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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).
B6-hTROP2 (hTACSTD2)
製品ID :
C001718
系統:
C57BL/6NCya
状況:
説明:
Tumor-Associated Calcium Signal Transducer 2, encoded by the TACSTD2 gene, is a prominent type I transmembrane glycoprotein critically involved in mediating diverse cellular processes [1]. Acting primarily as a cell surface receptor, TROP2 transduces extracellular signals to initiate intracellular calcium release, thereby influencing key cellular behaviors including proliferation, adhesion, migration, and differentiation. While its expression is notably high during embryonic development, particularly in fetal tissues and trophoblasts, and maintained at lower levels in some normal adult epithelial lineages, aberrant and significant upregulation of TROP2 is a hallmark feature across a wide spectrum of human carcinomas [2]. This dysregulated expression contributes substantially to tumor initiation, progression, and metastasis by modulating various signaling pathways [3]. Beyond its role in oncogenesis, germline mutations in TACSTD2 are identified as the underlying cause of the rare autosomal recessive disorder, gelatinous drop-like corneal dystrophy [4]. The distinct expression profile of TROP2, with its high levels in numerous solid tumors contrasted by limited expression in most healthy adult tissues, positions it as a compelling and clinically relevant target for developing targeted therapies, notably antibody-drug conjugates, aimed at treating TROP2-expressing cancers [3].
The B6-hTROP2 (hTACSTD2) mouse is a humanized model constructed by replacing the signal peptide and extracellular domain of the mouse Tacstd2 with the corresponding signal peptide and extracellular domain from the human TACSTD2 gene. The B6-hTROP2 (hTACSTD2) mice can be used for studies on pathogenesis of various cancers, as well as for TACSTD2-targeted drug development.
Tumor-Associated Calcium Signal Transducer 2, encoded by the TACSTD2 gene, is a prominent type I transmembrane glycoprotein critically involved in mediating diverse cellular processes [1]. Acting primarily as a cell surface receptor, TROP2 transduces extracellular signals to initiate intracellular calcium release, thereby influencing key cellular behaviors including proliferation, adhesion, migration, and differentiation. While its expression is notably high during embryonic development, particularly in fetal tissues and trophoblasts, and maintained at lower levels in some normal adult epithelial lineages, aberrant and significant upregulation of TROP2 is a hallmark feature across a wide spectrum of human carcinomas [2]. This dysregulated expression contributes substantially to tumor initiation, progression, and metastasis by modulating various signaling pathways [3]. Beyond its role in oncogenesis, germline mutations in TACSTD2 are identified as the underlying cause of the rare autosomal recessive disorder, gelatinous drop-like corneal dystrophy [4]. The distinct expression profile of TROP2, with its high levels in numerous solid tumors contrasted by limited expression in most healthy adult tissues, positions it as a compelling and clinically relevant target for developing targeted therapies, notably antibody-drug conjugates, aimed at treating TROP2-expressing cancers [3].
The B6-hTROP2 (hTACSTD2) mouse is a humanized model constructed by replacing the signal peptide and extracellular domain of the mouse Tacstd2 with the corresponding signal peptide and extracellular domain from the human TACSTD2 gene. The B6-hTROP2 (hTACSTD2) mice can be used for studies on pathogenesis of various cancers, as well as for TACSTD2-targeted drug development.
hITGB6
製品ID :
C001871
系統:
C57BL/6NCya
状況:
説明:
The ITGB6 gene encodes the integrin β6 subunit, a member of the integrin superfamily of adhesion receptors which are heterodimeric integral membrane proteins. This subunit pairs exclusively with the αv subunit (encoded by ITGAV) to form the integrin αvβ6 heterodimer [1]. The primary function of the resulting αvβ6 protein is to mediate cell-to-extracellular matrix (ECM) signaling, particularly by binding to ECM ligands like fibronectin and, crucially, by activating latent transforming growth factor-β1 (TGF-β1), a cytokine that regulates tissue homeostasis, repair, and immune suppression. Gene expression is largely restricted to epithelial cells and is typically low or absent in healthy adult epithelia but is significantly upregulated in tissues undergoing development, wound healing, fibrosis, and in many cancers (e.g., pancreatic, colon, lung, oral squamous cell carcinoma) where its expression often correlates with poor prognosis and increased invasiveness [2]. Associated diseases include various forms of cancer, chronic organ fibrosis (such as pulmonary fibrosis), and rare genetic conditions like Amelogenesis Imperfecta and a syndrome characterized by alopecia and intellectual disability [3].
