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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).
B6-hPCSK9/Apoe KO
Product ID:
I001220
Strain:
C57BL/6Cya
Status:
Description:
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 [1]. 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 [2]. PCSK9 has become an important 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 [3-4]. 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 [5-6].
Apolipoprotein E (ApoE) is a lipid particle-associated polymorphic carrier protein encoded by the APOE gene. It is a core component of plasma lipoproteins, participating in the production, transport, and clearance of lipoproteins. ApoE is associated with chylomicrons, chylomicron remnants, high-density lipoprotein (HDL), very low-density lipoprotein (VLDL), and intermediate-density lipoprotein (IDL), especially showing preferential binding to HDL [7]. ApoE is the most important lipid transport protein in the body, having a profound impact on lipid metabolism. The interaction of ApoE with the low-density lipoprotein receptor (LDLR) is essential for the normal processing (catabolism) of triglyceride-rich lipoproteins [8]. In peripheral tissues, ApoE is primarily produced by the liver and macrophages and mediates cholesterol metabolism. In the central nervous system, ApoE is produced mainly by astrocytes and is the major cholesterol carrier in the brain. ApoE is essential for transporting cholesterol from astrocytes to neurons [7-10]. In addition, ApoE forms a complex with activated C1q, becoming a checkpoint inhibitor target of the classical complement pathway [11]. Polymorphisms of the APOE are associated with Alzheimer's disease and lipid accumulation, hyperlipidemia, atherosclerosis, high cholesterolemia, etc., and are related to the risk of various cardiovascular diseases.
The B6-hPCSK9/Apoe KO mice are obtained by crossing B6-hPCSK9 mice (Catalog No.: I001179) with B6J-Apoe KO mice (Catalog No.: C001507). B6J-Apoe KO mice exhibit elevated cholesterol levels and spontaneous atherosclerosis phenotypes due to the disruption of ApoE protein synthesis, further exacerbated under a high-fat diet (HFD). On the other hand, B6-hPCSK9 mice have the mouse Pcsk9 gene sequence replaced with the human PCSK9 gene sequence through gene editing technology, expressing the human PCSK9 protein. They can be used for the development of PCSK9-targeted drugs in hyperlipidemia, stroke, coronary heart disease, and other atherosclerotic cardiovascular diseases (ASCVD). The B6-hPCSK9/Apoe KO mice, while expressing the human PCSK9 protein, exhibit significantly elevated cholesterol levels and spontaneous atherosclerosis characteristics. These mice provide an ideal platform for the PCSK9-targeted drug development in hyperlipidemia and cardiovascular diseases, demonstrating good clinical and pathological relevance.
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 [1]. 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 [2]. PCSK9 has become an important 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 [3-4]. 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 [5-6].
Apolipoprotein E (ApoE) is a lipid particle-associated polymorphic carrier protein encoded by the APOE gene. It is a core component of plasma lipoproteins, participating in the production, transport, and clearance of lipoproteins. ApoE is associated with chylomicrons, chylomicron remnants, high-density lipoprotein (HDL), very low-density lipoprotein (VLDL), and intermediate-density lipoprotein (IDL), especially showing preferential binding to HDL [7]. ApoE is the most important lipid transport protein in the body, having a profound impact on lipid metabolism. The interaction of ApoE with the low-density lipoprotein receptor (LDLR) is essential for the normal processing (catabolism) of triglyceride-rich lipoproteins [8]. In peripheral tissues, ApoE is primarily produced by the liver and macrophages and mediates cholesterol metabolism. In the central nervous system, ApoE is produced mainly by astrocytes and is the major cholesterol carrier in the brain. ApoE is essential for transporting cholesterol from astrocytes to neurons [7-10]. In addition, ApoE forms a complex with activated C1q, becoming a checkpoint inhibitor target of the classical complement pathway [11]. Polymorphisms of the APOE are associated with Alzheimer's disease and lipid accumulation, hyperlipidemia, atherosclerosis, high cholesterolemia, etc., and are related to the risk of various cardiovascular diseases.
The B6-hPCSK9/Apoe KO mice are obtained by crossing B6-hPCSK9 mice (Catalog No.: I001179) with B6J-Apoe KO mice (Catalog No.: C001507). B6J-Apoe KO mice exhibit elevated cholesterol levels and spontaneous atherosclerosis phenotypes due to the disruption of ApoE protein synthesis, further exacerbated under a high-fat diet (HFD). On the other hand, B6-hPCSK9 mice have the mouse Pcsk9 gene sequence replaced with the human PCSK9 gene sequence through gene editing technology, expressing the human PCSK9 protein. They can be used for the development of PCSK9-targeted drugs in hyperlipidemia, stroke, coronary heart disease, and other atherosclerotic cardiovascular diseases (ASCVD). The B6-hPCSK9/Apoe KO mice, while expressing the human PCSK9 protein, exhibit significantly elevated cholesterol levels and spontaneous atherosclerosis characteristics. These mice provide an ideal platform for the PCSK9-targeted drug development in hyperlipidemia and cardiovascular diseases, demonstrating good clinical and pathological relevance.
