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AG129(IFNα/β/γR-DKO)
Product ID:
C001893
Strain:
129S2/SvPasCya
Status:
Description:
Interferons (IFNs) are potent cytokines that serve as a critical component of the body's first line of defense against viral infections, playing a key role in inflammation and immune control by directly inducing pathogen-inhibiting molecules that suppress viral replication [1]. Arthropod-borne viruses (arboviruses) like Dengue virus (DENV), Zika virus (ZIKV), and Yellow Fever virus (YFV) encode proteins that antagonize the IFN response, helping these viruses evade host immunity and maintain sufficient viral loads in the blood (viremia) to sustain the vector-host transmission. Arboviruses pose a significant public health threat, affecting around 3.9 billion people in tropical and subtropical regions. However, most preclinical studies suggest that arboviruses cannot inhibit IFN responses in mice, rendering immunocompetent mice resistant to infection, with low viral loads and limited circulation, thus limiting their use in infection research [2-3]. As a result, immunodeficient mouse models with defects in multiple IFN signaling pathways have become essential tools for studying arbovirus pathogenesis and vaccine development [2-4].
Studies have demonstrated that wild-type mice of strains like C57BL/6, CD-1, or 129 rarely exhibit clinical symptoms after infection with arboviruses such as ZIKV. However, the virus has been detected in the blood, ovaries, and spleen of ZIKV-infected 129 mice, suggesting that this strain may be more susceptible to arboviruses [5-6]. Because the virus can persist in the bloodstream without causing disease or death, the 129 strain can be used to evaluate the teratogenic effects of such viruses. Furthermore, the 129 strain is commonly used in interferon signaling-deficient models related to other viral infections [7-8].
The IFNAR1 gene encodes a key component of the type I IFN receptor, while the IFNGR1 gene encodes the ligand-binding chain (α) of the type II (γ) IFN receptor. AG129(IFNα/β/γR-DKO) mice, which are knockout models for both the type I (α/β) IFN receptor (Ifnar1) and the type II (γ) IFN receptor (Ifngr1), lack functional IFNAR1 and IFNGR1 proteins, resulting in deficiencies in α/β/γ interferon receptor signaling and heightened susceptibility to viral infections. Homozygous AG129(IFNα/β/γR-DKO) mice are viable and fertile, and exhibit increased sensitivity to arboviral infections, generating viremia similar to that seen in humans. Compared to IFNα/β/γR KO mice on the C57BL/6 background, the 129-background AG129(IFNα/β/γR-DKO) mice exhibit more pronounced neurological symptoms after infection [6,9].
Interferons (IFNs) are potent cytokines that serve as a critical component of the body's first line of defense against viral infections, playing a key role in inflammation and immune control by directly inducing pathogen-inhibiting molecules that suppress viral replication [1]. Arthropod-borne viruses (arboviruses) like Dengue virus (DENV), Zika virus (ZIKV), and Yellow Fever virus (YFV) encode proteins that antagonize the IFN response, helping these viruses evade host immunity and maintain sufficient viral loads in the blood (viremia) to sustain the vector-host transmission. Arboviruses pose a significant public health threat, affecting around 3.9 billion people in tropical and subtropical regions. However, most preclinical studies suggest that arboviruses cannot inhibit IFN responses in mice, rendering immunocompetent mice resistant to infection, with low viral loads and limited circulation, thus limiting their use in infection research [2-3]. As a result, immunodeficient mouse models with defects in multiple IFN signaling pathways have become essential tools for studying arbovirus pathogenesis and vaccine development [2-4].
Studies have demonstrated that wild-type mice of strains like C57BL/6, CD-1, or 129 rarely exhibit clinical symptoms after infection with arboviruses such as ZIKV. However, the virus has been detected in the blood, ovaries, and spleen of ZIKV-infected 129 mice, suggesting that this strain may be more susceptible to arboviruses [5-6]. Because the virus can persist in the bloodstream without causing disease or death, the 129 strain can be used to evaluate the teratogenic effects of such viruses. Furthermore, the 129 strain is commonly used in interferon signaling-deficient models related to other viral infections [7-8].
The IFNAR1 gene encodes a key component of the type I IFN receptor, while the IFNGR1 gene encodes the ligand-binding chain (α) of the type II (γ) IFN receptor. AG129(IFNα/β/γR-DKO) mice, which are knockout models for both the type I (α/β) IFN receptor (Ifnar1) and the type II (γ) IFN receptor (Ifngr1), lack functional IFNAR1 and IFNGR1 proteins, resulting in deficiencies in α/β/γ interferon receptor signaling and heightened susceptibility to viral infections. Homozygous AG129(IFNα/β/γR-DKO) mice are viable and fertile, and exhibit increased sensitivity to arboviral infections, generating viremia similar to that seen in humans. Compared to IFNα/β/γR KO mice on the C57BL/6 background, the 129-background AG129(IFNα/β/γR-DKO) mice exhibit more pronounced neurological symptoms after infection [6,9].