hITGB6 mouse is a humanized model generated using gene editing technology, in which the sequence from aa.22 to partial intron 4 was replaced with Human ITGB6 CDS-Mouse Itgb6 CDS-3’UTR of Mouse Itgb6-WPRE-BGH pA cassette. The murine signal peptide was preserved. This model can be used for studying the pathological mechanisms and therapeutic approaches of various forms of cancer, chronic organ fibrosis (such as pulmonary fibrosis), and rare genetic conditions, as well as for the development of ITGB6-targeted drugs.
The ITGB6 gene encodes the integrin β6 subunit, a member of the integrin superfamily of adhesion receptors which are heterodimeric integral membrane proteins. This subunit pairs exclusively with the αv subunit (encoded by ITGAV) to form the integrin αvβ6 heterodimer [1]. The primary function of the resulting αvβ6 protein is to mediate cell-to-extracellular matrix (ECM) signaling, particularly by binding to ECM ligands like fibronectin and, crucially, by activating latent transforming growth factor-β1 (TGF-β1), a cytokine that regulates tissue homeostasis, repair, and immune suppression. Gene expression is largely restricted to epithelial cells and is typically low or absent in healthy adult epithelia but is significantly upregulated in tissues undergoing development, wound healing, fibrosis, and in many cancers (e.g., pancreatic, colon, lung, oral squamous cell carcinoma) where its expression often correlates with poor prognosis and increased invasiveness [2]. Associated diseases include various forms of cancer, chronic organ fibrosis (such as pulmonary fibrosis), and rare genetic conditions like Amelogenesis Imperfecta and a syndrome characterized by alopecia and intellectual disability [3].
hITGB6 mouse is a humanized model generated using gene editing technology, in which the sequence from aa.22 to partial intron 4 was replaced with Human ITGB6 CDS-Mouse Itgb6 CDS-3’UTR of Mouse Itgb6-WPRE-BGH pA cassette. The murine signal peptide was preserved. This model can be used for studying the pathological mechanisms and therapeutic approaches of various forms of cancer, chronic organ fibrosis (such as pulmonary fibrosis), and rare genetic conditions, as well as for the development of ITGB6-targeted drugs.
huHER2(ERBB2)
製品ID :
C001627
系統:
C57BL/6NCya
状況:
説明:
Epidermal growth factor receptor 2 (ERBB2), also known as HER2 or Neu protein, encoded by the ERBB2 gene, is a member of the ErbB receptor tyrosine kinase family. ERBB2 gene expression is subject to complex regulation, influenced by diverse transcription factors and signaling pathways, and is normally expressed at low levels in various epithelial tissues, including the breast, ovary, and gastrointestinal tract [1]. HER2, a transmembrane receptor tyrosine kinase, functions at the cell surface, primarily through heterodimerization with other epidermal growth factor receptor family members, such as HER3. This activation initiates downstream signaling pathways, including PI3K/Akt and MAPK, which regulate cell growth, proliferation, differentiation, and migration [1]. In tumor tissues, ERBB2 gene amplification or overexpression is frequently observed, particularly in solid tumors such as breast, gastric, and ovarian cancers. Elevated HER2 expression is strongly associated with tumorigenesis, progression, invasion, metastasis, and poor patient prognosis, establishing it as a key prognostic marker and therapeutic target in breast and other cancers [2-4]. Targeted therapies against HER2, including monoclonal antibodies such as trastuzumab and pertuzumab, and small molecule tyrosine kinase inhibitors, have become essential treatments for patients with HER2-positive breast cancer and other malignancies [4].