B6-hTL1A/hIL23A
Product ID:
C001837
Strain:
C57BL/6N;6JCya
Status:
Description:
TNF-like ligand 1A (TL1A), also known as TNF superfamily member 15 (TNFSF15), is a member of the tumor necrosis factor (TNF) family encoded by the TNFSF15 gene in humans. TL1A acts as a ligand for death receptor 3 (DR3) and decoy receptor 3 (DcR3), providing a stimulatory signal for downstream pathways. It regulates the proliferation, activation, and apoptosis of effector cells, as well as cytokine and chemokine production. TL1A is expressed in various immune cells, including monocytes, macrophages, dendritic cells, and T cells, as well as in non-immune cells such as synovial fibroblasts and endothelial cells. It plays a crucial role in modulating immune responses by promoting the differentiation and survival of T cells, particularly Th17 cells involved in inflammatory processes [1]. TL1A enhances IL-2 responses in anti-CD3/CD28-stimulated T cells and synergizes with IL-12 and IL-18 to augment IFN-γ release in human T and NK cells, biasing T cell differentiation toward a Th1 phenotype [2]. Dysregulation of TL1A expression is implicated in autoimmune diseases, including inflammatory bowel disease (IBD), rheumatoid arthritis (RA), primary biliary cholangitis (PBC), systemic lupus erythematosus (SLE), and ankylosing spondylitis (AS) [1]. TL1A has emerged as a promising therapeutic target, with ongoing research focused on developing monoclonal antibodies and other biologics to neutralize TL1A and reduce inflammation in autoimmune disorders. Clinical trial results suggest that TL1A inhibition can be used in the treatment of various autoimmune diseases, particularly IBD [3-5].
The IL23A gene encodes the p19 subunit, a component of interleukin-23 (IL-23), which forms a heterodimer with the p40 subunit (encoded by IL12B) to generate the functional IL-23 cytokine [1]. Primarily expressed by activated dendritic cells, macrophages, and monocytes, IL-23 signals through the IL-23 receptor (IL-23R) complex, activating the JAK-STAT pathway to promote Th17 cell differentiation and maintain IL-17 production. This process drives inflammatory responses and mucosal immunity against extracellular pathogens [6-7]. Genetic polymorphisms within IL23A are strongly associated with autoimmune and inflammatory diseases, including psoriasis, Crohn's disease, and inflammatory bowel disease, due to dysregulated Th17 activity and chronic inflammation [6-7]. Monoclonal antibodies targeting IL-23, such as risankizumab and guselkumab, selectively block the p19 subunit, demonstrating therapeutic efficacy in psoriasis and inflammatory bowel diseases by suppressing pathogenic IL-17/Th17 pathways [8]. While IL-23 plays a role in protective immunity, its overactivation contributes to tissue damage in autoimmune settings, highlighting its dual function in immune regulation and disease pathogenesis [6-9].
B6-hTL1A/hIL23A mice are humanized models generated by crossing B6-hTL1A (TNFSF15) mice (Catalog No.: C001603) with B6-hIL23A mice (Catalog No.: C001618). These mice are suitable for studying the pathological mechanisms and therapeutic strategies of allergic and inflammatory diseases, immune-related disorders, and cancer, as well as for the screening, development, and preclinical evaluation of TL1A/IL23A-targeted drugs.
TNF-like ligand 1A (TL1A), also known as TNF superfamily member 15 (TNFSF15), is a member of the tumor necrosis factor (TNF) family encoded by the TNFSF15 gene in humans. TL1A acts as a ligand for death receptor 3 (DR3) and decoy receptor 3 (DcR3), providing a stimulatory signal for downstream pathways. It regulates the proliferation, activation, and apoptosis of effector cells, as well as cytokine and chemokine production. TL1A is expressed in various immune cells, including monocytes, macrophages, dendritic cells, and T cells, as well as in non-immune cells such as synovial fibroblasts and endothelial cells. It plays a crucial role in modulating immune responses by promoting the differentiation and survival of T cells, particularly Th17 cells involved in inflammatory processes [1]. TL1A enhances IL-2 responses in anti-CD3/CD28-stimulated T cells and synergizes with IL-12 and IL-18 to augment IFN-γ release in human T and NK cells, biasing T cell differentiation toward a Th1 phenotype [2]. Dysregulation of TL1A expression is implicated in autoimmune diseases, including inflammatory bowel disease (IBD), rheumatoid arthritis (RA), primary biliary cholangitis (PBC), systemic lupus erythematosus (SLE), and ankylosing spondylitis (AS) [1]. TL1A has emerged as a promising therapeutic target, with ongoing research focused on developing monoclonal antibodies and other biologics to neutralize TL1A and reduce inflammation in autoimmune disorders. Clinical trial results suggest that TL1A inhibition can be used in the treatment of various autoimmune diseases, particularly IBD [3-5].
