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Abcb1a/Abcb1b-DKO(FVB)
製品ID :
C001493
系統:
FVB/NJCya
状況:
説明:
P-glycoprotein (P-gp), also known as multidrug resistance protein 1 (MDR1), is an ATP-binding cassette transporter that acts as a biological barrier by expelling toxins and foreign substances from cells. P-gp is capable of transporting many structurally and functionally different compounds out of cells [1]. However, the mechanism of MDR1 also prevents the uptake of many cancer treatment drugs by cells, leading to multidrug resistance (MDR) [2]. In normal organisms, MDR1’s distribution in the blood-brain barrier and blood-placenta barrier prevents exogenous drugs and toxins from entering the central nervous system and placenta of the organism, thereby protecting the organism and enabling it to perform normal physiological functions. In pathological conditions, however, the MDR1 in the blood-brain barrier prevents drugs from entering the central nervous system, and in tumor cells, leads to the development of MDR. The evolution of MDR remains one of the major obstacles to controlling or curing cancer [3-4].
In humans, the MDR1 protein is encoded by the ABCB1 gene. In mice, two closely located genes, Abcb1a and Abcb1b, encode the MDR1a and MDR1b subtypes of this protein. Mouse MDR1a and MDR1b have 80% homology with human MDR1. MDR1a and MDR1b have the same function as human MDR1 protein in resisting anticancer drugs. Although mouse MDR1a and MDR1b proteins are distributed in different tissues of the body, their overall distribution is consistent with that of human MDR1 protein [5-6]. In summary, the distribution and function of mouse MDR1a and MDR1b are consistent with those of human MDR1.
This strain is an MDR1 knockout model, in which the human ABCB1 gene’s homologous genes, Abcb1a and Abcb1b, were knocked out in mice using gene editing technology. This model lacks the expression of MDR1 protein and can be used for research in areas such as blood-brain barrier permeability-related diseases and multidrug resistance of anti-tumor drugs.
P-glycoprotein (P-gp), also known as multidrug resistance protein 1 (MDR1), is an ATP-binding cassette transporter that acts as a biological barrier by expelling toxins and foreign substances from cells. P-gp is capable of transporting many structurally and functionally different compounds out of cells [1]. However, the mechanism of MDR1 also prevents the uptake of many cancer treatment drugs by cells, leading to multidrug resistance (MDR) [2]. In normal organisms, MDR1’s distribution in the blood-brain barrier and blood-placenta barrier prevents exogenous drugs and toxins from entering the central nervous system and placenta of the organism, thereby protecting the organism and enabling it to perform normal physiological functions. In pathological conditions, however, the MDR1 in the blood-brain barrier prevents drugs from entering the central nervous system, and in tumor cells, leads to the development of MDR. The evolution of MDR remains one of the major obstacles to controlling or curing cancer [3-4].
In humans, the MDR1 protein is encoded by the ABCB1 gene. In mice, two closely located genes, Abcb1a and Abcb1b, encode the MDR1a and MDR1b subtypes of this protein. Mouse MDR1a and MDR1b have 80% homology with human MDR1. MDR1a and MDR1b have the same function as human MDR1 protein in resisting anticancer drugs. Although mouse MDR1a and MDR1b proteins are distributed in different tissues of the body, their overall distribution is consistent with that of human MDR1 protein [5-6]. In summary, the distribution and function of mouse MDR1a and MDR1b are consistent with those of human MDR1.
This strain is an MDR1 knockout model, in which the human ABCB1 gene’s homologous genes, Abcb1a and Abcb1b, were knocked out in mice using gene editing technology. This model lacks the expression of MDR1 protein and can be used for research in areas such as blood-brain barrier permeability-related diseases and multidrug resistance of anti-tumor drugs.
B6-Fgfr3*neoY367C
製品ID :
C001745
系統:
C57BL/6NCya
状況:
説明:
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).
BALB/c;B6J-Rosa26-hHRAS
製品ID :
I001214
系統:
BALB/c;B6JCya
状況:
説明:
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)
製品ID :
C001693
系統:
C57BL/6NCya
状況:
説明:
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
製品ID :
C001819
系統:
C57BL/6NCya
状況:
説明:
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
製品ID :
C001837
系統:
C57BL/6N;6JCya
状況:
説明:
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
製品ID :
C001772
系統:
C57BL/6NCya
状況:
説明:
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-hSERPINA1
製品ID :
C001697
系統:
C57BL/6JCya
状況:
説明:
The SERPINA1 gene encodes alpha-1 antitrypsin (AAT), a serine protease inhibitor primarily synthesized and secreted by hepatocytes in the liver, with additional expression in immune cells such as macrophages. AAT's main function is to inhibit neutrophil-derived proteases (e.g., elastase) to protect lung tissue from enzymatic degradation. This glycoprotein is crucial for maintaining lung tissue elasticity and regulating inflammatory responses. Mutations in the Serpina1 gene, particularly the Z variant (Glu342Lys), lead to alpha-1 antitrypsin deficiency (AATD), resulting in emphysema and chronic obstructive pulmonary disease (COPD) due to uncontrolled protease activity. Additionally, misfolded AAT accumulation in hepatocytes may cause cirrhosis or hepatocellular carcinoma [1-3]. The affected tissues primarily include the liver and lungs, with the former being damaged by protein aggregation and the latter by tissue destruction. This highlights AAT's systemic role in protease regulation and disease pathology.