A129(Ifnar1-KO)
Product ID:
C001891
Strain:
129S2/SvPasCya
Status:
Description:
Interferons (IFNs) are potent cytokines that serve as a critical component of the body's first line of defense against viral infections, playing a key role in inflammation and immune control by directly inducing pathogen-inhibiting molecules that suppress viral replication [1]. Arthropod-borne viruses (arboviruses) like Dengue virus (DENV), Zika virus (ZIKV), and Yellow Fever virus (YFV) encode proteins that antagonize the IFN response, helping these viruses evade host immunity and maintain sufficient viral loads in the blood (viremia) to sustain the vector-host transmission. Arboviruses pose a significant public health threat, affecting around 3.9 billion people in tropical and subtropical regions. However, most preclinical studies suggest that arboviruses cannot inhibit IFN responses in mice, rendering immunocompetent mice resistant to infection, with low viral loads and limited circulation, thus limiting their use in infection research [2-3]. As a result, immunodeficient mouse models with defects in multiple IFN signaling pathways have become essential tools for studying arbovirus pathogenesis and vaccine development [2-4].
Studies have demonstrated that wild-type mice of strains like C57BL/6, CD-1, or 129 rarely exhibit clinical symptoms after infection with arboviruses such as ZIKV. However, the virus has been detected in the blood, ovaries, and spleen of ZIKV-infected 129 mice, suggesting that this strain may be more susceptible to arboviruses [5-6]. Because the virus can persist in the bloodstream without causing disease or death, the 129 strain can be used to evaluate the teratogenic effects of such viruses. Furthermore, the 129 strain is commonly used in interferon signaling-deficient models related to other viral infections [7-8]. The IFNAR1 gene encodes a protein that is an essential component of the type I interferon (IFN) receptor, playing a critical role in the antiviral and immune responses. IFNAR1 is primarily expressed in immune cells, such as lymphocytes and dendritic cells, and various tissues, including the liver, brain, and skin. Defects in IFNAR1, whether due to mutations or regulatory abnormalities, can lead to severe diseases such as systemic lupus erythematosus, where excessive immune activation results in tissue damage, and certain cancers. Other diseases associated with IFNAR1 include hepatitis C, yellow fever, measles, papilloma, and viral infections.
The A129(Ifnar1-KO) mice on a 129 background are a type I (α/β) interferon receptor (Ifnar1) gene knockout model. The absence of the IFNAR1 protein in these mice leads to a lack of type I IFN receptor function, thereby reducing immune response and increasing susceptibility to viral infections. Homozygous A129(Ifnar1-KO) mice are viable and fertile, but they show increased susceptibility to arbovirus infections.
Interferons (IFNs) are potent cytokines that serve as a critical component of the body's first line of defense against viral infections, playing a key role in inflammation and immune control by directly inducing pathogen-inhibiting molecules that suppress viral replication [1]. Arthropod-borne viruses (arboviruses) like Dengue virus (DENV), Zika virus (ZIKV), and Yellow Fever virus (YFV) encode proteins that antagonize the IFN response, helping these viruses evade host immunity and maintain sufficient viral loads in the blood (viremia) to sustain the vector-host transmission. Arboviruses pose a significant public health threat, affecting around 3.9 billion people in tropical and subtropical regions. However, most preclinical studies suggest that arboviruses cannot inhibit IFN responses in mice, rendering immunocompetent mice resistant to infection, with low viral loads and limited circulation, thus limiting their use in infection research [2-3]. As a result, immunodeficient mouse models with defects in multiple IFN signaling pathways have become essential tools for studying arbovirus pathogenesis and vaccine development [2-4].
Studies have demonstrated that wild-type mice of strains like C57BL/6, CD-1, or 129 rarely exhibit clinical symptoms after infection with arboviruses such as ZIKV. However, the virus has been detected in the blood, ovaries, and spleen of ZIKV-infected 129 mice, suggesting that this strain may be more susceptible to arboviruses [5-6]. Because the virus can persist in the bloodstream without causing disease or death, the 129 strain can be used to evaluate the teratogenic effects of such viruses. Furthermore, the 129 strain is commonly used in interferon signaling-deficient models related to other viral infections [7-8]. The IFNAR1 gene encodes a protein that is an essential component of the type I interferon (IFN) receptor, playing a critical role in the antiviral and immune responses. IFNAR1 is primarily expressed in immune cells, such as lymphocytes and dendritic cells, and various tissues, including the liver, brain, and skin. Defects in IFNAR1, whether due to mutations or regulatory abnormalities, can lead to severe diseases such as systemic lupus erythematosus, where excessive immune activation results in tissue damage, and certain cancers. Other diseases associated with IFNAR1 include hepatitis C, yellow fever, measles, papilloma, and viral infections.
The A129(Ifnar1-KO) mice on a 129 background are a type I (α/β) interferon receptor (Ifnar1) gene knockout model. The absence of the IFNAR1 protein in these mice leads to a lack of type I IFN receptor function, thereby reducing immune response and increasing susceptibility to viral infections. Homozygous A129(Ifnar1-KO) mice are viable and fertile, but they show increased susceptibility to arbovirus infections.
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.
