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B6-hLPA(CKI)/Alb-cre/hPCSK9
製品ID :
I002079
系統:
C57BL/6NCya
状況:
説明:
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).
huIL17A
製品ID :
C001510
系統:
C57BL/6NCya
状況:
説明:
Interleukin 17A (IL-17A) is a signature cytokine of the T helper 17 (Th17) subset of CD4+ T cells and one of the six members (IL-17A~IL-17F) of the IL-17 family. IL-17A is primarily produced by Th17 cells and can also be produced by other immune cells under certain conditions, including CD8+ T cells, γδT cells, natural killer T (NKT) cells, monocytes, neutrophils, and microglia [1]. IL-17A mediates downstream pathways that induce the production of inflammatory molecules, chemokines, antimicrobial peptides, and remodeling proteins, which have important effects on host defense, cell transport, immune regulation, and tissue repair, especially in inducing innate immune defense. In healthy skin, commensal microorganisms induce the production of IL-17A to provide antifungal protection. When the skin barrier is damaged, IL-17A promotes epithelial cell proliferation and can clear pathogenic factors, promoting tissue repair and wound healing [2]. IL-17A usually protects the body when it is acutely injured, but when a wound requires long-term healing and becomes a chronic injury, the role of IL-17A may transform into wound erosion or excessive proliferation, ultimately leading to loss of function [3].
IL-17A plays a key role in various infectious diseases, inflammations, autoimmune diseases, and cancers. Its high expression level is associated with chronic inflammatory diseases such as rheumatoid arthritis, psoriasis, and multiple sclerosis. Lung injury caused by severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) is largely the result of the promotion of inflammatory reactions by cytokines such as IL-17A. Dysregulation of IL-17 signaling promotes pathogenic inflammation. IL-17A has a pathogenic role in mediating the important inflammatory pathway of psoriasis. The IL-23/Th17/IL-17A pathway is a key link in its pathogenesis, and inhibiting the expression of IL-17A can effectively alleviate psoriasis [4]. IL-17A is also associated with the course of ankylosing spondylitis (AS), and IL-17A inhibitors can effectively treat AS [5]. In addition, studies have shown that IL-17A is involved in the pathogenesis of neurodegenerative diseases in the central nervous system, and its expression level is related to the severity and progression of the disease [3].
huIL17A mice are humanized mouse models that express human IL-17A protein. They were constructed by using gene editing technology to replace the sequence encoding the endogenous extracellular domain of the mouse Il17a gene with the corresponding sequence from the human IL17A gene while retaining the mouse signal peptide. This strain can be used for mechanism research and preclinical evaluation of therapeutic drugs for various chronic inflammatory diseases such as rheumatoid arthritis, psoriasis, and multiple sclerosis. The homozygotes are viable and fertile.
Interleukin 17A (IL-17A) is a signature cytokine of the T helper 17 (Th17) subset of CD4+ T cells and one of the six members (IL-17A~IL-17F) of the IL-17 family. IL-17A is primarily produced by Th17 cells and can also be produced by other immune cells under certain conditions, including CD8+ T cells, γδT cells, natural killer T (NKT) cells, monocytes, neutrophils, and microglia [1]. IL-17A mediates downstream pathways that induce the production of inflammatory molecules, chemokines, antimicrobial peptides, and remodeling proteins, which have important effects on host defense, cell transport, immune regulation, and tissue repair, especially in inducing innate immune defense. In healthy skin, commensal microorganisms induce the production of IL-17A to provide antifungal protection. When the skin barrier is damaged, IL-17A promotes epithelial cell proliferation and can clear pathogenic factors, promoting tissue repair and wound healing [2]. IL-17A usually protects the body when it is acutely injured, but when a wound requires long-term healing and becomes a chronic injury, the role of IL-17A may transform into wound erosion or excessive proliferation, ultimately leading to loss of function [3].
IL-17A plays a key role in various infectious diseases, inflammations, autoimmune diseases, and cancers. Its high expression level is associated with chronic inflammatory diseases such as rheumatoid arthritis, psoriasis, and multiple sclerosis. Lung injury caused by severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) is largely the result of the promotion of inflammatory reactions by cytokines such as IL-17A. Dysregulation of IL-17 signaling promotes pathogenic inflammation. IL-17A has a pathogenic role in mediating the important inflammatory pathway of psoriasis. The IL-23/Th17/IL-17A pathway is a key link in its pathogenesis, and inhibiting the expression of IL-17A can effectively alleviate psoriasis [4]. IL-17A is also associated with the course of ankylosing spondylitis (AS), and IL-17A inhibitors can effectively treat AS [5]. In addition, studies have shown that IL-17A is involved in the pathogenesis of neurodegenerative diseases in the central nervous system, and its expression level is related to the severity and progression of the disease [3].