The huHER2(ERBB2) mouse is a humanized model constructed using gene editing technology, where the mouse HER2 extracellular domain was replaced with the human HER2 extracellular domain. Homozygous huHER2(ERBB2) mice are viable and fertile. This model can be used for studying the pathological mechanisms and therapeutic approaches of related cancers, and for the development of HER2-targeted drugs.
Epidermal growth factor receptor 2 (ERBB2), also known as HER2 or Neu protein, encoded by the ERBB2 gene, is a member of the ErbB receptor tyrosine kinase family. ERBB2 gene expression is subject to complex regulation, influenced by diverse transcription factors and signaling pathways, and is normally expressed at low levels in various epithelial tissues, including the breast, ovary, and gastrointestinal tract [1]. HER2, a transmembrane receptor tyrosine kinase, functions at the cell surface, primarily through heterodimerization with other epidermal growth factor receptor family members, such as HER3. This activation initiates downstream signaling pathways, including PI3K/Akt and MAPK, which regulate cell growth, proliferation, differentiation, and migration [1]. In tumor tissues, ERBB2 gene amplification or overexpression is frequently observed, particularly in solid tumors such as breast, gastric, and ovarian cancers. Elevated HER2 expression is strongly associated with tumorigenesis, progression, invasion, metastasis, and poor patient prognosis, establishing it as a key prognostic marker and therapeutic target in breast and other cancers [2-4]. Targeted therapies against HER2, including monoclonal antibodies such as trastuzumab and pertuzumab, and small molecule tyrosine kinase inhibitors, have become essential treatments for patients with HER2-positive breast cancer and other malignancies [4].
The huHER2(ERBB2) mouse is a humanized model constructed using gene editing technology, where the mouse HER2 extracellular domain was replaced with the human HER2 extracellular domain. Homozygous huHER2(ERBB2) mice are viable and fertile. This model can be used for studying the pathological mechanisms and therapeutic approaches of related cancers, and for the development of HER2-targeted drugs.
huIL4RA
製品ID :
C001629
系統:
C57BL/6NCya
状況:
説明:
Interleukin-4 (IL-4) and its receptor, IL-4R, are pivotal regulators of immune responses and inflammation. The IL4 gene encodes the IL-4 cytokine, a multifunctional protein predominantly secreted by Th2 cells, mast cells, and eosinophils, while the IL4R gene encodes the IL-4 receptor, which is expressed on a variety of immune cells, including B cells, T cells, macrophages, and endothelial cells. IL-4 binds to IL-4R, which exists in two distinct forms: Type I (comprising IL-4Rα and the common γ-chain) and Type II (comprising IL-4Rα and IL-13Rα1) [1]. This interaction activates the JAK-STAT signaling pathway, driving Th2 cell differentiation, B cell class switching to IgE, and anti-inflammatory responses. The IL-4/IL-4R signaling axis is critically implicated in allergic diseases such as asthma, atopic dermatitis, and allergic rhinitis, as well as in parasitic infections and certain cancers [2-5]. Dysregulation of this pathway underlies various pathological conditions, positioning IL-4R as a promising therapeutic target. For instance, dupilumab, a monoclonal antibody targeting IL-4Rα, has been approved for the treatment of atopic dermatitis, asthma, and chronic rhinosinusitis with nasal polyps, underscoring the therapeutic potential of modulating this pathway [6-7].
huIL4RA mice are humanized models generated using gene editing technology by replacing the extracellular domain of the mouse Il4ra with the corresponding human IL4R extracellular domain, while retaining the murine signal peptide. Homozygous huIL4RA mice are viable and fertile. This model is an invaluable tool for studying allergic diseases (e.g., asthma and atopic dermatitis), Th2 immune responses, parasitic infections, tumor immunology, and chronic inflammation. Furthermore, it is a robust preclinical platform for evaluating the efficacy and mechanisms of therapeutic agents targeting the IL-4Rα.