The IL23A gene encodes the p19 subunit, a component of interleukin-23 (IL-23), which forms a heterodimer with the p40 subunit (encoded by IL12B) to generate the functional IL-23 cytokine [1]. Primarily expressed by activated dendritic cells, macrophages, and monocytes, IL-23 signals through the IL-23 receptor (IL-23R) complex, activating the JAK-STAT pathway to promote Th17 cell differentiation and maintain IL-17 production. This process drives inflammatory responses and mucosal immunity against extracellular pathogens [6-7]. Genetic polymorphisms within IL23A are strongly associated with autoimmune and inflammatory diseases, including psoriasis, Crohn's disease, and inflammatory bowel disease, due to dysregulated Th17 activity and chronic inflammation [6-7]. Monoclonal antibodies targeting IL-23, such as risankizumab and guselkumab, selectively block the p19 subunit, demonstrating therapeutic efficacy in psoriasis and inflammatory bowel diseases by suppressing pathogenic IL-17/Th17 pathways [8]. While IL-23 plays a role in protective immunity, its overactivation contributes to tissue damage in autoimmune settings, highlighting its dual function in immune regulation and disease pathogenesis [6-9].
B6-hTL1A/hIL23A mice are humanized models generated by crossing B6-hTL1A (TNFSF15) mice (Catalog No.: C001603) with B6-hIL23A mice (Catalog No.: C001618). These mice are suitable for studying the pathological mechanisms and therapeutic strategies of allergic and inflammatory diseases, immune-related disorders, and cancer, as well as for the screening, development, and preclinical evaluation of TL1A/IL23A-targeted drugs.
B6-hα4β7/hTL1A
Product ID:
C001795
Strain:
C57BL/6Cya
Status:
Description:
The ITGA4 gene encodes the integrin α4 subunit, which pairs with the integrin β7 subunit, encoded by the ITGB7 gene, to form the heterodimeric transmembrane protein α4β7, a key member of the integrin protein family [1]. α4β7 is prominently expressed in immune tissues, including lymph nodes, bone marrow, spleen, and blood, as well as in diverse immune cell populations, such as T lymphocytes, B lymphocytes, monocytes, granulocytes, and natural killer cells [1]. Functionally, α4β7 mediates cell adhesion and migration, critically regulating immune cell trafficking and inflammatory processes. Specifically, α4β7 facilitates lymphocyte migration to sites of inflammation and intestinal lymphoid tissues through interactions with vascular cell adhesion molecule-1 (VCAM-1) and mucosal addressin cell adhesion molecule-1 (MAdCAM-1) [2]. Notably, ITGA4 and ITGB7 have been implicated in the pathogenesis of autoimmune diseases, including inflammatory bowel disease (IBD), Crohn's disease, ulcerative colitis, and multiple sclerosis [2-4]. Consequently, the targeting of α4β7 has emerged as a key therapeutic strategy for inflammatory and autoimmune disorders.
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 [5]. 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 [6]. 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) [5]. 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 [7-9].
B6-hα4β7/hTL1A mouse is a triple-gene humanized model for ITGA4, ITGB7, and TNFSF15, generated by crossing B6-hα4β7 mice with B6-hTL1A (TNFSF15) mice (Catalog No.: C001603). This model serves as a valuable tool for researching immune-related diseases, applicable to studies on T cell differentiation and survival, immune response regulation, and autoimmune diseases. It provides a robust preclinical research platform for the screening, development, and safety evaluation of α4β7/TL1A-targeted drugs.
The ITGA4 gene encodes the integrin α4 subunit, which pairs with the integrin β7 subunit, encoded by the ITGB7 gene, to form the heterodimeric transmembrane protein α4β7, a key member of the integrin protein family [1]. α4β7 is prominently expressed in immune tissues, including lymph nodes, bone marrow, spleen, and blood, as well as in diverse immune cell populations, such as T lymphocytes, B lymphocytes, monocytes, granulocytes, and natural killer cells [1]. Functionally, α4β7 mediates cell adhesion and migration, critically regulating immune cell trafficking and inflammatory processes. Specifically, α4β7 facilitates lymphocyte migration to sites of inflammation and intestinal lymphoid tissues through interactions with vascular cell adhesion molecule-1 (VCAM-1) and mucosal addressin cell adhesion molecule-1 (MAdCAM-1) [2]. Notably, ITGA4 and ITGB7 have been implicated in the pathogenesis of autoimmune diseases, including inflammatory bowel disease (IBD), Crohn's disease, ulcerative colitis, and multiple sclerosis [2-4]. Consequently, the targeting of α4β7 has emerged as a key therapeutic strategy for inflammatory and autoimmune disorders.