In mice, the Serpina1 gene cluster is located on chromosome 12, spanning a 230 kb genomic region, and encompasses five liver-specific human SERPINA1 homologous genes, which are arranged in the following order: Serpina1b, Serpina1d, Serpina1a, Serpina1c, and Serpina1e. The B6-hSERPINA1 mouse is a humanized model constructed by replacing the mouse Serpina1 gene cluster (from upstream of mouse Serpina1e to downstream of mouse Serpina1b) with the human SERPINA1 gene (from upstream to downstream of human SERPINA1). Homozygous B6-hSERPINA1 mice are viable and fertile and can be used to study the pathogenic mechanisms of emphysema and chronic obstructive pulmonary disease (COPD), cirrhosis, and hepatocellular carcinoma, as well as to develop related therapeutic approaches.
The SERPINA1 gene encodes alpha-1 antitrypsin (AAT), a serine protease inhibitor primarily synthesized and secreted by hepatocytes in the liver, with additional expression in immune cells such as macrophages. AAT's main function is to inhibit neutrophil-derived proteases (e.g., elastase) to protect lung tissue from enzymatic degradation. This glycoprotein is crucial for maintaining lung tissue elasticity and regulating inflammatory responses. Mutations in the Serpina1 gene, particularly the Z variant (Glu342Lys), lead to alpha-1 antitrypsin deficiency (AATD), resulting in emphysema and chronic obstructive pulmonary disease (COPD) due to uncontrolled protease activity. Additionally, misfolded AAT accumulation in hepatocytes may cause cirrhosis or hepatocellular carcinoma [1-3]. The affected tissues primarily include the liver and lungs, with the former being damaged by protein aggregation and the latter by tissue destruction. This highlights AAT's systemic role in protease regulation and disease pathology.
In mice, the Serpina1 gene cluster is located on chromosome 12, spanning a 230 kb genomic region, and encompasses five liver-specific human SERPINA1 homologous genes, which are arranged in the following order: Serpina1b, Serpina1d, Serpina1a, Serpina1c, and Serpina1e. The B6-hSERPINA1 mouse is a humanized model constructed by replacing the mouse Serpina1 gene cluster (from upstream of mouse Serpina1e to downstream of mouse Serpina1b) with the human SERPINA1 gene (from upstream to downstream of human SERPINA1). Homozygous B6-hSERPINA1 mice are viable and fertile and can be used to study the pathogenic mechanisms of emphysema and chronic obstructive pulmonary disease (COPD), cirrhosis, and hepatocellular carcinoma, as well as to develop related therapeutic approaches.
B6-hLAG3
製品ID :
C001787
系統:
C57BL/6JCya
状況:
説明:
The Lymphocyte Activation Gene 3 (LAG3), also known as CD223, is a gene encoding a transmembrane protein that acts as an immune checkpoint receptor. It is primarily expressed on activated T cells (CD4+, CD8+, and regulatory T cells), natural killer (NK) cells, and plasmacytoid dendritic cells (pDCs) [1]. LAG3 plays a crucial role in immune regulation and homeostasis by delivering inhibitory signals to immune cells, particularly upon binding to its primary ligand, MHC class II molecules, and other ligands like FGL1. This binding leads to reduced T cell activation, proliferation, cytokine production, and cytolytic activity, ultimately contributing to T cell exhaustion in chronic infections and cancer [2]. Conversely, in autoimmune diseases, dysregulation of LAG3 can lead to rapid, immune-mediated tissue damage [3]. Therefore, LAG3 is implicated in a range of associated diseases, including various cancers (e.g., melanoma, colorectal cancer, non-small cell lung carcinoma, Hodgkin lymphoma, multiple myeloma), chronic infections (e.g., HIV, hepatitis B virus, tuberculosis), and autoimmune disorders (e.g., rheumatoid arthritis, Hashimoto's thyroiditis). Due to its significant role in immune suppression, LAG3 is a major target for cancer immunotherapy, with many anti-LAG3 monoclonal antibodies currently under clinical investigation [4].
The B6-hLAG3 mouse is a humanized model constructed by replacing the endogenous extracellular domain (aa.24~442) of the mouse Lag3 gene with the human LAG3 extracellular domain (aa.23~450). The murine signal peptide (aa.1~23) and aa.443~521 are preserved. B6-hLAG3 mice can be used for research into the pathogenesis of various diseases, including malignant tumors, chronic infections, and autoimmune diseases, as well as for the screening, development, and safety evaluation of LAG3-targeted drugs.