Interleukin-4 (IL-4) and its receptor, IL-4R, are pivotal regulators of immune responses and inflammation. The IL4 gene encodes the IL-4 cytokine, a multifunctional protein predominantly secreted by Th2 cells, mast cells, and eosinophils, while the IL4R gene encodes the IL-4 receptor, which is expressed on a variety of immune cells, including B cells, T cells, macrophages, and endothelial cells. IL-4 binds to IL-4R, which exists in two distinct forms: Type I (comprising IL-4Rα and the common γ-chain) and Type II (comprising IL-4Rα and IL-13Rα1) [1]. This interaction activates the JAK-STAT signaling pathway, driving Th2 cell differentiation, B cell class switching to IgE, and anti-inflammatory responses. The IL-4/IL-4R signaling axis is critically implicated in allergic diseases such as asthma, atopic dermatitis, and allergic rhinitis, as well as in parasitic infections and certain cancers [2-5]. Dysregulation of this pathway underlies various pathological conditions, positioning IL-4R as a promising therapeutic target. For instance, dupilumab, a monoclonal antibody targeting IL-4Rα, has been approved for the treatment of atopic dermatitis, asthma, and chronic rhinosinusitis with nasal polyps, underscoring the therapeutic potential of modulating this pathway [6-7].
huIL4RA mice are humanized models generated using gene editing technology by replacing the extracellular domain of the mouse Il4ra with the corresponding human IL4R extracellular domain, while retaining the murine signal peptide. Homozygous huIL4RA mice are viable and fertile. This model is an invaluable tool for studying allergic diseases (e.g., asthma and atopic dermatitis), Th2 immune responses, parasitic infections, tumor immunology, and chronic inflammation. Furthermore, it is a robust preclinical platform for evaluating the efficacy and mechanisms of therapeutic agents targeting the IL-4Rα.
hEGFR
製品ID :
C001782
系統:
C57BL/6NCya
状況:
説明:
The Epidermal Growth Factor Receptor (EGFR) gene (also known as ERBB1 or HER1) encodes a transmembrane glycoprotein that belongs to the protein kinase superfamily. It is widely expressed in various cellular tissues, including epithelial and mesenchymal cells, bone cells, blood and immune cells, heart cells, glia, and stem neural cells, and is particularly abundant in the placenta [1]. Its primary function is to act as a receptor for members of the epidermal growth factor family, such as EGF and TGF-alpha. Upon ligand binding, EGFR undergoes dimerization and tyrosine autophosphorylation, initiating crucial downstream signaling pathways (like RAS-RAF-MEK-ERK and PI3 kinase-AKT) that regulate essential cellular processes including proliferation, survival, differentiation, and migration [2]. Aberrant gene expression, particularly overexpression, amplification, or activating mutations in EGFR, leads to its constitutive activation, promoting uncontrolled cell growth and survival [3]. This dysregulation is a significant factor in the development and progression of numerous cancers, most notably non-small cell lung cancer (especially adenocarcinoma), glioblastoma, colorectal carcinoma, and breast carcinoma, making EGFR a key target for personalized cancer therapies [4].
The hEGFR mouse is a humanized model constructed by replacing exon 2 and part of intron 2 of the mouse Egfr gene with the EGFR Chimeric cDNA-WPRE BGH pA cassette. The murine signal peptide and partial extracellular domain are preserved. hEGFR mice can be used for research into the pathogenesis of various cancers, including non-small cell lung cancer (adenocarcinoma), glioblastoma, colorectal cancer, and breast cancer, as well as for the screening, development, and safety assessment of EGFR-targeted therapies.