BALB/c-Zap70*W163C (SKG)
Product ID:
C001535
Strain:
BALB/cAnCya
Status:
Description:
The Zeta-chain-associated protein kinase, encoded by the ZAP70 gene, is a member of the protein tyrosine kinase family and plays a crucial role in T cell development, activation, and lymphocyte activation. Upon stimulation of the T cell antigen receptor (TCR), the ZAP70 protein is phosphorylated on tyrosine residues and, together with Src family kinases Lck and Fyn, plays a role in the initial steps of TCR-mediated signal transduction [1]. ZAP70 plays a key role in T cell signal transduction and is vital for thymocyte development. Defects in the ZAP70 protein can lead to severe combined immunodeficiency (SCID), characterized by the selective absence of CD8-positive T cells. Moreover, the expression of ZAP70 in B cells is associated with developing chronic lymphocytic leukemia (CLL) [1-2].
SKG mice are a BALB/c background strain carrying the W163C mutation in the Zap70 gene. This mutation alters the binding of the ZAP70 protein to the CD3ζ chain based on the immunoreceptor tyrosine-based activation motif (ITAM), thereby reducing TCR signal transduction and allowing autoreactive T cells to escape negative selection in the thymus and migrate to the periphery [3]. Under natural conditions or upon administration of serum complement activators, mice develop chronic autoimmune arthritis mediated by Th17 cells [4-5]. Furthermore, studies have shown that stimulation through various methods such as β-glucan or mannan can induce the disease process of rheumatoid arthritis (RA) in SKG mice, resulting in symptoms of autoimmune diseases such as ankylosing spondylitis (AS), psoriasis-like skin inflammation, RA-associated interstitial lung disease (RA-ILD), and Crohn’s disease-like ileitis [6-9].
The BALB/c-Zap70*W163C (SKG) mouse (referred to as the SKG mouse) is an autoimmune disease research model constructed by Cyagen through gene editing technology to introduce the W163C mutation into the Zap70 gene of BALB/c mice. The phenotype of this model is similar to that of the classic SKG mouse [10]. Under SPF conditions, upon triggering innate immune activation (such as β-glucan induction), it can present a variety of autoimmune disease phenotypes. Therefore, this mouse can be used for research on autoimmune diseases such as rheumatoid arthritis (RA), ankylosing spondylitis (AS), psoriasis-like skin inflammation, RA-associated interstitial lung disease (RA-ILD), and Crohn’s disease-like ileitis, as well as T cell signal transduction.
The Zeta-chain-associated protein kinase, encoded by the ZAP70 gene, is a member of the protein tyrosine kinase family and plays a crucial role in T cell development, activation, and lymphocyte activation. Upon stimulation of the T cell antigen receptor (TCR), the ZAP70 protein is phosphorylated on tyrosine residues and, together with Src family kinases Lck and Fyn, plays a role in the initial steps of TCR-mediated signal transduction [1]. ZAP70 plays a key role in T cell signal transduction and is vital for thymocyte development. Defects in the ZAP70 protein can lead to severe combined immunodeficiency (SCID), characterized by the selective absence of CD8-positive T cells. Moreover, the expression of ZAP70 in B cells is associated with developing chronic lymphocytic leukemia (CLL) [1-2].
SKG mice are a BALB/c background strain carrying the W163C mutation in the Zap70 gene. This mutation alters the binding of the ZAP70 protein to the CD3ζ chain based on the immunoreceptor tyrosine-based activation motif (ITAM), thereby reducing TCR signal transduction and allowing autoreactive T cells to escape negative selection in the thymus and migrate to the periphery [3]. Under natural conditions or upon administration of serum complement activators, mice develop chronic autoimmune arthritis mediated by Th17 cells [4-5]. Furthermore, studies have shown that stimulation through various methods such as β-glucan or mannan can induce the disease process of rheumatoid arthritis (RA) in SKG mice, resulting in symptoms of autoimmune diseases such as ankylosing spondylitis (AS), psoriasis-like skin inflammation, RA-associated interstitial lung disease (RA-ILD), and Crohn’s disease-like ileitis [6-9].
The BALB/c-Zap70*W163C (SKG) mouse (referred to as the SKG mouse) is an autoimmune disease research model constructed by Cyagen through gene editing technology to introduce the W163C mutation into the Zap70 gene of BALB/c mice. The phenotype of this model is similar to that of the classic SKG mouse [10]. Under SPF conditions, upon triggering innate immune activation (such as β-glucan induction), it can present a variety of autoimmune disease phenotypes. Therefore, this mouse can be used for research on autoimmune diseases such as rheumatoid arthritis (RA), ankylosing spondylitis (AS), psoriasis-like skin inflammation, RA-associated interstitial lung disease (RA-ILD), and Crohn’s disease-like ileitis, as well as T cell signal transduction.
