other skeletal deformities [3]. Y373C is one of the common activating mutations of FGFR3, accounting for approximately 50% of patients with thanatophoric dysplasia (TD-type I), but a lower proportion in the more prevalent achondroplasia (ACH) (ACH is primarily dominated by the G380R mutation). In reported literature, the Fgfr3*Y367C mutation is typically used to construct mouse models in a heterozygous form, which corresponds to the heterozygous nature of this mutation in human clinical patients. Its dominant-negative effect is sufficient to cause the disease. Heterozygous mice have an average lifespan of 6-8 weeks and exhibit severe disease phenotypes [4].
B6-Fgfr3*neoY367C mice are obtained by introducing the Y367C mutation into the mouse Fgfr3 gene using gene editing technology. Internal preliminary data show that homozygous B6-Fgfr3*neoY367C mice die at 3 weeks. This model can be used to study the mechanisms and therapeutic approaches for diseases such as achondroplasia (ACH) and thanatophoric dysplasia (TD).
The FGFR3 gene encodes Fibroblast Growth Factor Receptor 3, a transmembrane receptor tyrosine kinase that plays a crucial role in regulating cell growth, differentiation, and apoptosis. It is widely expressed in various tissues, including the brain, kidney, testis, lung, small intestine, and liver, but is particularly important in cells forming bones, especially within the growth plate of cartilage [1]. The Fdfr3*Y367C mutation, which corresponds to the human Y373C mutation (a gain-of-function mutation), leads to constitutive activation of the FGFR3 protein. This overactivity disrupts normal chondrocyte proliferation and differentiation, impairing endochondral ossification and linear bone growth [2]. As a result, this mutation is significantly associated with severe skeletal dysplasias, including Thanatophoric Dysplasia type I (TDI) and Achondroplasia (ACH), the most common form of short-limbed dwarfism, characterized by disproportionate short stature, macrocephaly, and other skeletal deformities [3]. Y373C is one of the common activating mutations of FGFR3, accounting for approximately 50% of patients with thanatophoric dysplasia (TD-type I), but a lower proportion in the more prevalent achondroplasia (ACH) (ACH is primarily dominated by the G380R mutation). In reported literature, the Fgfr3*Y367C mutation is typically used to construct mouse models in a heterozygous form, which corresponds to the heterozygous nature of this mutation in human clinical patients. Its dominant-negative effect is sufficient to cause the disease. Heterozygous mice have an average lifespan of 6-8 weeks and exhibit severe disease phenotypes [4].
B6-Fgfr3*neoY367C mice are obtained by introducing the Y367C mutation into the mouse Fgfr3 gene using gene editing technology. Internal preliminary data show that homozygous B6-Fgfr3*neoY367C mice die at 3 weeks. This model can be used to study the mechanisms and therapeutic approaches for diseases such as achondroplasia (ACH) and thanatophoric dysplasia (TD).
B6-huDLL3
Product ID:
C001854
Strain:
C57BL/6NCya
Status:
Description:
The DLL3 (Delta-like canonical Notch ligand 3) gene encodes a transmembrane protein belonging to the Delta/Serrate/Lag-2 (DSL) family of ligands. Functioning within the highly conserved Notch signaling pathway, DLL3 exhibits a unique, inhibitory role, contrasting with the canonical activating function of other Notch ligands. It is believed to antagonize Notch signaling by preventing ligand-receptor interactions or by promoting receptor degradation, a mechanism critical for establishing proper cell fate decisions during development [1]. This is particularly evident in the formation of somites, where DLL3's function is essential for the rhythmic segmentation of the presomitic mesoderm [2]. While its expression is largely restricted to fetal tissues and progenitor cells in healthy adults, DLL3 is ectopically and highly expressed in a number of neuroendocrine tumors, including small cell lung cancer (SCLC), making it a promising therapeutic target. Pathogenic variants in the DLL3 gene are directly linked to Spondylocostal dysostosis type 1, a congenital disorder of vertebral segmentation [3].
The B6-huDLL3 mice are a humanized model constructed through gene editing technology, in which the mouse Dll3 endogenous extracellular domain is replaced with the human DLL3 extracellular domain. The murine signal peptide and transmembrane-cytoplasmic region are preserved. This model can be used for the study of the pathological mechanisms and treatment methods of DLL3-highly-expressed malignant tumors and Spondylocostal dysostosis type 1. It can also be applied to the development of DLL3-targeted drugs.
The DLL3 (Delta-like canonical Notch ligand 3) gene encodes a transmembrane protein belonging to the Delta/Serrate/Lag-2 (DSL) family of ligands. Functioning within the highly conserved Notch signaling pathway, DLL3 exhibits a unique, inhibitory role, contrasting with the canonical activating function of other Notch ligands. It is believed to antagonize Notch signaling by preventing ligand-receptor interactions or by promoting receptor degradation, a mechanism critical for establishing proper cell fate decisions during development [1]. This is particularly evident in the formation of somites, where DLL3's function is essential for the rhythmic segmentation of the presomitic mesoderm [2]. While its expression is largely restricted to fetal tissues and progenitor cells in healthy adults, DLL3 is ectopically and highly expressed in a number of neuroendocrine tumors, including small cell lung cancer (SCLC), making it a promising therapeutic target. Pathogenic variants in the DLL3 gene are directly linked to Spondylocostal dysostosis type 1, a congenital disorder of vertebral segmentation [3].
The B6-huDLL3 mice are a humanized model constructed through gene editing technology, in which the mouse Dll3 endogenous extracellular domain is replaced with the human DLL3 extracellular domain. The murine signal peptide and transmembrane-cytoplasmic region are preserved. This model can be used for the study of the pathological mechanisms and treatment methods of DLL3-highly-expressed malignant tumors and Spondylocostal dysostosis type 1. It can also be applied to the development of DLL3-targeted drugs.
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