The Epidermal Growth Factor Receptor (EGFR) gene (also known as ERBB1 or HER1) encodes a transmembrane glycoprotein that belongs to the protein kinase superfamily. It is widely expressed in various cellular tissues, including epithelial and mesenchymal cells, bone cells, blood and immune cells, heart cells, glia, and stem neural cells, and is particularly abundant in the placenta [1]. Its primary function is to act as a receptor for members of the epidermal growth factor family, such as EGF and TGF-alpha. Upon ligand binding, EGFR undergoes dimerization and tyrosine autophosphorylation, initiating crucial downstream signaling pathways (like RAS-RAF-MEK-ERK and PI3 kinase-AKT) that regulate essential cellular processes including proliferation, survival, differentiation, and migration [2]. Aberrant gene expression, particularly overexpression, amplification, or activating mutations in EGFR, leads to its constitutive activation, promoting uncontrolled cell growth and survival [3]. This dysregulation is a significant factor in the development and progression of numerous cancers, most notably non-small cell lung cancer (especially adenocarcinoma), glioblastoma, colorectal carcinoma, and breast carcinoma, making EGFR a key target for personalized cancer therapies [4].
The hEGFR mouse is a humanized model constructed by replacing exon 2 and part of intron 2 of the mouse Egfr gene with the EGFR Chimeric cDNA-WPRE BGH pA cassette. The murine signal peptide and partial extracellular domain are preserved. hEGFR mice can be used for research into the pathogenesis of various cancers, including non-small cell lung cancer (adenocarcinoma), glioblastoma, colorectal cancer, and breast cancer, as well as for the screening, development, and safety assessment of EGFR-targeted therapies.
huANGPTL4(2)
製品ID :
C002113
系統:
C57BL/6Cya
状況:
説明:
Angiopoietin-like protein 4 (ANGPTL4) is a member of the angiopoietin-like protein family and is highly expressed in metabolically active organs and tissues, such as the liver, adipose tissue, and small intestine [1]. As a physiological inhibitor of lipoprotein lipase (LPL), ANGPTL4 non-covalently binds to and inhibits LPL activity primarily through its N-terminal domain, thereby blocking the peripheral hydrolysis and clearance of triglyceride-rich lipoproteins (e.g., chylomicrons and very-low-density lipoprotein remnants) and participating in the regulation of systemic lipid metabolism and triglyceride homeostasis [2]. Studies have demonstrated that the dysfunction of ANGPTL4 is closely associated with obesity, type 2 diabetes (T2D), hypertriglyceridemia, atherosclerotic cardiovascular disease (ASCVD), metabolic dysfunction-associated steatotic liver disease (MASLD), and microenvironmental remodeling in malignancies such as triple-negative breast cancer, making it an important drug discovery target in metabolic disorders, cardiovascular diseases, and oncology translational medicine [2-5].
The huANGPTL4(2) mouse is a humanized model developed via gene editing technology, in which the sequences from the start codon to the 3'UTR of the endogenous mouse Angptl4 gene were replaced with the sequences from the start codon to the 3'UTR of the human ANGPTL4 gene. This model is applicable to the study of pathological mechanisms of diseases such as organ fibrosis, related malignancies, and hypertriglyceridemia, as well as to the screening, development, and preclinical in vivo evaluation of drugs targeting human ANGPTL4, including antibodies, nucleic acid drugs (such as siRNA and antisense oligonucleotides, ASO), and small molecule inhibitors.
Angiopoietin-like protein 4 (ANGPTL4) is a member of the angiopoietin-like protein family and is highly expressed in metabolically active organs and tissues, such as the liver, adipose tissue, and small intestine [1]. As a physiological inhibitor of lipoprotein lipase (LPL), ANGPTL4 non-covalently binds to and inhibits LPL activity primarily through its N-terminal domain, thereby blocking the peripheral hydrolysis and clearance of triglyceride-rich lipoproteins (e.g., chylomicrons and very-low-density lipoprotein remnants) and participating in the regulation of systemic lipid metabolism and triglyceride homeostasis [2]. Studies have demonstrated that the dysfunction of ANGPTL4 is closely associated with obesity, type 2 diabetes (T2D), hypertriglyceridemia, atherosclerotic cardiovascular disease (ASCVD), metabolic dysfunction-associated steatotic liver disease (MASLD), and microenvironmental remodeling in malignancies such as triple-negative breast cancer, making it an important drug discovery target in metabolic disorders, cardiovascular diseases, and oncology translational medicine [2-5].
