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Alb-cre+/MYC+
製品ID :
C001339
系統:
C57BL/6JCya
状況:
説明:
The MYC oncogene family comprises regulatory genes and proto-oncogenes that encode transcription factors, involved in various cellular processes such as the cell cycle, apoptosis, DNA repair, and metabolism. Members include c-Myc (MYC), l-Myc (MYCL), and n-Myc (MYCN). c-Myc (MYC) is a basic helix-loop-helix leucine zipper (bHLHZip) transcription factor, which forms heterodimers with Max protein to bind DNA and regulate the expression of approximately 15% of genes, thereby participating in key cellular processes such as cell proliferation, apoptosis, DNA repair, and metabolism. In many cancers, c-Myc is overexpressed, leading to uncontrolled cell proliferation and tumor growth, such as in Burkitt's lymphoma where c-Myc gene rearrangement is common. Dysregulation of the MYC oncogene plays a crucial role in tumorigenesis, predominantly through transcriptional dysregulation resulting in overexpression of c-Myc protein.
Alb-Cre+/MYC+ mice are generated by crossing H11-CAG-LSL-hMYC-IRES-EGFP mice (Catalog Number: C001338), which conditionally express the human c-Myc oncogene, with Alb-Cre mice that express Cre recombinase specifically in hepatocytes under the control of the Alb promoter. The Cre-mediated recombination results in the deletion of the transcriptional stop sequence (Loxp-Stop-Loxp, LSL) in H11-CAG-LSL-hMYC-IRES-EGFP mice, leading to overexpression of the MYC oncogene in the liver and subsequent carcinogenesis. This model, therefore, spontaneously develops liver cancer with an early onset.
The MYC oncogene family comprises regulatory genes and proto-oncogenes that encode transcription factors, involved in various cellular processes such as the cell cycle, apoptosis, DNA repair, and metabolism. Members include c-Myc (MYC), l-Myc (MYCL), and n-Myc (MYCN). c-Myc (MYC) is a basic helix-loop-helix leucine zipper (bHLHZip) transcription factor, which forms heterodimers with Max protein to bind DNA and regulate the expression of approximately 15% of genes, thereby participating in key cellular processes such as cell proliferation, apoptosis, DNA repair, and metabolism. In many cancers, c-Myc is overexpressed, leading to uncontrolled cell proliferation and tumor growth, such as in Burkitt's lymphoma where c-Myc gene rearrangement is common. Dysregulation of the MYC oncogene plays a crucial role in tumorigenesis, predominantly through transcriptional dysregulation resulting in overexpression of c-Myc protein.
Alb-Cre+/MYC+ mice are generated by crossing H11-CAG-LSL-hMYC-IRES-EGFP mice (Catalog Number: C001338), which conditionally express the human c-Myc oncogene, with Alb-Cre mice that express Cre recombinase specifically in hepatocytes under the control of the Alb promoter. The Cre-mediated recombination results in the deletion of the transcriptional stop sequence (Loxp-Stop-Loxp, LSL) in H11-CAG-LSL-hMYC-IRES-EGFP mice, leading to overexpression of the MYC oncogene in the liver and subsequent carcinogenesis. This model, therefore, spontaneously develops liver cancer with an early onset.
BALB/c-hCD3
製品ID :
C001326
系統:
BALB/cAnCya
状況:
説明:
Cluster of differentiation 3 (CD3) is a multimeric protein complex that is essential for T cell activation and antigen recognition. It consists of five different polypeptide chains (γ, δ, ε, ζ, and η) that are noncovalently associated with the T cell receptor (TCR). The TCR is responsible for recognizing antigens presented by antigen-presenting cells (APCs), while CD3 transduces the activation signal into the T cell and activates helper T-cells and cytotoxic T-cells [1-2]. The CD3-TCR complex is expressed on the surface of all mature T cells, and its assembly is required for T cell development and function. CD3 plays a crucial role in stabilizing the TCR and facilitating its interaction with antigens. It also recruits signaling molecules to the TCR, which initiates a cascade of events that leads to T cell activation. CD3 is a highly specific T cell marker, and its expression is increased upon T cell activation. This makes it a valuable tool for identifying and characterizing T cells in tissues and blood samples. CD3 staining is also used to diagnose T-cell lymphomas and leukemias. Due to its essential role in T cell activation, CD3 is a promising target for immunosuppressive therapy. Several anti-CD3 monoclonal antibodies have been developed and are being tested in clinical trials for the treatment of autoimmune diseases, such as type 1 diabetes and rheumatoid arthritis [3].