huIL17A mice are humanized mouse models that express human IL-17A protein. They were constructed by using gene editing technology to replace the sequence encoding the endogenous extracellular domain of the mouse Il17a gene with the corresponding sequence from the human IL17A gene while retaining the mouse signal peptide. This strain can be used for mechanism research and preclinical evaluation of therapeutic drugs for various chronic inflammatory diseases such as rheumatoid arthritis, psoriasis, and multiple sclerosis. The homozygotes are viable and fertile.
huIL6
製品ID :
C001605
系統:
C57BL/6NCya
状況:
説明:
Interleukin-6 (IL-6) is a cytokine that plays a crucial role in inflammation and B cell maturation. It is primarily produced and secreted into the serum at sites of acute and chronic inflammation, inducing inflammatory responses through the interleukin-6 receptor alpha (IL-6Rα). Upon binding to IL-6Rα, IL-6 interacts with two GP130 molecules to form a hexameric complex in a 2:2:2 configuration. This receptor complex formation recruits tyrosine kinases from the Janus kinase family (JAK1, JAK2, and TYK2), which phosphorylate tyrosine sites within the intracellular domain of GP130, leading to the activation of signaling cascades. IL-6 has a broad impact on both immune and non-immune cells. In CD4+ T helper (Th) cells, IL-6 drives the differentiation of activated naïve Th cells into IL-17 and IL-22 expressing Th17 and Th22 cells, which are crucial for anti-bacterial and anti-fungal defense. Conversely, IL-6 inhibits the differentiation of CD4+ T regulatory cells, which play a key role in restraining inflammatory responses. In hepatocytes, IL-6 induces the expression of inflammation-induced acute phase proteins, including C-reactive protein (CRP) [1]. IL-6 is a pleiotropic cytokine associated with various diseases, including diabetes and systemic juvenile idiopathic arthritis. IL-6 signatures, partially based on the activity of STAT1 and STAT3, are indicators of prognosis or therapeutic response in patients with autoimmune diseases or cancer. Its role as a target in cancer immunotherapy and autoimmune diseases has attracted widespread attention [2-4].
The huIL6 mouse is an Il6 gene humanized model, in which the endogenous Il6 gene sequence in mice is replaced in situ with the human IL6 gene sequence. This model can be used in researching autoimmune diseases, inflammation-related diseases, cancer, and infectious diseases. It is also useful for the development, screening, and evaluation of IL6-targeted drugs.
Interleukin-6 (IL-6) is a cytokine that plays a crucial role in inflammation and B cell maturation. It is primarily produced and secreted into the serum at sites of acute and chronic inflammation, inducing inflammatory responses through the interleukin-6 receptor alpha (IL-6Rα). Upon binding to IL-6Rα, IL-6 interacts with two GP130 molecules to form a hexameric complex in a 2:2:2 configuration. This receptor complex formation recruits tyrosine kinases from the Janus kinase family (JAK1, JAK2, and TYK2), which phosphorylate tyrosine sites within the intracellular domain of GP130, leading to the activation of signaling cascades. IL-6 has a broad impact on both immune and non-immune cells. In CD4+ T helper (Th) cells, IL-6 drives the differentiation of activated naïve Th cells into IL-17 and IL-22 expressing Th17 and Th22 cells, which are crucial for anti-bacterial and anti-fungal defense. Conversely, IL-6 inhibits the differentiation of CD4+ T regulatory cells, which play a key role in restraining inflammatory responses. In hepatocytes, IL-6 induces the expression of inflammation-induced acute phase proteins, including C-reactive protein (CRP) [1]. IL-6 is a pleiotropic cytokine associated with various diseases, including diabetes and systemic juvenile idiopathic arthritis. IL-6 signatures, partially based on the activity of STAT1 and STAT3, are indicators of prognosis or therapeutic response in patients with autoimmune diseases or cancer. Its role as a target in cancer immunotherapy and autoimmune diseases has attracted widespread attention [2-4].