The huANGPTL4(2) mouse is a humanized model developed via gene editing technology, in which the sequences from the start codon to the 3'UTR of the endogenous mouse Angptl4 gene were replaced with the sequences from the start codon to the 3'UTR of the human ANGPTL4 gene. This model is applicable to the study of pathological mechanisms of diseases such as organ fibrosis, related malignancies, and hypertriglyceridemia, as well as to the screening, development, and preclinical in vivo evaluation of drugs targeting human ANGPTL4, including antibodies, nucleic acid drugs (such as siRNA and antisense oligonucleotides, ASO), and small molecule inhibitors.
huIL4/huIL4RA
製品ID :
C001834
系統:
C57BL/6NCya
状況:
説明:
Interleukin-4 (IL-4) and its receptor, IL-4R, are pivotal regulators of immune responses and inflammation. The IL4 gene encodes the IL-4 cytokine, a multifunctional protein predominantly secreted by Th2 cells, mast cells, and eosinophils, while the IL4R gene encodes the IL-4 receptor, which is expressed on a variety of immune cells, including B cells, T cells, macrophages, and endothelial cells. IL-4 binds to IL-4R, which exists in two distinct forms: Type I (comprising IL-4Rα and the common γ-chain) and Type II (comprising IL-4Rα and IL-13Rα1) [1]. This interaction activates the JAK-STAT signaling pathway, driving Th2 cell differentiation, B cell class switching to IgE, and anti-inflammatory responses. The IL-4/IL-4R signaling axis is critically implicated in allergic diseases such as asthma, atopic dermatitis, and allergic rhinitis, as well as in parasitic infections and certain cancers [2-5]. Dysregulation of this pathway underlies various pathological conditions, positioning IL-4Rα as a promising therapeutic target. For instance, dupilumab, a monoclonal antibody targeting IL-4Rα, has been approved for the treatment of atopic dermatitis, asthma, and chronic rhinosinusitis with nasal polyps, underscoring the therapeutic potential of modulating this pathway [6-7].
The huIL4/huIL4RA mouse model is generated by crossing IL4 humanized mice (Catalog Number: C001628) with IL4R humanized mice (Catalog Number: C001629), resulting in a dual-humanized model. This model faithfully recapitulates the human IL-4/IL-4R signaling pathway, making it an invaluable tool for studying allergic diseases (e.g., asthma and atopic dermatitis), Th2 immune responses, parasitic infections, tumor immunology, and chronic inflammation. Furthermore, it serves as a robust preclinical platform for evaluating the efficacy and mechanisms of therapeutic agents targeting the IL-4/IL-4Rα pathway.
Interleukin-4 (IL-4) and its receptor, IL-4R, are pivotal regulators of immune responses and inflammation. The IL4 gene encodes the IL-4 cytokine, a multifunctional protein predominantly secreted by Th2 cells, mast cells, and eosinophils, while the IL4R gene encodes the IL-4 receptor, which is expressed on a variety of immune cells, including B cells, T cells, macrophages, and endothelial cells. IL-4 binds to IL-4R, which exists in two distinct forms: Type I (comprising IL-4Rα and the common γ-chain) and Type II (comprising IL-4Rα and IL-13Rα1) [1]. This interaction activates the JAK-STAT signaling pathway, driving Th2 cell differentiation, B cell class switching to IgE, and anti-inflammatory responses. The IL-4/IL-4R signaling axis is critically implicated in allergic diseases such as asthma, atopic dermatitis, and allergic rhinitis, as well as in parasitic infections and certain cancers [2-5]. Dysregulation of this pathway underlies various pathological conditions, positioning IL-4Rα as a promising therapeutic target. For instance, dupilumab, a monoclonal antibody targeting IL-4Rα, has been approved for the treatment of atopic dermatitis, asthma, and chronic rhinosinusitis with nasal polyps, underscoring the therapeutic potential of modulating this pathway [6-7].