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 [5]. 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 [6]. 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) [5]. 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 [7-9].
B6-hα4β7/hTL1A mouse is a triple-gene humanized model for ITGA4, ITGB7, and TNFSF15, generated by crossing B6-hα4β7 mice with B6-hTL1A (TNFSF15) mice (Catalog No.: C001603). This model serves as a valuable tool for researching immune-related diseases, applicable to studies on T cell differentiation and survival, immune response regulation, and autoimmune diseases. It provides a robust preclinical research platform for the screening, development, and safety evaluation of α4β7/TL1A-targeted drugs.
B6-hIL6ST
Product ID:
C001786
Strain:
C57BL/6NCya
Status:
Description:
The IL6ST gene, also known as gp130, encodes a crucial signal-transducing protein that is part of the receptor complex for a wide range of cytokines, including Interleukin-6 (IL-6), leukemia inhibitory factor (LIF), ciliary neurotrophic factor (CNTF), and oncostatin M (OSM) [1]. This protein is ubiquitously expressed across various cellular tissues, including but not limited to the brain, heart, thymus, spleen, kidney, lung, liver, and endometrial tissues, playing critical roles in mediating signals that regulate immune response, hematopoiesis, pain control, bone metabolism, and embryonic development. Its function involves homodimerization upon cytokine binding to initiate intracellular signaling pathways like JAK-MAPK and JAK-STAT3, thereby influencing cell proliferation, differentiation, and survival [2]. Dysregulation or mutations in IL6ST are associated with several diseases, notably various forms of Hyper-IgE Syndrome (HIES), particularly Hyper-IgE recurrent infection syndrome type 4 (autosomal recessive and dominant forms), as well as playing a role in conditions like rheumatoid arthritis, multiple sclerosis, Crohn's disease, inflammatory bowel disease, breast cancer, and endometriosis [3-4].
The B6-hIL6ST mouse is a humanized model constructed by replacing the endogenous partial extracellular domain of the mouse Il6st gene with the human IL6ST partial extracellular domain. The murine signal peptide, transmembrane, and cytoplasmic domains are preserved. B6-hIL6ST mice can be used for research into the pathogenesis of inflammatory and autoimmune diseases, as well as certain tumors, and for the screening, development, and safety evaluation of IL6ST-targeted drugs.
The IL6ST gene, also known as gp130, encodes a crucial signal-transducing protein that is part of the receptor complex for a wide range of cytokines, including Interleukin-6 (IL-6), leukemia inhibitory factor (LIF), ciliary neurotrophic factor (CNTF), and oncostatin M (OSM) [1]. This protein is ubiquitously expressed across various cellular tissues, including but not limited to the brain, heart, thymus, spleen, kidney, lung, liver, and endometrial tissues, playing critical roles in mediating signals that regulate immune response, hematopoiesis, pain control, bone metabolism, and embryonic development. Its function involves homodimerization upon cytokine binding to initiate intracellular signaling pathways like JAK-MAPK and JAK-STAT3, thereby influencing cell proliferation, differentiation, and survival [2]. Dysregulation or mutations in IL6ST are associated with several diseases, notably various forms of Hyper-IgE Syndrome (HIES), particularly Hyper-IgE recurrent infection syndrome type 4 (autosomal recessive and dominant forms), as well as playing a role in conditions like rheumatoid arthritis, multiple sclerosis, Crohn's disease, inflammatory bowel disease, breast cancer, and endometriosis [3-4].
The B6-hIL6ST mouse is a humanized model constructed by replacing the endogenous partial extracellular domain of the mouse Il6st gene with the human IL6ST partial extracellular domain. The murine signal peptide, transmembrane, and cytoplasmic domains are preserved. B6-hIL6ST mice can be used for research into the pathogenesis of inflammatory and autoimmune diseases, as well as certain tumors, and for the screening, development, and safety evaluation of IL6ST-targeted drugs.