B6-hLPA(CKI)/Alb-cre/hPCSK9
Product ID:
I002079
Strain:
C57BL/6NCya
Status:
Description:
Lipoprotein A (LPA) is a type of particle similar to low-density lipoprotein (LDL) that is considered one of the risk factors for cardiovascular disease (CVD), such as atherosclerosis, coronary heart disease, stroke, etc [1]. LP(a) is similar in size and lipid content to LDL (low-density lipoprotein) and also contains the lipoprotein ApoB-100. However, unlike LDL, LP(a) additionally contains a variable-length lipoprotein called Apo(a), which covalently binds to ApoB-100 through a single disulfide bond. LP(a) plays an important role in systemic lipid transport, guiding inflammatory cells into blood vessel walls and leading to smooth muscle cell proliferation. Furthermore, it is involved in wound healing and tissue repair, interacting with the components of blood vessel walls and the extracellular matrix [2]. However, LP(a) can also cause arterial narrowing by adhering to the arterial wall, accelerating the formation of blood clots, and thereby triggering a series of pathological changes related to coronary heart disease, cardiovascular disease, atherosclerosis, thrombus formation, and stroke [3].
The plasma concentration of LP(a) is closely related to genetic factors and is primarily regulated by the LPA gene. Therefore, the LPA gene is an important potential target for cardiovascular disease treatment. The LPA gene encodes a serine protease that inhibits the activity of tissue-type plasminogen activator I. Fragments of this protein, generated through protein hydrolysis, can adhere to atherosclerotic lesions in arteries, promoting blood clot formation. The LPA gene is expressed in both humans and non-human primates but is not expressed in mice. Constructing mouse models expressing the human LPA gene is of significant importance for developing lipid-lowering drugs, which can drive the development of novel therapies for cardiovascular diseases. Currently, various novel therapies targeting the transcription rate of the LPA gene are under development, including small interfering RNA (siRNA) and antisense oligonucleotides (ASO) [4].
Proprotein convertase subtilisin/kexin 9 (PCSK9) is a serine protease primarily produced in the liver but expressed in other tissues, including the intestine, heart, and neurons. The N-terminal domain of the PCSK9 protein is responsible for protein localization and stability, while the C-terminal domain is responsible for protein enzymatic activity [5]. The Low-density lipoprotein receptor (LDLR) is a receptor that is responsible for clearing low-density lipoprotein cholesterol (LDL-C) from the blood. PCSK9 cleaves the intracellular domain of LDLR on the cell surface, causing it to detach from the cell membrane and be transported to the lysosome for degradation, promoting LDLR degradation, and increasing plasma LDL-C. Overexpression or gain-of-function mutations of the PCSK9 gene can lead to LDL-C accumulation by reducing LDLR levels. This can cause hypercholesterolemia, which increases the risk of cardiovascular diseases, such as atherosclerosis and coronary heart disease, and neurodegenerative diseases, such as Alzheimer's disease [6]. PCSK9 has emerged as a key target for the development of lipid-lowering drugs. Several PCSK9-targeted antibodies or small nucleic acid drugs have been approved for marketing worldwide, including evolocumab from Amgen, alirocumab from Sanofi and Regeneron, and inclisiran from Novartis. These drugs primarily work by inhibiting PCSK9 activity or preventing PCSK9 protein from binding to LDLR, lowering LDL-C levels in the blood to treat hypercholesterolemia [7-8]. In addition, PCSK9 can promote tumor growth and development by regulating cell proliferation, migration, and invasion. It can also regulate the expression of inflammatory factors that contribute to inflammation. Therefore, targeting the expression of PCSK9 has been investigated in tumor immunotherapy and autoimmune disease therapy [9-10].
The B6-hLPA (CKI)/Alb-cre/hPCSK9 mouse model is generated by crossing B6-hLPA (CKI) mice (Catalog No.: C001521, a mouse strain with conditional expression of the human LPA gene), Alb-Cre mice (liver-specific Cre-expressing mice), and B6-hPCSK9 mice (Catalog No.: C001617). This model harbors two cardiovascular disease risk factors, namely Lp (a) (lipoprotein (a)) and PCSK9, making it suitable for research on hyperlipidemia, stroke, coronary heart disease, and other atherosclerotic cardiovascular diseases (ASCVD).
Lipoprotein A (LPA) is a type of particle similar to low-density lipoprotein (LDL) that is considered one of the risk factors for cardiovascular disease (CVD), such as atherosclerosis, coronary heart disease, stroke, etc [1]. LP(a) is similar in size and lipid content to LDL (low-density lipoprotein) and also contains the lipoprotein ApoB-100. However, unlike LDL, LP(a) additionally contains a variable-length lipoprotein called Apo(a), which covalently binds to ApoB-100 through a single disulfide bond. LP(a) plays an important role in systemic lipid transport, guiding inflammatory cells into blood vessel walls and leading to smooth muscle cell proliferation. Furthermore, it is involved in wound healing and tissue repair, interacting with the components of blood vessel walls and the extracellular matrix [2]. However, LP(a) can also cause arterial narrowing by adhering to the arterial wall, accelerating the formation of blood clots, and thereby triggering a series of pathological changes related to coronary heart disease, cardiovascular disease, atherosclerosis, thrombus formation, and stroke [3].