The huIL6 mouse is an Il6 gene humanized model, in which the endogenous Il6 gene sequence in mice is replaced in situ with the human IL6 gene sequence. This model can be used in researching autoimmune diseases, inflammation-related diseases, cancer, and infectious diseases. It is also useful for the development, screening, and evaluation of IL6-targeted drugs.
huIL17F
製品ID :
C001715
系統:
C57BL/6NCya
状況:
説明:
The IL17F gene, located on chromosome 6p12.2, is primarily expressed by activated T cells, particularly Th17 cells, as well as other immune cells like γδ T cells and some innate immune cells [1]. The gene encodes the interleukin-17F (IL-17F) cytokine, a disulfide-linked homodimer protein that shares significant sequence homology with IL-17A [2]. Functionally, IL-17F is a pro-inflammatory cytokine that binds to the IL-17RA/RC receptor complex, triggering downstream signaling pathways involving Act1 and TRAF6, leading to the induction of various cytokines (like IL-6, IL-8, GM-CSF) and chemokines, which contribute to neutrophil recruitment and inflammation in barrier tissues such as the skin, lungs, and gut [3]. Elevated levels or dysregulation of IL-17F have been implicated in the pathogenesis of several autoimmune and inflammatory diseases, including psoriasis, rheumatoid arthritis, inflammatory bowel disease (like Crohn's disease and ulcerative colitis), and potentially Sjögren's syndrome, highlighting its role in chronic inflammatory processes [2-4].
The huIL17F mouse is a humanized model constructed by replacing the sequence of the mouse Il17f gene in situ with the corresponding sequence from the human IL17F gene. The huIL17F mice can be used for studies on psoriasis, rheumatoid arthritis, inflammatory bowel disease, and pathogenesis of inflammatory disorders, as well as for IL17F-targeted drug development.
The IL17F gene, located on chromosome 6p12.2, is primarily expressed by activated T cells, particularly Th17 cells, as well as other immune cells like γδ T cells and some innate immune cells [1]. The gene encodes the interleukin-17F (IL-17F) cytokine, a disulfide-linked homodimer protein that shares significant sequence homology with IL-17A [2]. Functionally, IL-17F is a pro-inflammatory cytokine that binds to the IL-17RA/RC receptor complex, triggering downstream signaling pathways involving Act1 and TRAF6, leading to the induction of various cytokines (like IL-6, IL-8, GM-CSF) and chemokines, which contribute to neutrophil recruitment and inflammation in barrier tissues such as the skin, lungs, and gut [3]. Elevated levels or dysregulation of IL-17F have been implicated in the pathogenesis of several autoimmune and inflammatory diseases, including psoriasis, rheumatoid arthritis, inflammatory bowel disease (like Crohn's disease and ulcerative colitis), and potentially Sjögren's syndrome, highlighting its role in chronic inflammatory processes [2-4].
The huIL17F mouse is a humanized model constructed by replacing the sequence of the mouse Il17f gene in situ with the corresponding sequence from the human IL17F gene. The huIL17F mice can be used for studies on psoriasis, rheumatoid arthritis, inflammatory bowel disease, and pathogenesis of inflammatory disorders, as well as for IL17F-targeted drug development.
huANGPTL3
製品ID :
C001400
系統:
C57BL/6JCya
状況:
説明:
Angiopoietin‑like protein 3 (ANGPTL3) is mainly expressed in the liver and is a secreted glycoprotein structurally related to angiopoietins. The mature form of human ANGPTL3 protein contains an N‑terminal coiled‑coil domain and a C‑terminal fibrinogen‑like (FBN) domain. Through binding of its FBN‑like domain to integrin αvβ3, ANGPTL3 induces endothelial cell adhesion and migration, thereby playing a role in the regulation of angiogenesis [1]. In addition, ANGPTL3 can directly inhibit lipoprotein lipase (LPL) and endothelial lipase (EL), which are closely involved in the hydrolysis of circulating triglycerides (TG) and high‑density lipoprotein cholesterol (HDL‑C), respectively, thereby elevating circulating TG levels and affecting HDL levels [2-3]. In humans, ANGPTL3 is an important factor for HDL levels, and its plasma level is positively correlated with HDL‑C. Loss‑of‑function mutations in the ANGPTL3 gene (especially homozygous or compound heterozygous) lead to familial combined hypolipidemia (FHBL2) [4]. Furthermore, ANGPTL3 also plays important roles in biological and pathological processes related to lipid metabolism and angiogenesis, such as atherosclerosis, tumors, nephrotic syndrome, diabetes, and liver disease [3].
This strain is a mouse Angptl3 gene humanized model. The mouse Angptl3 gene is replaced with the human ANGPTL3 gene sequence by gene editing technology, which expresses the human ANGPTL3 protein while retaining the signal peptide of mouse Angptl3. This model can be used to study the pathogenesis of metabolic diseases such as atherosclerosis, diabetes, and familial combined hyperlipidemia (FCH), as well as the development and screening of ANGPTL3-targeted drugs. The homozygous huANGPTL3 mice are viable and fertile.