The huIL4/huIL4RA mouse model is generated by crossing IL4 humanized mice (Catalog Number: C001628) with IL4R humanized mice (Catalog Number: C001629), resulting in a dual-humanized model. This model faithfully recapitulates the human IL-4/IL-4R signaling pathway, making it an invaluable tool for studying allergic diseases (e.g., asthma and atopic dermatitis), Th2 immune responses, parasitic infections, tumor immunology, and chronic inflammation. Furthermore, it serves as a robust preclinical platform for evaluating the efficacy and mechanisms of therapeutic agents targeting the IL-4/IL-4Rα pathway.
hCRBN(BALB/c)
製品ID :
C001724
系統:
BALB/cAnCya
状況:
説明:
The CRBN gene, located on human chromosome 3, exhibits broad expression across diverse tissues, including the brain, kidney, muscle, and immune cell populations such as monocytes, macrophages, dendritic cells, and B lymphocytes [1]. This gene encodes cereblon, a protein that functions as a key substrate receptor within the CRL4-CRBN E3 ubiquitin ligase complex. This complex mediates the ubiquitination and subsequent proteasomal degradation of specific target proteins, thereby regulating crucial cellular processes encompassing protein homeostasis, ion transport, and AMPK signaling [1-2]. Notably, mutations in CRBN are implicated in autosomal recessive nonsyndromic intellectual disability [2]. Furthermore, Cereblon protein serves as a primary molecular target for targeted protein degradation (TPD/TBD) therapy by specifically modulating the enzymatic activity of the CRL4-CRBN complex and altering its substrate recognition properties, thereby enabling the selective degradation of specific transcription factors. This molecular mechanism has emerged as a critical theoretical foundation for the clinical treatment of malignant hematological diseases, such as multiple myeloma, leading to the development of diverse therapeutic modalities including molecular glues and proteolysis targeting chimeras (PROTACs) [3-5].
hCRBN(BALB/c) mice are humanized models generated by gene editing technology, in which the exon 2 to partial intron 2 of the mouse Crbn gene was replaced in situ with the Exon 2~11 of the coding sequence (CDS) of the human CRBN gene. This model can be used to study the pathological mechanisms and therapeutic methods of autosomal recessive nonsyndromic intellectual disability and multiple myeloma, and other hematological cancers, as well as the screening, development, and preclinical efficacy and safety evaluation of CRBN-based targeted protein degradation (TPD) therapies.
The CRBN gene, located on human chromosome 3, exhibits broad expression across diverse tissues, including the brain, kidney, muscle, and immune cell populations such as monocytes, macrophages, dendritic cells, and B lymphocytes [1]. This gene encodes cereblon, a protein that functions as a key substrate receptor within the CRL4-CRBN E3 ubiquitin ligase complex. This complex mediates the ubiquitination and subsequent proteasomal degradation of specific target proteins, thereby regulating crucial cellular processes encompassing protein homeostasis, ion transport, and AMPK signaling [1-2]. Notably, mutations in CRBN are implicated in autosomal recessive nonsyndromic intellectual disability [2]. Furthermore, Cereblon protein serves as a primary molecular target for targeted protein degradation (TPD/TBD) therapy by specifically modulating the enzymatic activity of the CRL4-CRBN complex and altering its substrate recognition properties, thereby enabling the selective degradation of specific transcription factors. This molecular mechanism has emerged as a critical theoretical foundation for the clinical treatment of malignant hematological diseases, such as multiple myeloma, leading to the development of diverse therapeutic modalities including molecular glues and proteolysis targeting chimeras (PROTACs) [3-5].
hCRBN(BALB/c) mice are humanized models generated by gene editing technology, in which the exon 2 to partial intron 2 of the mouse Crbn gene was replaced in situ with the Exon 2~11 of the coding sequence (CDS) of the human CRBN gene. This model can be used to study the pathological mechanisms and therapeutic methods of autosomal recessive nonsyndromic intellectual disability and multiple myeloma, and other hematological cancers, as well as the screening, development, and preclinical efficacy and safety evaluation of CRBN-based targeted protein degradation (TPD) therapies.
