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B6-hIL2RA
製品ID :
C001713
系統:
C57BL/6NCya
状況:
説明:
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-hPD-1/hVEGFA
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 B6-hPD-1/hVEGFA mouse is a humanized model obtained by crossbreeding hPD-1 mice (Catalog No. C001524) with B6-hVEGFA 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 B6-hPD-1/hVEGFA mouse is a humanized model obtained by crossbreeding hPD-1 mice (Catalog No. C001524) with B6-hVEGFA 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.
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-hIL23A/hIL12B
製品ID :
C001620
系統:
C57BL/6NCya
状況:
説明:
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 [1-2]. 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 [1-2]. 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 [3]. Also, monoclonal antibodies targeting IL-12B, such as ustekinumab, are clinically utilized for the treatment of moderate to severe psoriasis and Crohn's disease [5]. 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 [1-4].
B6-hIL23A&hIL12B mice are IL12B and IL23A double humanized mouse models obtained by mating IL12B humanized mouse models with IL23A humanized mouse models. They express human IL12B and IL23A genomic sequences under the control of mouse promoters. This model is capable of reproducing human IL-23 cytokines and is a valuable tool for studying immune-related diseases. In addition, this model also provides a powerful preclinical research platform for evaluating the efficacy and mechanism of therapeutic drugs targeting IL-23 cytokines.
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 [1-2]. 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 [1-2]. 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 [3]. Also, monoclonal antibodies targeting IL-12B, such as ustekinumab, are clinically utilized for the treatment of moderate to severe psoriasis and Crohn's disease [5]. 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 [1-4].
B6-hIL23A&hIL12B mice are IL12B and IL23A double humanized mouse models obtained by mating IL12B humanized mouse models with IL23A humanized mouse models. They express human IL12B and IL23A genomic sequences under the control of mouse promoters. This model is capable of reproducing human IL-23 cytokines and is a valuable tool for studying immune-related diseases. In addition, this model also provides a powerful preclinical research platform for evaluating the efficacy and mechanism of therapeutic drugs targeting IL-23 cytokines.
B6-hCXCR2
製品ID :
C001626
系統:
C57BL/6NCya
状況:
説明:
C-X-C motif chemokine receptor 2 (CXCR2), encoded by the CXCR2 gene, is a member of the G protein-coupled receptor family [1]. While predominantly expressed in neutrophils, CXCR2 is also found in diverse tissue cells, including brain, lung, and other immune cell types [1-2]. As a cell surface receptor, CXCR2 binds specific chemokines, such as interleukin-8 (IL-8) and CXCL1, initiating intracellular signaling cascades involving phosphatidylinositol-3 kinase (PI3K), mitogen-activated protein kinase (MAPK), and nuclear factor-κB (NF-κB) pathways [2]. The principal physiological role of CXCR2 is to mediate neutrophil chemotaxis to sites of inflammation, thereby contributing to immune responses and inflammatory processes [3]. Additionally, CXCR2 has been implicated in the development and progression of various cancers, including melanoma, pancreatic, ovarian, breast, and prostate cancers, by regulating tumor cell survival, proliferation, metastasis, and angiogenesis [1-4]. Aberrant CXCR2 expression or function is associated with a range of pathological conditions, encompassing both inflammatory diseases and cancers.
The B6-hCXCR2 mouse is a humanized model constructed using gene editing technology to replace the entire base sequence of the mouse Cxcr2 gene in situ with the corresponding sequence from the human CXCR2 gene. Homozygous B6-hCXCR2 mice are viable and fertile. This model can be used for studying the pathological mechanisms and therapeutic approaches of inflammatory diseases and cancers, and for the development of CXCR2-targeted drugs.