Angiopoietin‑like protein 3 (ANGPTL3) is mainly expressed in the liver and is a secreted glycoprotein structurally related to angiopoietins. The mature form of human ANGPTL3 protein contains an N‑terminal coiled‑coil domain and a C‑terminal fibrinogen‑like (FBN) domain. Through binding of its FBN‑like domain to integrin αvβ3, ANGPTL3 induces endothelial cell adhesion and migration, thereby playing a role in the regulation of angiogenesis [1]. In addition, ANGPTL3 can directly inhibit lipoprotein lipase (LPL) and endothelial lipase (EL), which are closely involved in the hydrolysis of circulating triglycerides (TG) and high‑density lipoprotein cholesterol (HDL‑C), respectively, thereby elevating circulating TG levels and affecting HDL levels [2-3]. In humans, ANGPTL3 is an important factor for HDL levels, and its plasma level is positively correlated with HDL‑C. Loss‑of‑function mutations in the ANGPTL3 gene (especially homozygous or compound heterozygous) lead to familial combined hypolipidemia (FHBL2) [4]. Furthermore, ANGPTL3 also plays important roles in biological and pathological processes related to lipid metabolism and angiogenesis, such as atherosclerosis, tumors, nephrotic syndrome, diabetes, and liver disease [3].
This strain is a mouse Angptl3 gene humanized model. The mouse Angptl3 gene is replaced with the human ANGPTL3 gene sequence by gene editing technology, which expresses the human ANGPTL3 protein while retaining the signal peptide of mouse Angptl3. This model can be used to study the pathogenesis of metabolic diseases such as atherosclerosis, diabetes, and familial combined hyperlipidemia (FCH), as well as the development and screening of ANGPTL3-targeted drugs. The homozygous huANGPTL3 mice are viable and fertile.
huIL6/hIL6RA/Apoe-KO
製品ID :
C002139
系統:
C57BL/6Cya
状況:
説明:
Interleukin-6 (IL-6) is a cytokine that plays a crucial role in inflammation and B cell maturation. It is primarily produced and secreted into the serum at sites of acute and chronic inflammation, inducing inflammatory responses through the interleukin-6 receptor alpha (IL-6Rα). The IL6RA (IL6R, also known as CD126) gene encodes a subunit of the interleukin-6 (IL-6) receptor complex. The IL-6 receptor is a protein complex composed of the IL6RA protein and the interleukin-6 signal transducer (IL6ST/GP130/IL6-beta). This receptor subunit is shared by many other cytokines. The expression of IL-6R is primarily restricted to hepatocytes, leukocytes, and megakaryocytes. Upon binding to IL-6Rα, IL-6 interacts with two GP130 molecules to form a hexameric complex in a 2:2:2 configuration [1]. Once the IL-6 receptor complex is activated, multiple downstream events allow IL-6 to mediate its diverse effects. These include the pathways of the GTPase Ras and its effector Raf, the mitogen-activated protein kinase cascade that controls cellular proliferation and differentiation, and the pathways involving tyrosine kinases of the Jak family and transcription factors of the STAT family [2].
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 [3]. 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 [4]. 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 [3-6]. In addition, ApoE forms a complex with activated C1q, becoming a checkpoint inhibitor target of the classical complement pathway [7].
The huIL6/hIL6RA/Apoe-KO mouse is a combined genetically modified model generated by crossing the huIL6 mouse (Catalog No.: C001605), the hIL6RA mouse (Catalog No.: C001606), and the Apoe-KO(6J) mouse (Catalog No.: C001507). The huIL6/hIL6RA/Apoe-KO mouse can be utilized for the screening, pharmacodynamic evaluation, safety assessment, and mechanism of action studies of IL6/IL6RA-targeted therapeutics. With the Apoe knockout background, the model can also be used for research on hypercholesterolemia and atherosclerosis, providing a preclinical research tool for exploring the effects of IL6/IL6RA-targeted interventions in relevant disease settings.
Interleukin-6 (IL-6) is a cytokine that plays a crucial role in inflammation and B cell maturation. It is primarily produced and secreted into the serum at sites of acute and chronic inflammation, inducing inflammatory responses through the interleukin-6 receptor alpha (IL-6Rα). The IL6RA (IL6R, also known as CD126) gene encodes a subunit of the interleukin-6 (IL-6) receptor complex. The IL-6 receptor is a protein complex composed of the IL6RA protein and the interleukin-6 signal transducer (IL6ST/GP130/IL6-beta). This receptor subunit is shared by many other cytokines. The expression of IL-6R is primarily restricted to hepatocytes, leukocytes, and megakaryocytes. Upon binding to IL-6Rα, IL-6 interacts with two GP130 molecules to form a hexameric complex in a 2:2:2 configuration [1]. Once the IL-6 receptor complex is activated, multiple downstream events allow IL-6 to mediate its diverse effects. These include the pathways of the GTPase Ras and its effector Raf, the mitogen-activated protein kinase cascade that controls cellular proliferation and differentiation, and the pathways involving tyrosine kinases of the Jak family and transcription factors of the STAT family [2].