B6-hOX40L (hTNFSF4)
Product ID:
C001719
Strain:
C57BL/6NCya
Status:
Description:
The TNFSF4 gene (tumor necrosis factor superfamily member 4, also known as OX40L) encodes the OX40 ligand protein, a type II transmembrane protein mainly expressed on antigen-presenting cells (APCs, such as dendritic cells, B cells, and macrophages), as well as endothelial cells and smooth muscle cells [1]. This protein binds to the receptor OX40 (TNFRSF4) on the surface of T cells, providing crucial co-stimulatory signals that enhance T-cell proliferation, survival, and cytokine secretion, thereby playing a central role in adaptive immunity and inflammatory responses [2]. Dysregulated expression of TNFSF4 is associated with various autoimmune diseases, such as systemic lupus erythematosus (SLE) and rheumatoid arthritis (RA), and its gene polymorphisms have been proven to be related to disease susceptibility [3]. Altering the OX40-OX40L interaction can either enhance the immune response to fight cancer or suppress it to treat autoimmune diseases [4]. Blocking the OX40-OX40L binding may alleviate autoimmune diseases by reducing the levels of pro-inflammatory cytokines and enhancing the function of regulatory T cells. Due to its crucial role in immune regulation, OX40L is regarded as an important target for treating autoimmune diseases and cancer immunotherapy, and current drug development focuses on monoclonal antibodies and OX40L inhibitors.
B6-hOX40L (hTNFSF4) mice are a humanized model constructed by using gene editing technology to replace the endogenous extracellular domain of the mouse Tnfsf4 gene with the extracellular domain of the human TNFSF4 gene. This model can be used for research on autoimmune diseases (such as systemic lupus erythematosus and rheumatoid arthritis), cancer immunology, and TNFSF4-targeted drug development.
The TNFSF4 gene (tumor necrosis factor superfamily member 4, also known as OX40L) encodes the OX40 ligand protein, a type II transmembrane protein mainly expressed on antigen-presenting cells (APCs, such as dendritic cells, B cells, and macrophages), as well as endothelial cells and smooth muscle cells [1]. This protein binds to the receptor OX40 (TNFRSF4) on the surface of T cells, providing crucial co-stimulatory signals that enhance T-cell proliferation, survival, and cytokine secretion, thereby playing a central role in adaptive immunity and inflammatory responses [2]. Dysregulated expression of TNFSF4 is associated with various autoimmune diseases, such as systemic lupus erythematosus (SLE) and rheumatoid arthritis (RA), and its gene polymorphisms have been proven to be related to disease susceptibility [3]. Altering the OX40-OX40L interaction can either enhance the immune response to fight cancer or suppress it to treat autoimmune diseases [4]. Blocking the OX40-OX40L binding may alleviate autoimmune diseases by reducing the levels of pro-inflammatory cytokines and enhancing the function of regulatory T cells. Due to its crucial role in immune regulation, OX40L is regarded as an important target for treating autoimmune diseases and cancer immunotherapy, and current drug development focuses on monoclonal antibodies and OX40L inhibitors.
B6-hOX40L (hTNFSF4) mice are a humanized model constructed by using gene editing technology to replace the endogenous extracellular domain of the mouse Tnfsf4 gene with the extracellular domain of the human TNFSF4 gene. This model can be used for research on autoimmune diseases (such as systemic lupus erythematosus and rheumatoid arthritis), cancer immunology, and TNFSF4-targeted drug development.
B6-hIL2RA
Product ID:
C001713
Strain:
C57BL/6NCya
Status:
Description:
The interleukin-2 receptor alpha subunit, encoded by the IL2RA gene and also known as CD25, is a critical determinant of IL-2 signaling, a pathway fundamental to T cell biology. While CD25 alone exhibits low affinity for IL-2, its assembly with the IL-2 receptor beta and gamma chains forms the high-affinity receptor complex essential for robust cellular responses to this pleiotropic cytokine [1]. Expressed prominently on activated T lymphocytes, including effector and regulatory T cells, CD25 is pivotal for diverse processes such as T cell proliferation, differentiation, and the maintenance of immune tolerance, largely mediated through its indispensable role in regulatory T cell development and function [2]. Consequently, perturbations in IL2RA expression or genetic variants within the locus are strongly associated with susceptibility to a range of severe autoimmune disorders, including multiple sclerosis, type 1 diabetes, and rheumatoid arthritis, highlighting its central involvement in immune homeostasis breakdown [3]. Furthermore, aberrant CD25 expression has been observed in certain malignancies, suggesting roles beyond adaptive immunity [4]. The demonstrable impact of IL2RA on immune regulation and disease pathogenesis underscores its significance as a key molecule in immunology and a compelling target for therapeutic intervention.
The B6-hIL2RA mouse is a humanized model constructed by replacing the sequence of the mouse Il2ra endogenous extracellular domain in situ with the corresponding extracellular domain from the human IL2RA. The murine signal peptide and transmembrane-cytoplasmic region were preserved. The B6-hIL2RA mice can be used for the study of the pathogenesis of autoimmune diseases such as multiple sclerosis, type 1 diabetes, and rheumatoid arthritis, and certain malignancies, as well as for IL2RA-targeted drug development.