huRANKL(TNFSF11)
製品ID :
C002107
系統:
C57BL/6Cya
状況:
説明:
The TNFSF11 gene (also known as receptor activator of nuclear factor‑κB ligand, RANKL) encodes a key member of the tumor necrosis factor superfamily. Its expression is broadly distributed across multiple cell types within the bone microenvironment and the immune system, including osteoblasts, osteocytes, bone marrow stromal cells, activated T cells, and certain B cells [1]. The cytokine encoded by this gene exerts its effects by specifically binding to the signaling receptor TNFRSF11A/RANK and the decoy receptor TNFRSF11B/OPG, thereby regulating core biological processes, such as osteoclast differentiation, activation, and bone remodeling, while also participating in lymph node organogenesis, T‑cell–dendritic cell interactions, and mammary gland development [2]. TNFSF11 plays a central role in both bone homeostasis and adaptive immunity: on one hand, it serves as a critical inducer of osteoclast differentiation and activation, mediating bone resorption and calcium–phosphate metabolism [3]; on the other hand, it provides survival and functional signals to immune cells and promotes osteo‑immune crosstalk under inflammatory conditions [4]. Dysregulation of TNFSF11 expression or signaling has been causally linked to multiple human diseases. Loss‑of‑function mutations impair osteoclastogenesis, leading to autosomal recessive osteopetrosis, whereas hyperactivation or aberrant expression of TNFSF11 signaling promotes pathological bone resorption and contributes to conditions such as osteoporosis, rheumatoid arthritis-associated bone erosion, and tumor bone metastasis, including breast and prostate cancer [5-8].
The huRANKL(TNFSF11) mouse is a humanized model constructed via gene-editing technology. The mouse Tnfsf11 endogenous extracellular domain was replaced with the human TNFSF11 extracellular domain. This model can be used for the mechanistic studies of various bone metabolism- and bone immunity-related diseases, including osteoporosis, bone erosion in rheumatoid arthritis, osteopetrosis, and tumor bone metastasis, as well as for the screening, development, and preclinical in vivo evaluation of TNFSF11-targeting antibodies, small molecule inhibitors, and other therapeutic agents.
The TNFSF11 gene (also known as receptor activator of nuclear factor‑κB ligand, RANKL) encodes a key member of the tumor necrosis factor superfamily. Its expression is broadly distributed across multiple cell types within the bone microenvironment and the immune system, including osteoblasts, osteocytes, bone marrow stromal cells, activated T cells, and certain B cells [1]. The cytokine encoded by this gene exerts its effects by specifically binding to the signaling receptor TNFRSF11A/RANK and the decoy receptor TNFRSF11B/OPG, thereby regulating core biological processes, such as osteoclast differentiation, activation, and bone remodeling, while also participating in lymph node organogenesis, T‑cell–dendritic cell interactions, and mammary gland development [2]. TNFSF11 plays a central role in both bone homeostasis and adaptive immunity: on one hand, it serves as a critical inducer of osteoclast differentiation and activation, mediating bone resorption and calcium–phosphate metabolism [3]; on the other hand, it provides survival and functional signals to immune cells and promotes osteo‑immune crosstalk under inflammatory conditions [4]. Dysregulation of TNFSF11 expression or signaling has been causally linked to multiple human diseases. Loss‑of‑function mutations impair osteoclastogenesis, leading to autosomal recessive osteopetrosis, whereas hyperactivation or aberrant expression of TNFSF11 signaling promotes pathological bone resorption and contributes to conditions such as osteoporosis, rheumatoid arthritis-associated bone erosion, and tumor bone metastasis, including breast and prostate cancer [5-8].
The huRANKL(TNFSF11) mouse is a humanized model constructed via gene-editing technology. The mouse Tnfsf11 endogenous extracellular domain was replaced with the human TNFSF11 extracellular domain. This model can be used for the mechanistic studies of various bone metabolism- and bone immunity-related diseases, including osteoporosis, bone erosion in rheumatoid arthritis, osteopetrosis, and tumor bone metastasis, as well as for the screening, development, and preclinical in vivo evaluation of TNFSF11-targeting antibodies, small molecule inhibitors, and other therapeutic agents.
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