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 [3]. 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 [4]. 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 [3-6]. In addition, ApoE forms a complex with activated C1q, becoming a checkpoint inhibitor target of the classical complement pathway [7].
The huIL6/hIL6RA/Apoe-KO mouse is a combined genetically modified model generated by crossing the huIL6 mouse (Catalog No.: C001605), the hIL6RA mouse (Catalog No.: C001606), and the Apoe-KO(6J) mouse (Catalog No.: C001507). The huIL6/hIL6RA/Apoe-KO mouse can be utilized for the screening, pharmacodynamic evaluation, safety assessment, and mechanism of action studies of IL6/IL6RA-targeted therapeutics. With the Apoe knockout background, the model can also be used for research on hypercholesterolemia and atherosclerosis, providing a preclinical research tool for exploring the effects of IL6/IL6RA-targeted interventions in relevant disease settings.
huIL18R1/huIL18RAP/huIL18BP
製品ID :
C002137
系統:
C57BL/6Cya
状況:
説明:
Interleukin-18 (IL-18) is an important pro-inflammatory cytokine that binds to its receptor complex (IL-18Rα encoded by IL18R1 and IL-18Rβ encoded by IL18RAP), activating downstream MyD88/NF-κB and MAPK signaling pathways and playing key regulatory roles in innate and adaptive immunity [1]. The IL18BP (Interleukin 18 Binding Protein) gene encodes a secreted, high-affinity, naturally occurring antagonist of the proinflammatory cytokine IL-18, functioning by binding IL-18 to prevent it from interacting with its receptor, thereby inhibiting IL-18-induced immune responses, such as interferon-gamma (IFN-γ) production [2]. The gene's protein, IL-18BP, is constitutively expressed and secreted primarily by mononuclear cells (such as monocytes/macrophages and T-cells) and is widely expressed at the RNA level in numerous tissues, including the spleen, lung, placenta, and small intestine [3].
The huIL18R1/huIL18RAP/huIL18BP mouse is a triple-gene humanized model obtained by crossing the huIL18R1/huIL18RAP mouse (Catalog No.: C002016) with the huIL18BP mouse (Catalog No.: C001869). The huIL18R1/huIL18RAP/huIL18BP mouse can be utilized for screening, pharmacodynamic evaluation, safety assessment, and mechanism of action studies of multi-target therapeutics targeting the IL-18 receptor complex (IL18R1/IL18RAP) and the natural antagonist of IL-18, IL18BP. It provides an ideal preclinical research platform for developing innovative therapies for inflammatory bowel disease (IBD), rheumatoid arthritis (RA), psoriasis, and systemic lupus erythematosus (SLE), as well as for tumor immunology-related research.
Interleukin-18 (IL-18) is an important pro-inflammatory cytokine that binds to its receptor complex (IL-18Rα encoded by IL18R1 and IL-18Rβ encoded by IL18RAP), activating downstream MyD88/NF-κB and MAPK signaling pathways and playing key regulatory roles in innate and adaptive immunity [1]. The IL18BP (Interleukin 18 Binding Protein) gene encodes a secreted, high-affinity, naturally occurring antagonist of the proinflammatory cytokine IL-18, functioning by binding IL-18 to prevent it from interacting with its receptor, thereby inhibiting IL-18-induced immune responses, such as interferon-gamma (IFN-γ) production [2]. The gene's protein, IL-18BP, is constitutively expressed and secreted primarily by mononuclear cells (such as monocytes/macrophages and T-cells) and is widely expressed at the RNA level in numerous tissues, including the spleen, lung, placenta, and small intestine [3].