The interleukin-2 receptor alpha subunit, encoded by the IL2RA gene and also known as CD25, is a critical determinant of IL-2 signaling, a pathway fundamental to T cell biology. While CD25 alone exhibits low affinity for IL-2, its assembly with the IL-2 receptor beta and gamma chains forms the high-affinity receptor complex essential for robust cellular responses to this pleiotropic cytokine [1]. Expressed prominently on activated T lymphocytes, including effector and regulatory T cells, CD25 is pivotal for diverse processes such as T cell proliferation, differentiation, and the maintenance of immune tolerance, largely mediated through its indispensable role in regulatory T cell development and function [2]. Consequently, perturbations in IL2RA expression or genetic variants within the locus are strongly associated with susceptibility to a range of severe autoimmune disorders, including multiple sclerosis, type 1 diabetes, and rheumatoid arthritis, highlighting its central involvement in immune homeostasis breakdown [3]. Furthermore, aberrant CD25 expression has been observed in certain malignancies, suggesting roles beyond adaptive immunity [4]. The demonstrable impact of IL2RA on immune regulation and disease pathogenesis underscores its significance as a key molecule in immunology and a compelling target for therapeutic intervention.
The B6-hIL2RA mouse is a humanized model constructed by replacing the sequence of the mouse Il2ra endogenous extracellular domain in situ with the corresponding extracellular domain from the human IL2RA. The murine signal peptide and transmembrane-cytoplasmic region were preserved. The B6-hIL2RA mice can be used for the study of the pathogenesis of autoimmune diseases such as multiple sclerosis, type 1 diabetes, and rheumatoid arthritis, and certain malignancies, as well as for IL2RA-targeted drug development.
B6-hBAFFR (hTNFRSF13C)
Product ID:
C001711
Strain:
C57BL/6NCya
Status:
Description:
The gene TNFRSF13C encodes the B cell-activating factor receptor (BAFF-R), also known as BLyS receptor 3 (BR3) or CD268. As a member of the tumor necrosis factor receptor superfamily (TNFRSF), BAFF-R functions as a crucial type III transmembrane signaling protein on lymphocytes. Its expression is predominantly observed on the surface of B cells throughout various stages of their development, from transitional to mature naive and memory populations, underscoring its vital role in peripheral B cell homeostasis [1]. BAFF-R serves as the primary receptor for the cytokine BAFF (TNFSF13B), and their interaction delivers essential survival and maturation signals to B cells, mediated through downstream pathways including the activation of NF-κB and PI3K. Genetic alterations in TNFRSF13C, including point mutations and deletions, or dysregulation of the BAFF-BAFF-R axis, are increasingly recognized for their contribution to immune pathology [2]. Such aberrations are associated with primary immunodeficiencies like common variable immunodeficiency (CVID), characterized by profound defects in antibody production and recurrent infections, as well as a range of autoimmune diseases such as systemic lupus erythematosus (SLE) and Sjögren's syndrome, and certain B cell malignancies [2-3]. The critical, non-redundant function of BAFF-R in B cell biology highlights its significance as a key node in adaptive immunity and positions the BAFF-BAFF-R pathway as a compelling target for therapeutic intervention in a spectrum of immune-mediated disorders.
The B6-hBAFFR (hTNFRSF13C) mouse is a humanized model constructed by replacing the sequence of the mouse Tnfrsf13c endogenous extracellular domain in situ with the corresponding extracellular domain from the human TNFRSF13C. The B6-hBAFFR (hTNFRSF13C) mice can be used for the study of the pathogenesis of immune-mediated disorders such as common variable immunodeficiency (CVID), systemic lupus erythematosus (SLE), and Sjögren's syndrome, and certain B cell malignancies, as well as for TNFRSF13C-targeted drug development.
The gene TNFRSF13C encodes the B cell-activating factor receptor (BAFF-R), also known as BLyS receptor 3 (BR3) or CD268. As a member of the tumor necrosis factor receptor superfamily (TNFRSF), BAFF-R functions as a crucial type III transmembrane signaling protein on lymphocytes. Its expression is predominantly observed on the surface of B cells throughout various stages of their development, from transitional to mature naive and memory populations, underscoring its vital role in peripheral B cell homeostasis [1]. BAFF-R serves as the primary receptor for the cytokine BAFF (TNFSF13B), and their interaction delivers essential survival and maturation signals to B cells, mediated through downstream pathways including the activation of NF-κB and PI3K. Genetic alterations in TNFRSF13C, including point mutations and deletions, or dysregulation of the BAFF-BAFF-R axis, are increasingly recognized for their contribution to immune pathology [2]. Such aberrations are associated with primary immunodeficiencies like common variable immunodeficiency (CVID), characterized by profound defects in antibody production and recurrent infections, as well as a range of autoimmune diseases such as systemic lupus erythematosus (SLE) and Sjögren's syndrome, and certain B cell malignancies [2-3]. The critical, non-redundant function of BAFF-R in B cell biology highlights its significance as a key node in adaptive immunity and positions the BAFF-BAFF-R pathway as a compelling target for therapeutic intervention in a spectrum of immune-mediated disorders.