The BALB/c-hCD3 mice are a CD3 humanized model obtained by replacing the mouse CD3 coding gene with the human CD3 gene using embryonic stem (ES) cell targeting technology. This model can be used to study T cell activation and antigen recognition mechanisms and for the development of CD3-targeted drugs in immunosuppressive therapies for autoimmune diseases.
Cluster of differentiation 3 (CD3) is a multimeric protein complex that is essential for T cell activation and antigen recognition. It consists of five different polypeptide chains (γ, δ, ε, ζ, and η) that are noncovalently associated with the T cell receptor (TCR). The TCR is responsible for recognizing antigens presented by antigen-presenting cells (APCs), while CD3 transduces the activation signal into the T cell and activates helper T-cells and cytotoxic T-cells [1-2]. The CD3-TCR complex is expressed on the surface of all mature T cells, and its assembly is required for T cell development and function. CD3 plays a crucial role in stabilizing the TCR and facilitating its interaction with antigens. It also recruits signaling molecules to the TCR, which initiates a cascade of events that leads to T cell activation. CD3 is a highly specific T cell marker, and its expression is increased upon T cell activation. This makes it a valuable tool for identifying and characterizing T cells in tissues and blood samples. CD3 staining is also used to diagnose T-cell lymphomas and leukemias. Due to its essential role in T cell activation, CD3 is a promising target for immunosuppressive therapy. Several anti-CD3 monoclonal antibodies have been developed and are being tested in clinical trials for the treatment of autoimmune diseases, such as type 1 diabetes and rheumatoid arthritis [3].
The BALB/c-hCD3 mice are a CD3 humanized model obtained by replacing the mouse CD3 coding gene with the human CD3 gene using embryonic stem (ES) cell targeting technology. This model can be used to study T cell activation and antigen recognition mechanisms and for the development of CD3-targeted drugs in immunosuppressive therapies for autoimmune diseases.
B6-hLPA (CKI) /Alb-cre
製品ID :
C001522
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].
This strain was generated by mating B6-hLPA(CKI) mice (catalog number: C001521) with Alb-Cre mice (liver-specific Cre-expressing mice), resulting in a mouse model with liver-specific overexpression of the human LPA gene. B6-hLPA(CKI)/Alb-cre mice can be used to study the relationship between the LPA gene and hyperlipidemia and related cardiovascular diseases.
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].
This strain was generated by mating B6-hLPA(CKI) mice (catalog number: C001521) with Alb-Cre mice (liver-specific Cre-expressing mice), resulting in a mouse model with liver-specific overexpression of the human LPA gene. B6-hLPA(CKI)/Alb-cre mice can be used to study the relationship between the LPA gene and hyperlipidemia and related cardiovascular diseases.
B6-hLPA (CKI)
製品ID :
C001521
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 contains the lipoprotein ApoB-100. However, unlike LDL, LP(a) 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].
This strain was a conditional mouse model expressing the human LPA gene, where the ‘loxP-Stop-loxP-hLPA’ sequence was inserted into the intron 1 of the ROSA26 safe harbor locus. When this model is bred with tool mice expressing Cre recombinase, sequence recombination occurs in the Cre-positive cells and tissues of the offspring mice. After the Cre-recombinase-mediated deletion of the stop element (LSL), specific expression of the human LPA gene can be achieved. The B6-hLPA(CKI) mice can be used for research related to atherosclerosis, and thrombotic cardiovascular diseases, as well as the development, screening, and preclinical evaluation of human LPA gene-targeted drugs.
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 contains the lipoprotein ApoB-100. However, unlike LDL, LP(a) 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].