C-X-C motif chemokine receptor 2 (CXCR2), encoded by the CXCR2 gene, is a member of the G protein-coupled receptor family [1]. While predominantly expressed in neutrophils, CXCR2 is also found in diverse tissue cells, including brain, lung, and other immune cell types [1-2]. As a cell surface receptor, CXCR2 binds specific chemokines, such as interleukin-8 (IL-8) and CXCL1, initiating intracellular signaling cascades involving phosphatidylinositol-3 kinase (PI3K), mitogen-activated protein kinase (MAPK), and nuclear factor-κB (NF-κB) pathways [2]. The principal physiological role of CXCR2 is to mediate neutrophil chemotaxis to sites of inflammation, thereby contributing to immune responses and inflammatory processes [3]. Additionally, CXCR2 has been implicated in the development and progression of various cancers, including melanoma, pancreatic, ovarian, breast, and prostate cancers, by regulating tumor cell survival, proliferation, metastasis, and angiogenesis [1-4]. Aberrant CXCR2 expression or function is associated with a range of pathological conditions, encompassing both inflammatory diseases and cancers.
The B6-hCXCR2 mouse is a humanized model constructed using gene editing technology to replace the entire base sequence of the mouse Cxcr2 gene in situ with the corresponding sequence from the human CXCR2 gene. Homozygous B6-hCXCR2 mice are viable and fertile. This model can be used for studying the pathological mechanisms and therapeutic approaches of inflammatory diseases and cancers, and for the development of CXCR2-targeted drugs.
B6-huMSLN
製品ID :
C001856
系統:
C57BL/6NCya
状況:
説明:
The MSLN gene encodes a preproprotein that is proteolytically processed into two distinct proteins: megakaryocyte potentiating factor (MPF) and mesothelin [1]. MPF functions as a cytokine that promotes the formation of megakaryocytes in bone marrow, while mesothelin is a glycosylphosphatidylinositol-anchored cell-surface protein that may play a role in cell adhesion. While mesothelin expression is normally low and restricted to mesothelial cells lining the pleura, peritoneum, and pericardium, it is highly overexpressed in several epithelial cancers, including malignant mesothelioma, ovarian cancer, pancreatic cancer, and certain types of lung cancer [2-3]. This high expression and its function in promoting cell proliferation and metastasis make mesothelin a significant biomarker and a target for cancer therapies [4].
The B6-huMSLN mouse model was generated by replacing sequences from the ATG start codon to the TGA stop codon of the endogenous mouse Msln gene with the sequences from the ATG start codon to the TGA stop codon of the human MSLN gene. This model can be used to study the pathological mechanisms and therapeutic approaches for several cancers, including malignant mesothelioma, ovarian cancer, pancreatic cancer, and certain types of lung cancer, as well as for the development of MSLN-targeted drugs.
The MSLN gene encodes a preproprotein that is proteolytically processed into two distinct proteins: megakaryocyte potentiating factor (MPF) and mesothelin [1]. MPF functions as a cytokine that promotes the formation of megakaryocytes in bone marrow, while mesothelin is a glycosylphosphatidylinositol-anchored cell-surface protein that may play a role in cell adhesion. While mesothelin expression is normally low and restricted to mesothelial cells lining the pleura, peritoneum, and pericardium, it is highly overexpressed in several epithelial cancers, including malignant mesothelioma, ovarian cancer, pancreatic cancer, and certain types of lung cancer [2-3]. This high expression and its function in promoting cell proliferation and metastasis make mesothelin a significant biomarker and a target for cancer therapies [4].
The B6-huMSLN mouse model was generated by replacing sequences from the ATG start codon to the TGA stop codon of the endogenous mouse Msln gene with the sequences from the ATG start codon to the TGA stop codon of the human MSLN gene. This model can be used to study the pathological mechanisms and therapeutic approaches for several cancers, including malignant mesothelioma, ovarian cancer, pancreatic cancer, and certain types of lung cancer, as well as for the development of MSLN-targeted drugs.
B6-hPD-1/hPD-L1
製品ID :
I001202
系統:
C57BL/6Cya
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].