The plasma concentration of LP(a) is closely related to genetic factors and is primarily regulated by the LPA gene. Therefore, the LPA gene is an important potential target for cardiovascular disease treatment. The LPA gene encodes a serine protease that inhibits the activity of tissue-type plasminogen activator I. Fragments of this protein, generated through protein hydrolysis, can adhere to atherosclerotic lesions in arteries, promoting blood clot formation. The LPA gene is expressed in both humans and non-human primates but is not expressed in mice. Constructing mouse models expressing the human LPA gene is of significant importance for developing lipid-lowering drugs, which can drive the development of novel therapies for cardiovascular diseases. Currently, various novel therapies targeting the transcription rate of the LPA gene are under development, including small interfering RNA (siRNA) and antisense oligonucleotides (ASO) [4].
Proprotein convertase subtilisin/kexin 9 (PCSK9) is a serine protease primarily produced in the liver but expressed in other tissues, including the intestine, heart, and neurons. The N-terminal domain of the PCSK9 protein is responsible for protein localization and stability, while the C-terminal domain is responsible for protein enzymatic activity [5]. The Low-density lipoprotein receptor (LDLR) is a receptor that is responsible for clearing low-density lipoprotein cholesterol (LDL-C) from the blood. PCSK9 cleaves the intracellular domain of LDLR on the cell surface, causing it to detach from the cell membrane and be transported to the lysosome for degradation, promoting LDLR degradation, and increasing plasma LDL-C. Overexpression or gain-of-function mutations of the PCSK9 gene can lead to LDL-C accumulation by reducing LDLR levels. This can cause hypercholesterolemia, which increases the risk of cardiovascular diseases, such as atherosclerosis and coronary heart disease, and neurodegenerative diseases, such as Alzheimer's disease [6]. PCSK9 has emerged as a key target for the development of lipid-lowering drugs. Several PCSK9-targeted antibodies or small nucleic acid drugs have been approved for marketing worldwide, including evolocumab from Amgen, alirocumab from Sanofi and Regeneron, and inclisiran from Novartis. These drugs primarily work by inhibiting PCSK9 activity or preventing PCSK9 protein from binding to LDLR, lowering LDL-C levels in the blood to treat hypercholesterolemia [7-8]. In addition, PCSK9 can promote tumor growth and development by regulating cell proliferation, migration, and invasion. It can also regulate the expression of inflammatory factors that contribute to inflammation. Therefore, targeting the expression of PCSK9 has been investigated in tumor immunotherapy and autoimmune disease therapy [9-10].
The B6-hLPA (CKI)/Alb-cre/hPCSK9 mouse model is generated by crossing B6-hLPA (CKI) mice (Catalog No.: C001521, a mouse strain with conditional expression of the human LPA gene), Alb-Cre mice (liver-specific Cre-expressing mice), and B6-hPCSK9 mice (Catalog No.: C001617). This model harbors two cardiovascular disease risk factors, namely Lp (a) (lipoprotein (a)) and PCSK9, making it suitable for research on hyperlipidemia, stroke, coronary heart disease, and other atherosclerotic cardiovascular diseases (ASCVD).
BALB/c-Il10 KO
Product ID:
C001527
Strain:
BALB/cAnCya
Status:
Description:
Interleukin-10 (IL-10) is a cytokine secreted by activated T cells, monocytes, B cells, and macrophages, among other antigen-presenting cells. It exhibits broad biological activity. In immune regulation and inflammatory responses, IL-10 can reduce the expression of Th1 cytokines, MHC-II antigens, or co-stimulatory molecules. Simultaneously, it enhances B cell survival, proliferation, and antibody production. Both overexpression (as seen in systemic lupus erythematosus and tuberculosis) and deficiency (as observed in inflammatory bowel disease, psoriasis, asthma, and rheumatoid arthritis) of IL-10 have pathological and physiological significance. IL-10 is a critical susceptibility gene for inflammatory bowel disease (IBD), and its functional defects play a central role in the development of ulcerative colitis (UC)-type IBD [1]. The genetic polymorphism of IL-10 may also contribute to the occurrence of UC-type IBD or Crohn’s disease (CD)-type IBD [2]. Therefore, IL-10 gene knockout mice exhibit a phenotype similar to human inflammatory bowel disease (IBD) and are widely used in research related to relevant diseases [3].
During the gene editing process, using different mouse strain backgrounds may lead to differences in disease phenotypes. BALB/c strain and C57BL/6 strain exhibit significant differences in susceptibility to infection, resistance, and immune deficiencies. For specific applications such as evaluating antifungal drug efficacy, cancer treatment, and immunological research, the BALB/c strain has its unique advantages [4-6]. Research has found that IL-10-deficient BALB/c mice are more susceptible to colitis than mice of the C57BL/6 strain. Additionally, the disease phenotype is more severe in IL-10-deficient BALB/c mice, making them a more effective model for simulating the disease progression of human colitis [7].
This model is Il10 gene knockout mice, where the Il10 gene homologous to the human IL10 gene has been knocked out in BALB/cAnCya mice. Homozygous BALB/c-Il10 KO mice are viable and fertile. At 8 to 9 weeks of age, BALB/c-Il10 KO mice spontaneously develop colitis symptoms, characterized by weight loss, reduced survival rates, elevated levels of inflammatory factors, and abnormalities in intestinal inflammation and phenotype. BALB/c-Il10 KO mice can be used for research related to Crohn’s disease (CD), colitis, other inflammatory bowel diseases (IBD), cancer, congenital and adaptive immune disorders, as well as various inflammation or autoimmune conditions. It should be noted that due to individual variability and environmental factors, the disease presentation of this model may vary. The data in this manual are based on internal facility observations and are provided for reference. Actual disease presentation may vary; please use the mice according to your specific experimental conditions for best results.