This strain was a conditional mouse model expressing the human LPA gene, where the ‘loxP-Stop-loxP-hLPA’ sequence was inserted into the intron 1 of the ROSA26 safe harbor locus. When this model is bred with tool mice expressing Cre recombinase, sequence recombination occurs in the Cre-positive cells and tissues of the offspring mice. After the Cre-recombinase-mediated deletion of the stop element (LSL), specific expression of the human LPA gene can be achieved. The B6-hLPA(CKI) mice can be used for research related to atherosclerosis, and thrombotic cardiovascular diseases, as well as the development, screening, and preclinical evaluation of human LPA gene-targeted drugs.
B6-hCALCA
製品ID :
C001523
系統:
C57BL/6JCya
状況:
説明:
Calcitonin-related polypeptide alpha (CALCA) is a protein-encoded gene, also known as CALC1, CGRP, or CGRP-α. Multiple genetic factors and epigenetic modifications regulate CALCA gene expression, and it forms peptide hormones calcitonin (CT), α-isoform of calcitonin gene-related peptide (CGRP), and katacalcin through tissue-specific RNA alternative splicing and non-active precursor protein cleavage in transcription and translation. Calcitonin is synthesized and secreted by thyroid parafollicular cells, mainly involved in regulating calcium levels and phosphorus metabolism in bones and kidneys. It can reduce the concentration of calcium and phosphorus in the plasma and inhibit the absorption of calcium and phosphorus. CGRP mainly acts as a vasodilator and antimicrobial peptide, which can cause dilatation of coronary arteries, cerebral vessels, and systemic vessels, and help to regulate blood pressure. CGRP is also widely distributed in the pain pathways of the peripheral and central nervous system (CNS) of the human body, and its receptors are also expressed in the pain pathways. CGRP participates in the transmission of pain signals from the periphery to the CNS and plays a key role in pain regulation, which is related to the pathogenesis of a variety of pain diseases and related syndromes, including somatic pain, visceral pain, neuropathic pain, inflammatory pain, and migraine. Katacalcin mainly exists as a peptide that can effectively lower plasma calcium, and its effect of lowering serum calcium levels is almost the same as that of calcitonin. CALCA gene polymorphism is associated with a variety of diseases, including reflex sympathetic dystrophy syndrome, complex regional pain syndrome, ischemic stroke, Parkinson's disease, ovarian cancer, bone mineral density, migraine, schizophrenia, bipolar disorder, and primary hypertension [1-5]. CALCA is a potential target for new therapies for a variety of diseases. Currently, various CALCA antagonists are being developed for the treatment of migraine and primary hypertension, and research on targeting CALCA for diseases such as Alzheimer's disease and Parkinson's disease is also ongoing [6-7].
This strain is a humanized mouse model of the Calca gene. Using gene editing technology, the base sequence of the mouse Calca gene from the start codon to the 3’UTR region was replaced by the corresponding sequence in the human CALCA gene, while the 5’UTR region of the mouse Calca gene was retained. Homozygous B6-hCALCA mice are viable and fertile and can be used to study the mechanisms of various physiological and pathological processes such as blood pressure regulation, cell proliferation, cell apoptosis, vascular biology, physiological bone marrow production, inflammation, tumor growth, and research on CALCA-targeted migraine drugs and therapies.
Calcitonin-related polypeptide alpha (CALCA) is a protein-encoded gene, also known as CALC1, CGRP, or CGRP-α. Multiple genetic factors and epigenetic modifications regulate CALCA gene expression, and it forms peptide hormones calcitonin (CT), α-isoform of calcitonin gene-related peptide (CGRP), and katacalcin through tissue-specific RNA alternative splicing and non-active precursor protein cleavage in transcription and translation. Calcitonin is synthesized and secreted by thyroid parafollicular cells, mainly involved in regulating calcium levels and phosphorus metabolism in bones and kidneys. It can reduce the concentration of calcium and phosphorus in the plasma and inhibit the absorption of calcium and phosphorus. CGRP mainly acts as a vasodilator and antimicrobial peptide, which can cause dilatation of coronary arteries, cerebral vessels, and systemic vessels, and help to regulate blood pressure. CGRP is also widely distributed in the pain pathways of the peripheral and central nervous system (CNS) of the human body, and its receptors are also expressed in the pain pathways. CGRP participates in the transmission of pain signals from the periphery to the CNS and plays a key role in pain regulation, which is related to the pathogenesis of a variety of pain diseases and related syndromes, including somatic pain, visceral pain, neuropathic pain, inflammatory pain, and migraine. Katacalcin mainly exists as a peptide that can effectively lower plasma calcium, and its effect of lowering serum calcium levels is almost the same as that of calcitonin. CALCA gene polymorphism is associated with a variety of diseases, including reflex sympathetic dystrophy syndrome, complex regional pain syndrome, ischemic stroke, Parkinson's disease, ovarian cancer, bone mineral density, migraine, schizophrenia, bipolar disorder, and primary hypertension [1-5]. CALCA is a potential target for new therapies for a variety of diseases. Currently, various CALCA antagonists are being developed for the treatment of migraine and primary hypertension, and research on targeting CALCA for diseases such as Alzheimer's disease and Parkinson's disease is also ongoing [6-7].