Programmed cell death 1 ligand 1 (PD-L1), also known as cluster of differentiation 274 (CD274) or B7 homolog 1 (B7H1), is an immune inhibitory receptor ligand. PD-L1 is a type I transmembrane protein with immunoglobulin V-like (IgV) and C-like (IgC) structural domains and is expressed by hematopoietic and non-hematopoietic cells, including T cells, B cells, and various types of tumor cells [2]. PD-L1 can bind to the PD-1 on the surface of CD8+ T cells, inhibiting the activity of CD8+ T cells. This interaction can prevent the immune system from damaging normal tissues, but it can also be used by tumor cells to escape immune surveillance. Monoclonal antibodies that competitively bind to PD-L1 can relieve the immune function inhibition mediated by the binding of PD-1 and PD-L1. This can reactivate CD8+ T cells, triggering the human body's anti-tumor immune response [3]. Therefore, developing of antibody drugs targeting PD-1 and PD-L1 is a hot area in tumor immunotherapy [3-5].
B6-hPD-1/hPDL1 mice are PD-1 and CD274 double humanized mouse models obtained by mating PD-1 humanized mouse models with CD274 humanized mouse models. They express human PD-1 and CD274 genomic sequences under the control of mouse promoters. This model is a valuable tool for studying cancer immunotherapy. In addition, this model also provides a powerful preclinical research platform for evaluating the efficacy and mechanism of therapeutic drugs targeting PD-1 and PD-L1.
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].
Programmed cell death 1 ligand 1 (PD-L1), also known as cluster of differentiation 274 (CD274) or B7 homolog 1 (B7H1), is an immune inhibitory receptor ligand. PD-L1 is a type I transmembrane protein with immunoglobulin V-like (IgV) and C-like (IgC) structural domains and is expressed by hematopoietic and non-hematopoietic cells, including T cells, B cells, and various types of tumor cells [2]. PD-L1 can bind to the PD-1 on the surface of CD8+ T cells, inhibiting the activity of CD8+ T cells. This interaction can prevent the immune system from damaging normal tissues, but it can also be used by tumor cells to escape immune surveillance. Monoclonal antibodies that competitively bind to PD-L1 can relieve the immune function inhibition mediated by the binding of PD-1 and PD-L1. This can reactivate CD8+ T cells, triggering the human body's anti-tumor immune response [3]. Therefore, developing of antibody drugs targeting PD-1 and PD-L1 is a hot area in tumor immunotherapy [3-5].
B6-hPD-1/hPDL1 mice are PD-1 and CD274 double humanized mouse models obtained by mating PD-1 humanized mouse models with CD274 humanized mouse models. They express human PD-1 and CD274 genomic sequences under the control of mouse promoters. This model is a valuable tool for studying cancer immunotherapy. In addition, this model also provides a powerful preclinical research platform for evaluating the efficacy and mechanism of therapeutic drugs targeting PD-1 and PD-L1.
B6-hPD-1/hPD-L1/hVEGFA
製品ID :
C001838
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].
Programmed cell death 1 ligand 1 (PD-L1), also known as cluster of differentiation 274 (CD274) or B7 homolog 1 (B7H1), is an immune inhibitory receptor ligand. PD-L1 is a type I transmembrane protein with immunoglobulin V-like (IgV) and C-like (IgC) structural domains and is expressed by hematopoietic and non-hematopoietic cells, including T cells, B cells, and various types of tumor cells [2]. PD-L1 can bind to the PD-1 on the surface of CD8+ T cells, inhibiting the activity of CD8+ T cells. This interaction can prevent the immune system from damaging normal tissues, but it can also be used by tumor cells to escape immune surveillance. Monoclonal antibodies that competitively bind to PD-L1 can relieve the immune function inhibition mediated by the binding of PD-1 and PD-L1. This can reactivate CD8+ T cells, triggering the human body's anti-tumor immune response [3]. Therefore, development of antibody drugs targeting PD-1 and PD-L1 is a hot area in tumor immunotherapy [3-5].