Interleukin-10 (IL-10) is a cytokine secreted by activated T cells, monocytes, B cells, and macrophages, among other antigen-presenting cells. It exhibits broad biological activity. In immune regulation and inflammatory responses, IL-10 can reduce the expression of Th1 cytokines, MHC-II antigens, or co-stimulatory molecules. Simultaneously, it enhances B cell survival, proliferation, and antibody production. Both overexpression (as seen in systemic lupus erythematosus and tuberculosis) and deficiency (as observed in inflammatory bowel disease, psoriasis, asthma, and rheumatoid arthritis) of IL-10 have pathological and physiological significance. IL-10 is a critical susceptibility gene for inflammatory bowel disease (IBD), and its functional defects play a central role in the development of ulcerative colitis (UC)-type IBD [1]. The genetic polymorphism of IL-10 may also contribute to the occurrence of UC-type IBD or Crohn’s disease (CD)-type IBD [2]. Therefore, IL-10 gene knockout mice exhibit a phenotype similar to human inflammatory bowel disease (IBD) and are widely used in research related to relevant diseases [3].
During the gene editing process, using different mouse strain backgrounds may lead to differences in disease phenotypes. BALB/c strain and C57BL/6 strain exhibit significant differences in susceptibility to infection, resistance, and immune deficiencies. For specific applications such as evaluating antifungal drug efficacy, cancer treatment, and immunological research, the BALB/c strain has its unique advantages [4-6]. Research has found that IL-10-deficient BALB/c mice are more susceptible to colitis than mice of the C57BL/6 strain. Additionally, the disease phenotype is more severe in IL-10-deficient BALB/c mice, making them a more effective model for simulating the disease progression of human colitis [7].
This model is Il10 gene knockout mice, where the Il10 gene homologous to the human IL10 gene has been knocked out in BALB/cAnCya mice. Homozygous BALB/c-Il10 KO mice are viable and fertile. At 8 to 9 weeks of age, BALB/c-Il10 KO mice spontaneously develop colitis symptoms, characterized by weight loss, reduced survival rates, elevated levels of inflammatory factors, and abnormalities in intestinal inflammation and phenotype. BALB/c-Il10 KO mice can be used for research related to Crohn’s disease (CD), colitis, other inflammatory bowel diseases (IBD), cancer, congenital and adaptive immune disorders, as well as various inflammation or autoimmune conditions. It should be noted that due to individual variability and environmental factors, the disease presentation of this model may vary. The data in this manual are based on internal facility observations and are provided for reference. Actual disease presentation may vary; please use the mice according to your specific experimental conditions for best results.
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.
B6-huTNFR2 (huTNFRSF1B)
Product ID:
C001913
Strain:
C57BL/6NCya
Status:
Description:
The TNFR2 gene, officially known as TNFRSF1B (Tumor Necrosis Factor Receptor Superfamily Member 1B), encodes the Tumor Necrosis Factor Receptor 2 protein (also called p75 or CD120b), a member of the TNF-receptor superfamily. Unlike its counterpart TNFR1 (which is widely expressed), TNFR2 exhibits more restricted expression, primarily on specific immune cells like regulatory T cells (Tregs), endothelial cells, and certain neuronal cells and microglia in the central nervous system (CNS), as well as on various cancer cells and mesenchymal stem cells [1]. The TNFR2 protein functions as a receptor for the cytokine TNF-α and generally signals for cell survival, proliferation, and anti-apoptosis by recruiting anti-apoptotic proteins and activating the NF-κB pathway (lacking the death domain found in TNFR1, which typically signals apoptosis) [2]. A soluble form of the receptor, sTNFR2, is also produced via proteolytic processing and can act as a TNF-α binding protein [3]. Dysregulation or polymorphisms of the TNFRSF1B gene and its encoded protein are associated with various diseases, including autoimmune disorders (such as rheumatoid arthritis, systemic lupus erythematosus, and inflammatory bowel disease), several cancers (including breast, cervical, and colon cancer, where it promotes tumor growth and immune escape), and neurodegenerative diseases like Alzheimer's and schizophrenia.
The B6-huTNFR2 (huTNFRSF1B) mouse is a humanized model constructed through gene-editing technology, in which the upstream of exon 2 to p.G258 of the mouse Tnfrsf1b gene was replaced with the upstream of exon 2 to p.D257 of the human TNFRSF1B gene. This model can be used for research on diseases such as autoimmune disorders, several cancers, neurodegenerative diseases like Alzheimer's and schizophrenia, as well as for screening, development, and preclinical evaluation of TNFRSF1B-targeted therapeutics.