The B6-hBAFFR (hTNFRSF13C) mouse is a humanized model constructed by replacing the sequence of the mouse Tnfrsf13c endogenous extracellular domain in situ with the corresponding extracellular domain from the human TNFRSF13C. The B6-hBAFFR (hTNFRSF13C) mice can be used for the study of the pathogenesis of immune-mediated disorders such as common variable immunodeficiency (CVID), systemic lupus erythematosus (SLE), and Sjögren's syndrome, and certain B cell malignancies, as well as for TNFRSF13C-targeted drug development.
B6-hIL7R
Product ID:
C001633
Strain:
C57BL/6NCya
Status:
Description:
The IL7R gene encodes the interleukin-7 receptor α chain (IL-7Rα), also known as CD127, a member of the type I cytokine receptor family. Expressed on T, B, NK, monocytes, and dendritic cells, IL7R gene expression is tightly regulated by transcription factors during immune cell development, playing a critical role in early T and B cell development and homeostasis [1]. IL-7Rα forms a functional receptor complex with the common γ chain receptor (IL2RG), constituting the IL-7 receptor. This complex activates downstream signaling pathways, including JAK-STAT5 and PI3K-AKT, which upregulate Bcl-2 and cell cycle regulators, promoting lymphocyte survival, proliferation, and differentiation, essential for T and B cell maturation [1-2]. The IL-7/IL-7Rα axis is central to maintaining peripheral T cell homeostasis, regulating memory T cell generation, and promoting thymic T cell output. It also influences NK cell development and innate lymphoid cell (ILC) maturation. Notably, IL7R gene polymorphisms are associated with autoimmune diseases, such as multiple sclerosis and systemic lupus erythematosus [1-3]. Dysregulation of IL-7R signaling is pathogenic; deficiency is linked to severe combined immunodeficiency (SCID) [4], while overexpression or aberrant activation may promote tumor growth, metastasis, and alter the tumor microenvironment [5]. Consequently, targeting the IL-7R pathway holds therapeutic potential for immune and tumor-related diseases, positioning IL-7Rα as a potential target in autoimmune diseases, immunodeficiency, and cancer [3-5].
The B6-hIL7R mouse is a humanized model constructed using gene editing technology, where the mouse IL7R endogenous extracellular domain was replaced with the human IL7R extracellular domain. The murine IL7R signal peptide and cytoplasmic region was preserved. Homozygous B6-hIL7R mice are viable and fertile. This model can be used for studying the pathological mechanisms and therapeutic approaches of autoimmune diseases, immunodeficiency, and cancer, and for the development of IL7R-targeted drugs.
The IL7R gene encodes the interleukin-7 receptor α chain (IL-7Rα), also known as CD127, a member of the type I cytokine receptor family. Expressed on T, B, NK, monocytes, and dendritic cells, IL7R gene expression is tightly regulated by transcription factors during immune cell development, playing a critical role in early T and B cell development and homeostasis [1]. IL-7Rα forms a functional receptor complex with the common γ chain receptor (IL2RG), constituting the IL-7 receptor. This complex activates downstream signaling pathways, including JAK-STAT5 and PI3K-AKT, which upregulate Bcl-2 and cell cycle regulators, promoting lymphocyte survival, proliferation, and differentiation, essential for T and B cell maturation [1-2]. The IL-7/IL-7Rα axis is central to maintaining peripheral T cell homeostasis, regulating memory T cell generation, and promoting thymic T cell output. It also influences NK cell development and innate lymphoid cell (ILC) maturation. Notably, IL7R gene polymorphisms are associated with autoimmune diseases, such as multiple sclerosis and systemic lupus erythematosus [1-3]. Dysregulation of IL-7R signaling is pathogenic; deficiency is linked to severe combined immunodeficiency (SCID) [4], while overexpression or aberrant activation may promote tumor growth, metastasis, and alter the tumor microenvironment [5]. Consequently, targeting the IL-7R pathway holds therapeutic potential for immune and tumor-related diseases, positioning IL-7Rα as a potential target in autoimmune diseases, immunodeficiency, and cancer [3-5].