The huIL18R1/huIL18RAP/huIL18BP mouse is a triple-gene humanized model obtained by crossing the huIL18R1/huIL18RAP mouse (Catalog No.: C002016) with the huIL18BP mouse (Catalog No.: C001869). The huIL18R1/huIL18RAP/huIL18BP mouse can be utilized for screening, pharmacodynamic evaluation, safety assessment, and mechanism of action studies of multi-target therapeutics targeting the IL-18 receptor complex (IL18R1/IL18RAP) and the natural antagonist of IL-18, IL18BP. It provides an ideal preclinical research platform for developing innovative therapies for inflammatory bowel disease (IBD), rheumatoid arthritis (RA), psoriasis, and systemic lupus erythematosus (SLE), as well as for tumor immunology-related research.
huIL5RA
製品ID :
C002007
系統:
C57BL/6NCya
状況:
説明:
The IL5RA gene encodes the interleukin-5 receptor subunit alpha (IL5RA), the receptor subunit that specifically binds IL5. It is primarily expressed on eosinophils, basophils, and their progenitor cells, with low expression levels in most normal tissues [1]. IL5RA plays a critical role in the proliferation, differentiation, survival, recruitment, and activation of eosinophils. Upon binding to IL5, it activates downstream signaling pathways such as JAK2-STAT5, thereby promoting type 2 inflammatory responses. Excessive activation of the IL5/IL5RA axis in cells or tissues can lead to eosinophil expansion and tissue infiltration, exacerbating inflammation and tissue damage [2]. IL5RA exerts a central regulatory role in the pathogenesis of eosinophil-related inflammatory diseases, including severe eosinophilic asthma (SEA), chronic rhinosinusitis with nasal polyps (CRSwNP), and eosinophilic granulomatosis with polyangiitis (EGPA) [3-5]. Studies have shown that abnormal IL5RA expression is causally associated with the genetic risk of multiple myeloma (MM), positioning it as a potential tumor biomarker and therapeutic target [6]. Humanized anti-IL5RA CAR-T cell therapy can effectively deplete eosinophils and their precursors at various developmental stages in the bone marrow and peripheral blood [1]. Currently, multiple clinical drugs targeting the IL-5/IL5RA pathway have been approved or are under development, including mepolizumab, reslizumab, and benralizumab [7-8].
The huIL5RA mouse was generated by replacing the mouse Il5ra endogenous extracellular domain with the human IL5RA extracellular domain. The murine transmembrane-cytoplasmic region was preserved. huIL5RA mice can be used for research and development as well as preclinical pharmacological and efficacy evaluation of IL5RA-targeted drugs for multiple eosinophil-related inflammatory diseases, including severe eosinophilic asthma (SEA), chronic rhinosinusitis with nasal polyps (CRSwNP), and eosinophilic granulomatosis with polyangiitis (EGPA), as well as multiple myeloma (MM).
The IL5RA gene encodes the interleukin-5 receptor subunit alpha (IL5RA), the receptor subunit that specifically binds IL5. It is primarily expressed on eosinophils, basophils, and their progenitor cells, with low expression levels in most normal tissues [1]. IL5RA plays a critical role in the proliferation, differentiation, survival, recruitment, and activation of eosinophils. Upon binding to IL5, it activates downstream signaling pathways such as JAK2-STAT5, thereby promoting type 2 inflammatory responses. Excessive activation of the IL5/IL5RA axis in cells or tissues can lead to eosinophil expansion and tissue infiltration, exacerbating inflammation and tissue damage [2]. IL5RA exerts a central regulatory role in the pathogenesis of eosinophil-related inflammatory diseases, including severe eosinophilic asthma (SEA), chronic rhinosinusitis with nasal polyps (CRSwNP), and eosinophilic granulomatosis with polyangiitis (EGPA) [3-5]. Studies have shown that abnormal IL5RA expression is causally associated with the genetic risk of multiple myeloma (MM), positioning it as a potential tumor biomarker and therapeutic target [6]. Humanized anti-IL5RA CAR-T cell therapy can effectively deplete eosinophils and their precursors at various developmental stages in the bone marrow and peripheral blood [1]. Currently, multiple clinical drugs targeting the IL-5/IL5RA pathway have been approved or are under development, including mepolizumab, reslizumab, and benralizumab [7-8].
The huIL5RA mouse was generated by replacing the mouse Il5ra endogenous extracellular domain with the human IL5RA extracellular domain. The murine transmembrane-cytoplasmic region was preserved. huIL5RA mice can be used for research and development as well as preclinical pharmacological and efficacy evaluation of IL5RA-targeted drugs for multiple eosinophil-related inflammatory diseases, including severe eosinophilic asthma (SEA), chronic rhinosinusitis with nasal polyps (CRSwNP), and eosinophilic granulomatosis with polyangiitis (EGPA), as well as multiple myeloma (MM).
huPD-1/huVEGFA
製品ID :
C001598
系統:
C57BL/6JCya
状況:
説明:
Programmed cell death protein 1 (PDCD1/PD-1) is a member of the B7-CD28 costimulatory receptor family. It is an inhibitory receptor expressed on activated T cells and plays a role in regulating the function of effector T cells, including CD8+ T cells, and promoting the differentiation of CD4+ T cells into regulatory T cells. PD-1 is expressed in a variety of tumors and plays an important role in antitumor immunity. In addition, PD-1 is involved in the defense against autoimmune diseases and has inhibitory effects on antitumor and antimicrobial immunity [1]. PD-1 binds to programmed death ligands 1 and 2 (PD-L1 and PD-L2) to inhibit T cell activation, reduce the production of corresponding cytokines, and regulate T cell survival [2]. Drugs targeting this pathway can reactivate T cells to activate antitumor immune responses [3].