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 [6]. 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 [7]. 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 [7-8]. 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, thereby inhibiting tumor growth [9]. Thus, VEGFA is an important target for anti-angiogenic cancer therapies.
B6-hPD-1/hPD-L1/hVEGFA mouse is a triple-gene humanized model generated by crossing B6-hPD-1/hPD-L1 mice (Catalog No.: I001202) with B6-hVEGFA mice (Catalog No.: C001555). This model serves as a valuable tool for research on cancer immunotherapy and can also be used for the screening, development, and preclinical evaluation of PD-1/PD-L1/VEGFA-targeted drugs.
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].
Programmed cell death 1 ligand 1 (PD-L1), also known as cluster of differentiation 274 (CD274) or B7 homolog 1 (B7H1), is an immune inhibitory receptor ligand. PD-L1 is a type I transmembrane protein with immunoglobulin V-like (IgV) and C-like (IgC) structural domains and is expressed by hematopoietic and non-hematopoietic cells, including T cells, B cells, and various types of tumor cells [2]. PD-L1 can bind to the PD-1 on the surface of CD8+ T cells, inhibiting the activity of CD8+ T cells. This interaction can prevent the immune system from damaging normal tissues, but it can also be used by tumor cells to escape immune surveillance. Monoclonal antibodies that competitively bind to PD-L1 can relieve the immune function inhibition mediated by the binding of PD-1 and PD-L1. This can reactivate CD8+ T cells, triggering the human body's anti-tumor immune response [3]. Therefore, development of antibody drugs targeting PD-1 and PD-L1 is a hot area in tumor immunotherapy [3-5].
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 [6]. 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 [7]. 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 [7-8]. 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, thereby inhibiting tumor growth [9]. Thus, VEGFA is an important target for anti-angiogenic cancer therapies.
B6-hPD-1/hPD-L1/hVEGFA mouse is a triple-gene humanized model generated by crossing B6-hPD-1/hPD-L1 mice (Catalog No.: I001202) with B6-hVEGFA mice (Catalog No.: C001555). This model serves as a valuable tool for research on cancer immunotherapy and can also be used for the screening, development, and preclinical evaluation of PD-1/PD-L1/VEGFA-targeted drugs.
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.
B6-huOSM/hOSMR
製品ID :
C001901
系統:
C57BL/6NCya
状況:
説明:
The B6-huOSM/hOSMR mouse is a dual-gene humanized model obtained by crossing B6-huOSM mice (catalog No.: C001815) with B6-hOSMR mice (catalog No.: C001841). This model can be used for studying the pathogenesis of inflammatory diseases (such as rheumatoid arthritis, osteoarthritis, and inflammatory bowel disease), cancers (cervical squamous cell carcinoma, lung adenocarcinoma, and pancreatic cancer), pulmonary and skin diseases (such as asthma and psoriasis), cardiovascular diseases (such as atherosclerosis), liver diseases (such as fibrosis), and hematopoietic system and bone marrow-related diseases, as well as for the development of OSM/OSMR-targeted drugs.
The B6-huOSM/hOSMR mouse is a dual-gene humanized model obtained by crossing B6-huOSM mice (catalog No.: C001815) with B6-hOSMR mice (catalog No.: C001841). This model can be used for studying the pathogenesis of inflammatory diseases (such as rheumatoid arthritis, osteoarthritis, and inflammatory bowel disease), cancers (cervical squamous cell carcinoma, lung adenocarcinoma, and pancreatic cancer), pulmonary and skin diseases (such as asthma and psoriasis), cardiovascular diseases (such as atherosclerosis), liver diseases (such as fibrosis), and hematopoietic system and bone marrow-related diseases, as well as for the development of OSM/OSMR-targeted drugs.
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