The B6-hIL7R mouse is a humanized model constructed using gene editing technology, where the mouse IL7R endogenous extracellular domain was replaced with the human IL7R extracellular domain. The murine IL7R signal peptide and cytoplasmic region was preserved. Homozygous B6-hIL7R mice are viable and fertile. This model can be used for studying the pathological mechanisms and therapeutic approaches of autoimmune diseases, immunodeficiency, and cancer, and for the development of IL7R-targeted drugs.
B6-hGDF15
Product ID:
C001520
Strain:
C57BL/6JCya
Status:
Description:
The Growth Differentiation Factor 15 (GDF15) gene encodes a secreted ligand of the Transforming Growth Factor-β (TGF-β) superfamily protein. This protein plays a crucial role in the TGFβ signaling pathway, which is integral to various cellular processes [1]. GDF15 is involved in the body’s response to stress following cell damage. It is associated with tissue hypoxia, inflammation, acute injury, and oxidative stress, among other disease states. Elevated levels of GDF15 in the serum are considered a potential biomarker for the progression of cancer, as it is overexpressed in various types of tumor cells, including colon, prostate, pancreatic, breast, and thyroid cancers [2-3]. Interestingly, GDF15 is not solely a pathological biomarker. Despite its association with disease states, it also exhibits high expression under various non-pathological conditions. Studies suggest that GDF15 may exert a protective effect on the heart, liver, kidney, and lungs following inflammation and injury, highlighting its potential role in tissue repair and recovery [4].
GDF15 is an important biomarker for metabolic diseases, cardiovascular diseases, tumors, and more, and holds potential as a therapeutic target. It can induce anorexia by activating the GFRAL-RET receptor in the brainstem, making it a promising target for anti-obesity therapy [5]. Furthermore, GDF15 neutralization could potentially alleviate anorexia and weight loss, common side effects of platinum-based chemotherapy [6]. Research has shown that a therapeutic antagonistic monoclonal antibody can inhibit RET signal transduction by blocking the interaction between GDF15-driven RET and cell surface GFRAL. This could reverse excessive lipid oxidation in tumor-bearing mice and prevent cancer cachexia [7]. The potential of GDF15 as a therapeutic target is being increasingly recognized in the scientific community. In this context, the construction of animal gene humanization models for this target is of significant importance, providing a crucial tool for further research and development in this area.
This strain is a mouse Gdf15 gene humanized model expressing human GDF15 protein obtained by replacing the sequence encoding the endogenous structural domain in the mouse Gdf15 gene with the sequence encoding the structural domain in the human GDF15 gene. B6-hGDF15 mice can be used for research on metabolic diseases, cardiovascular diseases, tumor occurrence and development, etc., to assist in the preclinical evaluation of GDF15-targeted drugs.
The Growth Differentiation Factor 15 (GDF15) gene encodes a secreted ligand of the Transforming Growth Factor-β (TGF-β) superfamily protein. This protein plays a crucial role in the TGFβ signaling pathway, which is integral to various cellular processes [1]. GDF15 is involved in the body’s response to stress following cell damage. It is associated with tissue hypoxia, inflammation, acute injury, and oxidative stress, among other disease states. Elevated levels of GDF15 in the serum are considered a potential biomarker for the progression of cancer, as it is overexpressed in various types of tumor cells, including colon, prostate, pancreatic, breast, and thyroid cancers [2-3]. Interestingly, GDF15 is not solely a pathological biomarker. Despite its association with disease states, it also exhibits high expression under various non-pathological conditions. Studies suggest that GDF15 may exert a protective effect on the heart, liver, kidney, and lungs following inflammation and injury, highlighting its potential role in tissue repair and recovery [4].
GDF15 is an important biomarker for metabolic diseases, cardiovascular diseases, tumors, and more, and holds potential as a therapeutic target. It can induce anorexia by activating the GFRAL-RET receptor in the brainstem, making it a promising target for anti-obesity therapy [5]. Furthermore, GDF15 neutralization could potentially alleviate anorexia and weight loss, common side effects of platinum-based chemotherapy [6]. Research has shown that a therapeutic antagonistic monoclonal antibody can inhibit RET signal transduction by blocking the interaction between GDF15-driven RET and cell surface GFRAL. This could reverse excessive lipid oxidation in tumor-bearing mice and prevent cancer cachexia [7]. The potential of GDF15 as a therapeutic target is being increasingly recognized in the scientific community. In this context, the construction of animal gene humanization models for this target is of significant importance, providing a crucial tool for further research and development in this area.
This strain is a mouse Gdf15 gene humanized model expressing human GDF15 protein obtained by replacing the sequence encoding the endogenous structural domain in the mouse Gdf15 gene with the sequence encoding the structural domain in the human GDF15 gene. B6-hGDF15 mice can be used for research on metabolic diseases, cardiovascular diseases, tumor occurrence and development, etc., to assist in the preclinical evaluation of GDF15-targeted drugs.
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