The TNFR2 gene, officially known as TNFRSF1B (Tumor Necrosis Factor Receptor Superfamily Member 1B), encodes the Tumor Necrosis Factor Receptor 2 protein (also called p75 or CD120b), a member of the TNF-receptor superfamily. Unlike its counterpart TNFR1 (which is widely expressed), TNFR2 exhibits more restricted expression, primarily on specific immune cells like regulatory T cells (Tregs), endothelial cells, and certain neuronal cells and microglia in the central nervous system (CNS), as well as on various cancer cells and mesenchymal stem cells [1]. The TNFR2 protein functions as a receptor for the cytokine TNF-α and generally signals for cell survival, proliferation, and anti-apoptosis by recruiting anti-apoptotic proteins and activating the NF-κB pathway (lacking the death domain found in TNFR1, which typically signals apoptosis) [2]. A soluble form of the receptor, sTNFR2, is also produced via proteolytic processing and can act as a TNF-α binding protein [3]. Dysregulation or polymorphisms of the TNFRSF1B gene and its encoded protein are associated with various diseases, including autoimmune disorders (such as rheumatoid arthritis, systemic lupus erythematosus, and inflammatory bowel disease), several cancers (including breast, cervical, and colon cancer, where it promotes tumor growth and immune escape), and neurodegenerative diseases like Alzheimer's and schizophrenia.
The B6-huTNFR2 (huTNFRSF1B) mouse is a humanized model constructed through gene-editing technology, in which the upstream of exon 2 to p.G258 of the mouse Tnfrsf1b gene was replaced with the upstream of exon 2 to p.D257 of the human TNFRSF1B gene. This model can be used for research on diseases such as autoimmune disorders, several cancers, neurodegenerative diseases like Alzheimer's and schizophrenia, as well as for screening, development, and preclinical evaluation of TNFRSF1B-targeted therapeutics.
Cfh-KO
Product ID:
C001776
Strain:
C57BL/6JCya
Status:
Description:
The CFH gene encodes complement factor H, a crucial secreted plasma glycoprotein with twenty short consensus repeat (SCR) domains. Its primary function is to regulate the complement system, a vital part of the innate immune response. CFH acts to prevent uncontrolled activation of the complement pathway on healthy host cells and tissues, thereby restricting its destructive action to foreign invaders [1]. Gene expression of CFH is notably high in the liver, where it is synthesized and secreted into the bloodstream. It is also expressed in various other tissues, including ocular tissues like the retina and retinal pigment epithelium (RPE), sclera, and ciliary body, as well as in the kidney, lung, and certain immune cells [2-4]. The protein binds to C3b, accelerating the decay of alternative pathway C3-convertase and acting as a cofactor for Factor I-mediated inactivation of C3b [1-2]. Dysregulation or mutations in the CFH gene are associated with several diseases, including age-related macular degeneration (AMD), a common cause of vision loss characterized by drusen accumulation, atypical hemolytic-uremic syndrome (aHUS), which causes abnormal blood clots and kidney failure, C3 glomerulopathy (C3G), a rare kidney disease, and Membranoproliferative glomerulonephritis (MPGN), particularly type II (also known as Dense Deposit Disease), a group of kidney diseases characterized by inflammation and damage to the kidney's filtering units (glomeruli), often due to complement dysregulation [2-4].
The Cfh-KO mouse is a gene knockout model created using gene-editing techniques to knock out exons 2~3 of the Cfh gene (the homolog of the human CFH gene) in mice. This model can be used for research into the pathogenic mechanisms of diseases such as age-related macular degeneration, atypical hemolytic uremic syndrome, C3 glomerulopathy, and Type II membranoproliferative glomerulonephritis, as well as for the development of related treatment methods.
The CFH gene encodes complement factor H, a crucial secreted plasma glycoprotein with twenty short consensus repeat (SCR) domains. Its primary function is to regulate the complement system, a vital part of the innate immune response. CFH acts to prevent uncontrolled activation of the complement pathway on healthy host cells and tissues, thereby restricting its destructive action to foreign invaders [1]. Gene expression of CFH is notably high in the liver, where it is synthesized and secreted into the bloodstream. It is also expressed in various other tissues, including ocular tissues like the retina and retinal pigment epithelium (RPE), sclera, and ciliary body, as well as in the kidney, lung, and certain immune cells [2-4]. The protein binds to C3b, accelerating the decay of alternative pathway C3-convertase and acting as a cofactor for Factor I-mediated inactivation of C3b [1-2]. Dysregulation or mutations in the CFH gene are associated with several diseases, including age-related macular degeneration (AMD), a common cause of vision loss characterized by drusen accumulation, atypical hemolytic-uremic syndrome (aHUS), which causes abnormal blood clots and kidney failure, C3 glomerulopathy (C3G), a rare kidney disease, and Membranoproliferative glomerulonephritis (MPGN), particularly type II (also known as Dense Deposit Disease), a group of kidney diseases characterized by inflammation and damage to the kidney's filtering units (glomeruli), often due to complement dysregulation [2-4].
The Cfh-KO mouse is a gene knockout model created using gene-editing techniques to knock out exons 2~3 of the Cfh gene (the homolog of the human CFH gene) in mice. This model can be used for research into the pathogenic mechanisms of diseases such as age-related macular degeneration, atypical hemolytic uremic syndrome, C3 glomerulopathy, and Type II membranoproliferative glomerulonephritis, as well as for the development of related treatment methods.