The Lymphocyte Activation Gene 3 (LAG3), also known as CD223, is a gene encoding a transmembrane protein that acts as an immune checkpoint receptor. It is primarily expressed on activated T cells (CD4+, CD8+, and regulatory T cells), natural killer (NK) cells, and plasmacytoid dendritic cells (pDCs) [1]. LAG3 plays a crucial role in immune regulation and homeostasis by delivering inhibitory signals to immune cells, particularly upon binding to its primary ligand, MHC class II molecules, and other ligands like FGL1. This binding leads to reduced T cell activation, proliferation, cytokine production, and cytolytic activity, ultimately contributing to T cell exhaustion in chronic infections and cancer [2]. Conversely, in autoimmune diseases, dysregulation of LAG3 can lead to rapid, immune-mediated tissue damage [3]. Therefore, LAG3 is implicated in a range of associated diseases, including various cancers (e.g., melanoma, colorectal cancer, non-small cell lung carcinoma, Hodgkin lymphoma, multiple myeloma), chronic infections (e.g., HIV, hepatitis B virus, tuberculosis), and autoimmune disorders (e.g., rheumatoid arthritis, Hashimoto's thyroiditis). Due to its significant role in immune suppression, LAG3 is a major target for cancer immunotherapy, with many anti-LAG3 monoclonal antibodies currently under clinical investigation [4].
The B6-hLAG3 mouse is a humanized model constructed by replacing the endogenous extracellular domain (aa.24~442) of the mouse Lag3 gene with the human LAG3 extracellular domain (aa.23~450). The murine signal peptide (aa.1~23) and aa.443~521 are preserved. B6-hLAG3 mice can be used for research into the pathogenesis of various diseases, including malignant tumors, chronic infections, and autoimmune diseases, as well as for the screening, development, and safety evaluation of LAG3-targeted drugs.
B6-hIL2RG
製品ID :
C001801
系統:
C57BL/6NCya
状況:
説明:
The IL2RG (Interleukin 2 Receptor Subunit Gamma) gene, located on the X chromosome, provides instructions for making the common gamma chain protein (also known as CD132 or γc). This protein is a critical signaling component shared by the receptors for several interleukins, including IL-2, IL-4, IL-7, IL-9, IL-15, and IL-21. IL2RG is widely expressed, particularly in lymphoid tissues like the lymph nodes, appendix, thymus, and spleen, as well as in immature blood-forming cells in the bone marrow, and also detected in other tissues such as skin and intestine [1-2]. The common gamma chain is essential for the development, proliferation, and function of various immune cells, including T cells, B cells, and natural killer (NK) cells, by facilitating intracellular signaling pathways such as JAK/STAT, MAPK, and PI3K/AKT, which are crucial for immune system homeostasis [1-2]. Mutations in the IL2RG gene are primarily associated with X-linked severe combined immunodeficiency (X-SCID), a severe inherited disorder causing profound defects in both cellular and humoral immunity, typically affecting males and leading to recurrent, life-threatening infections [3-4]. Less severe "hypomorphic" mutations can cause X-linked combined immunodeficiency (XCID), and IL2RG dysregulation has also been implicated in certain cancers and autoimmune conditions [1].
The B6-hIL2RG mouse is a humanized model, constructed by replacing the coding sequences of the endogenous mouse Il2rg gene with the coding sequences of the human IL2RG gene. B6-hIL2RG mice can be used for research into the pathogenesis of X-linked severe combined immunodeficiency (X-SCID), certain autoimmune diseases, and hematological malignancies, as well as for the screening, development, and safety evaluation of IL2RG-targeted drugs.
The IL2RG (Interleukin 2 Receptor Subunit Gamma) gene, located on the X chromosome, provides instructions for making the common gamma chain protein (also known as CD132 or γc). This protein is a critical signaling component shared by the receptors for several interleukins, including IL-2, IL-4, IL-7, IL-9, IL-15, and IL-21. IL2RG is widely expressed, particularly in lymphoid tissues like the lymph nodes, appendix, thymus, and spleen, as well as in immature blood-forming cells in the bone marrow, and also detected in other tissues such as skin and intestine [1-2]. The common gamma chain is essential for the development, proliferation, and function of various immune cells, including T cells, B cells, and natural killer (NK) cells, by facilitating intracellular signaling pathways such as JAK/STAT, MAPK, and PI3K/AKT, which are crucial for immune system homeostasis [1-2]. Mutations in the IL2RG gene are primarily associated with X-linked severe combined immunodeficiency (X-SCID), a severe inherited disorder causing profound defects in both cellular and humoral immunity, typically affecting males and leading to recurrent, life-threatening infections [3-4]. Less severe "hypomorphic" mutations can cause X-linked combined immunodeficiency (XCID), and IL2RG dysregulation has also been implicated in certain cancers and autoimmune conditions [1].
The B6-hIL2RG mouse is a humanized model, constructed by replacing the coding sequences of the endogenous mouse Il2rg gene with the coding sequences of the human IL2RG gene. B6-hIL2RG mice can be used for research into the pathogenesis of X-linked severe combined immunodeficiency (X-SCID), certain autoimmune diseases, and hematological malignancies, as well as for the screening, development, and safety evaluation of IL2RG-targeted drugs.
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