This strain is a humanized mouse model of the Calca gene. Using gene editing technology, the base sequence of the mouse Calca gene from the start codon to the 3’UTR region was replaced by the corresponding sequence in the human CALCA gene, while the 5’UTR region of the mouse Calca gene was retained. Homozygous B6-hCALCA mice are viable and fertile and can be used to study the mechanisms of various physiological and pathological processes such as blood pressure regulation, cell proliferation, cell apoptosis, vascular biology, physiological bone marrow production, inflammation, tumor growth, and research on CALCA-targeted migraine drugs and therapies.
B6-hPCSK9/Apoe KO
製品ID :
I001220
系統:
C57BL/6Cya
状況:
説明:
Proprotein convertase subtilisin/kexin 9 (PCSK9) is a serine protease primarily produced in the liver but expressed in other tissues, including the intestine, heart, and neurons. The N-terminal domain of the PCSK9 protein is responsible for protein localization and stability, while the C-terminal domain is responsible for protein enzymatic activity [1]. The Low-density lipoprotein receptor (LDLR) is a receptor that is responsible for clearing low-density lipoprotein cholesterol (LDL-C) from the blood. PCSK9 cleaves the intracellular domain of LDLR on the cell surface, causing it to detach from the cell membrane and be transported to the lysosome for degradation, promoting LDLR degradation, and increasing plasma LDL-C. Overexpression or gain-of-function mutations of the PCSK9 gene can lead to LDL-C accumulation by reducing LDLR levels. This can cause hypercholesterolemia, which increases the risk of cardiovascular diseases, such as atherosclerosis and coronary heart disease, and neurodegenerative diseases, such as Alzheimer's disease [2]. PCSK9 has become an important target for the development of lipid-lowering drugs. Several PCSK9-targeted antibodies or small nucleic acid drugs have been approved for marketing worldwide, including evolocumab from Amgen, alirocumab from Sanofi and Regeneron, and inclisiran from Novartis. These drugs primarily work by inhibiting PCSK9 activity or preventing PCSK9 protein from binding to LDLR, lowering LDL-C levels in the blood to treat hypercholesterolemia [3-4]. In addition, PCSK9 can promote tumor growth and development by regulating cell proliferation, migration, and invasion. It can also regulate the expression of inflammatory factors that contribute to inflammation. Therefore, targeting the expression of PCSK9 has been investigated in tumor immunotherapy and autoimmune disease therapy [5-6].
Apolipoprotein E (ApoE) is a lipid particle-associated polymorphic carrier protein encoded by the APOE gene. It is a core component of plasma lipoproteins, participating in the production, transport, and clearance of lipoproteins. ApoE is associated with chylomicrons, chylomicron remnants, high-density lipoprotein (HDL), very low-density lipoprotein (VLDL), and intermediate-density lipoprotein (IDL), especially showing preferential binding to HDL [7]. ApoE is the most important lipid transport protein in the body, having a profound impact on lipid metabolism. The interaction of ApoE with the low-density lipoprotein receptor (LDLR) is essential for the normal processing (catabolism) of triglyceride-rich lipoproteins [8]. In peripheral tissues, ApoE is primarily produced by the liver and macrophages and mediates cholesterol metabolism. In the central nervous system, ApoE is produced mainly by astrocytes and is the major cholesterol carrier in the brain. ApoE is essential for transporting cholesterol from astrocytes to neurons [7-10]. In addition, ApoE forms a complex with activated C1q, becoming a checkpoint inhibitor target of the classical complement pathway [11]. Polymorphisms of the APOE are associated with Alzheimer's disease and lipid accumulation, hyperlipidemia, atherosclerosis, high cholesterolemia, etc., and are related to the risk of various cardiovascular diseases.