The Vascular Endothelial Growth Factor (VEGF) family is a group of particular endothelial growth factors intimately associated with angiogenesis. These factors promote increased vascular permeability, extracellular matrix degeneration, vascular endothelial cell migration and proliferation, and are capable of stimulating angiogenesis and increasing the permeability of existing vessels. As such, they play a pivotal role in normal vascular development and wound healing. The VEGF family comprises VEGFA, VEGFB, VEGFC, VEGFD, VEGFE, and PLGF [4]. Of these, VEGFA is the most commonly targeted in research related to neovascular ophthalmic diseases due to its crucial role in the proliferation, migration, and formation of endothelial cell microvessels [5]. Overexpression of VEGFA in the eye can result in abnormal vascular growth and leakage, leading to various ophthalmic diseases such as Age-Related Macular Degeneration (AMD), Diabetic Retinopathy (DR), and corneal neovascularization [5-6]. The progression of solid tumors depends on vascularization and angiogenesis within malignant tissues, with VEGFA playing a crucial role among various pro-angiogenic factors. The VEGFA gene is upregulated in many known tumors, correlating with tumor staging and progression. Blocking VEGFA may lead to vascular network regression, inhibiting tumor growth [7]. Thus, VEGFA is an important target for anti-angiogenic cancer therapies.
The huPD-1/huVEGFA mouse is a humanized model obtained by crossbreeding huPD-1 mice (Catalog No. C001524) with huVEGFA mice (Catalog No. C001555). This model can be used for research in drug development, efficacy and safety evaluation, tumor immunotherapy evaluation, and immune system mechanisms related to human PD-1/VEGFA.
Programmed cell death protein 1 (PDCD1/PD-1) is a member of the B7-CD28 costimulatory receptor family. It is an inhibitory receptor expressed on activated T cells and plays a role in regulating the function of effector T cells, including CD8+ T cells, and promoting the differentiation of CD4+ T cells into regulatory T cells. PD-1 is expressed in a variety of tumors and plays an important role in antitumor immunity. In addition, PD-1 is involved in the defense against autoimmune diseases and has inhibitory effects on antitumor and antimicrobial immunity [1]. PD-1 binds to programmed death ligands 1 and 2 (PD-L1 and PD-L2) to inhibit T cell activation, reduce the production of corresponding cytokines, and regulate T cell survival [2]. Drugs targeting this pathway can reactivate T cells to activate antitumor immune responses [3].
The Vascular Endothelial Growth Factor (VEGF) family is a group of particular endothelial growth factors intimately associated with angiogenesis. These factors promote increased vascular permeability, extracellular matrix degeneration, vascular endothelial cell migration and proliferation, and are capable of stimulating angiogenesis and increasing the permeability of existing vessels. As such, they play a pivotal role in normal vascular development and wound healing. The VEGF family comprises VEGFA, VEGFB, VEGFC, VEGFD, VEGFE, and PLGF [4]. Of these, VEGFA is the most commonly targeted in research related to neovascular ophthalmic diseases due to its crucial role in the proliferation, migration, and formation of endothelial cell microvessels [5]. Overexpression of VEGFA in the eye can result in abnormal vascular growth and leakage, leading to various ophthalmic diseases such as Age-Related Macular Degeneration (AMD), Diabetic Retinopathy (DR), and corneal neovascularization [5-6]. The progression of solid tumors depends on vascularization and angiogenesis within malignant tissues, with VEGFA playing a crucial role among various pro-angiogenic factors. The VEGFA gene is upregulated in many known tumors, correlating with tumor staging and progression. Blocking VEGFA may lead to vascular network regression, inhibiting tumor growth [7]. Thus, VEGFA is an important target for anti-angiogenic cancer therapies.