Cd11b-hCD89(FCAR)
Product ID:
C001793
Strain:
C57BL/6NCya
Status:
Description:
CD89, also known as Fcα receptor (FCAR), is a receptor on the surface of various immune cells and belongs to the Fc receptor family. Fc receptors bind antibodies, linking the immune system’s recognition of pathogens with cellular immune responses. CD89 is primarily expressed on monocytes/macrophages, neutrophils, eosinophils, dendritic cells, and Kupffer cells in the liver, unlike other Fc receptors expressed on lymphocytes [1]. The function of CD89 primarily involves binding with IgA antibodies (especially IgA1 and IgA2), initiating various immune responses. CD89 can trigger phagocytosis (engulfing and destroying pathogens), antibody-dependent cellular cytotoxicity (ADCC) (killing infected or cancerous cells), and release inflammatory mediators (promoting inflammatory responses and recruiting immune cells) [2]. IgA nephropathy (IgAN) is a disease closely associated with CD89 and is the most common form of glomerulonephritis, characterized by the deposition of IgA (particularly IgA1) in the glomeruli. As the myeloid cell-specific Fc receptor for IgA, CD89 specifically binds IgA1, a highly glycosylated IgA subtype predominantly found in serum and responsible for neutralizing pathogens at mucosal surfaces [3-4]. In IgA nephropathy, one pathological mechanism is the formation of immune complexes between aberrantly glycosylated IgA1 and CD89. These complexes deposit in the glomerular mesangium, activate mesangial cells, and trigger inflammation, fibrosis, and kidney structural damage. Without treatment, the condition can progress to chronic kidney disease (CKD) and even end-stage renal disease (ESRD) [5-7].
Since mice lack a homologous gene to human CD89, introducing the human CD89 gene into mice aids in studying immune mechanisms and IgA nephropathy (IgAN). The Cd11b-hCD89(FCAR) mice are a humanized model constructed by integrating the coding sequence (CDS) of the human CD89 gene downstream of the TAA stop codon of the mouse Cd11b (Itgam) gene. The human CD89 gene is specifically expressed in myeloid cells under the regulation of the mouse Cd11b gene promoter. Cd11b-hCD89(FCAR) mice can be used in studies on immune responses, autoimmune mechanisms, as well as tumor and infectious diseases. They can also be crossed with the IgA1 humanized mouse model (Product No.: C001565) to construct an IgA nephropathy (IgAN) mouse model that better recapitulates human genetic mechanisms and pathological phenotypes [8], for researching IgAN mechanisms and developing therapies.
CD89, also known as Fcα receptor (FCAR), is a receptor on the surface of various immune cells and belongs to the Fc receptor family. Fc receptors bind antibodies, linking the immune system’s recognition of pathogens with cellular immune responses. CD89 is primarily expressed on monocytes/macrophages, neutrophils, eosinophils, dendritic cells, and Kupffer cells in the liver, unlike other Fc receptors expressed on lymphocytes [1]. The function of CD89 primarily involves binding with IgA antibodies (especially IgA1 and IgA2), initiating various immune responses. CD89 can trigger phagocytosis (engulfing and destroying pathogens), antibody-dependent cellular cytotoxicity (ADCC) (killing infected or cancerous cells), and release inflammatory mediators (promoting inflammatory responses and recruiting immune cells) [2]. IgA nephropathy (IgAN) is a disease closely associated with CD89 and is the most common form of glomerulonephritis, characterized by the deposition of IgA (particularly IgA1) in the glomeruli. As the myeloid cell-specific Fc receptor for IgA, CD89 specifically binds IgA1, a highly glycosylated IgA subtype predominantly found in serum and responsible for neutralizing pathogens at mucosal surfaces [3-4]. In IgA nephropathy, one pathological mechanism is the formation of immune complexes between aberrantly glycosylated IgA1 and CD89. These complexes deposit in the glomerular mesangium, activate mesangial cells, and trigger inflammation, fibrosis, and kidney structural damage. Without treatment, the condition can progress to chronic kidney disease (CKD) and even end-stage renal disease (ESRD) [5-7].
Since mice lack a homologous gene to human CD89, introducing the human CD89 gene into mice aids in studying immune mechanisms and IgA nephropathy (IgAN). The Cd11b-hCD89(FCAR) mice are a humanized model constructed by integrating the coding sequence (CDS) of the human CD89 gene downstream of the TAA stop codon of the mouse Cd11b (Itgam) gene. The human CD89 gene is specifically expressed in myeloid cells under the regulation of the mouse Cd11b gene promoter. Cd11b-hCD89(FCAR) mice can be used in studies on immune responses, autoimmune mechanisms, as well as tumor and infectious diseases. They can also be crossed with the IgA1 humanized mouse model (Product No.: C001565) to construct an IgA nephropathy (IgAN) mouse model that better recapitulates human genetic mechanisms and pathological phenotypes [8], for researching IgAN mechanisms and developing therapies.
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