The huPD-1/huVEGFA mouse is a humanized model obtained by crossbreeding huPD-1 mice (Catalog No. C001524) with huVEGFA mice (Catalog No. C001555). This model can be used for research in drug development, efficacy and safety evaluation, tumor immunotherapy evaluation, and immune system mechanisms related to human PD-1/VEGFA.
huOSM(BALB/c)
製品ID :
C001855
系統:
BALB/cAnCya
状況:
説明:
The OSM gene (Oncostatin M) encodes a secreted cytokine, Oncostatin M, which is a pleiotropic protein belonging to the leukemia inhibitory factor/oncostatin-M (LIF/OSM) family. This protein is expressed in various immune cells, including activated T lymphocytes, macrophages, and neutrophils, as well as in other tissues like endothelial cells, osteoblasts, and smooth muscle cells [1]. OSM plays diverse functions, acting as a growth regulator that can inhibit the proliferation of certain tumor cell lines, stimulate proliferation of others (e.g., AIDS-KS cells), and regulate the production of other cytokines like IL-6, G-CSF, and GM-CSF. Its activities are mediated through two receptor complexes: Type I (gp130 and LIFRβ) and Type II (gp130 and OSMRβ), primarily activating the JAK/STAT, MAPK, JNK, and PI3K/AKT signaling pathways [2]. OSM is implicated in a wide array of diseases, contributing to inflammatory conditions such as arthritis (rheumatoid and osteoarthritis), inflammatory bowel disease, lung and skin diseases (e.g., psoriasis, asthma), cardiovascular diseases (e.g., atherosclerosis), and liver diseases (e.g., fibrosis) [3]. It also exhibits a complex role in various cancers, sometimes inhibiting tumor growth in early stages or in specific cell lines, while promoting tumorigenesis, epithelial-mesenchymal transition (EMT), invasion, and metastasis in more advanced cancers like breast, cervical, ovarian, pancreatic, and lung cancers. Deficiency in OSM has also been linked to severe bone marrow failure syndromes [4].
huOSM(BALB/c) mice are humanized models constructed by gene-editing technology, in which the sequences from the ATG start codon to the TAG stop codon of the endogenous mouse Osm gene were replaced with the sequences from the ATG start codon to the TAG stop codon of the human OSM gene. This model can be used to study the pathogenesis of inflammatory diseases (such as rheumatoid arthritis, osteoarthritis, and inflammatory bowel disease), lung and skin diseases (such as asthma and psoriasis), cardiovascular diseases (such as atherosclerosis), liver diseases (such as fibrosis), and bone marrow failure syndrome, as well as the development of OSM-targeted drugs.
The OSM gene (Oncostatin M) encodes a secreted cytokine, Oncostatin M, which is a pleiotropic protein belonging to the leukemia inhibitory factor/oncostatin-M (LIF/OSM) family. This protein is expressed in various immune cells, including activated T lymphocytes, macrophages, and neutrophils, as well as in other tissues like endothelial cells, osteoblasts, and smooth muscle cells [1]. OSM plays diverse functions, acting as a growth regulator that can inhibit the proliferation of certain tumor cell lines, stimulate proliferation of others (e.g., AIDS-KS cells), and regulate the production of other cytokines like IL-6, G-CSF, and GM-CSF. Its activities are mediated through two receptor complexes: Type I (gp130 and LIFRβ) and Type II (gp130 and OSMRβ), primarily activating the JAK/STAT, MAPK, JNK, and PI3K/AKT signaling pathways [2]. OSM is implicated in a wide array of diseases, contributing to inflammatory conditions such as arthritis (rheumatoid and osteoarthritis), inflammatory bowel disease, lung and skin diseases (e.g., psoriasis, asthma), cardiovascular diseases (e.g., atherosclerosis), and liver diseases (e.g., fibrosis) [3]. It also exhibits a complex role in various cancers, sometimes inhibiting tumor growth in early stages or in specific cell lines, while promoting tumorigenesis, epithelial-mesenchymal transition (EMT), invasion, and metastasis in more advanced cancers like breast, cervical, ovarian, pancreatic, and lung cancers. Deficiency in OSM has also been linked to severe bone marrow failure syndromes [4].
huOSM(BALB/c) mice are humanized models constructed by gene-editing technology, in which the sequences from the ATG start codon to the TAG stop codon of the endogenous mouse Osm gene were replaced with the sequences from the ATG start codon to the TAG stop codon of the human OSM gene. This model can be used to study the pathogenesis of inflammatory diseases (such as rheumatoid arthritis, osteoarthritis, and inflammatory bowel disease), lung and skin diseases (such as asthma and psoriasis), cardiovascular diseases (such as atherosclerosis), liver diseases (such as fibrosis), and bone marrow failure syndrome, as well as the development of OSM-targeted drugs.
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