The B6-hPCSK9/Apoe KO mice are obtained by crossing B6-hPCSK9 mice (Catalog No.: C001617) with B6J-Apoe KO mice (Catalog No.: C001507). B6J-Apoe KO mice exhibit elevated cholesterol levels and spontaneous atherosclerosis phenotypes due to the disruption of ApoE protein synthesis, further exacerbated under a high-fat diet (HFD). On the other hand, B6-hPCSK9 mice have the mouse Pcsk9 gene sequence replaced with the human PCSK9 gene sequence through gene editing technology, expressing the human PCSK9 protein. They can be used for the development of PCSK9-targeted drugs in hyperlipidemia, stroke, coronary heart disease, and other atherosclerotic cardiovascular diseases (ASCVD). The B6-hPCSK9/Apoe KO mice, while expressing the human PCSK9 protein, exhibit significantly elevated cholesterol levels and spontaneous atherosclerosis characteristics. These mice provide an ideal platform for the PCSK9-targeted drug development in hyperlipidemia and cardiovascular diseases, demonstrating good clinical and pathological relevance.
Proprotein convertase subtilisin/kexin 9 (PCSK9) is a serine protease primarily produced in the liver but expressed in other tissues, including the intestine, heart, and neurons. The N-terminal domain of the PCSK9 protein is responsible for protein localization and stability, while the C-terminal domain is responsible for protein enzymatic activity [1]. The Low-density lipoprotein receptor (LDLR) is a receptor that is responsible for clearing low-density lipoprotein cholesterol (LDL-C) from the blood. PCSK9 cleaves the intracellular domain of LDLR on the cell surface, causing it to detach from the cell membrane and be transported to the lysosome for degradation, promoting LDLR degradation, and increasing plasma LDL-C. Overexpression or gain-of-function mutations of the PCSK9 gene can lead to LDL-C accumulation by reducing LDLR levels. This can cause hypercholesterolemia, which increases the risk of cardiovascular diseases, such as atherosclerosis and coronary heart disease, and neurodegenerative diseases, such as Alzheimer's disease [2]. PCSK9 has become an important target for the development of lipid-lowering drugs. Several PCSK9-targeted antibodies or small nucleic acid drugs have been approved for marketing worldwide, including evolocumab from Amgen, alirocumab from Sanofi and Regeneron, and inclisiran from Novartis. These drugs primarily work by inhibiting PCSK9 activity or preventing PCSK9 protein from binding to LDLR, lowering LDL-C levels in the blood to treat hypercholesterolemia [3-4]. In addition, PCSK9 can promote tumor growth and development by regulating cell proliferation, migration, and invasion. It can also regulate the expression of inflammatory factors that contribute to inflammation. Therefore, targeting the expression of PCSK9 has been investigated in tumor immunotherapy and autoimmune disease therapy [5-6].
Apolipoprotein E (ApoE) is a lipid particle-associated polymorphic carrier protein encoded by the APOE gene. It is a core component of plasma lipoproteins, participating in the production, transport, and clearance of lipoproteins. ApoE is associated with chylomicrons, chylomicron remnants, high-density lipoprotein (HDL), very low-density lipoprotein (VLDL), and intermediate-density lipoprotein (IDL), especially showing preferential binding to HDL [7]. ApoE is the most important lipid transport protein in the body, having a profound impact on lipid metabolism. The interaction of ApoE with the low-density lipoprotein receptor (LDLR) is essential for the normal processing (catabolism) of triglyceride-rich lipoproteins [8]. In peripheral tissues, ApoE is primarily produced by the liver and macrophages and mediates cholesterol metabolism. In the central nervous system, ApoE is produced mainly by astrocytes and is the major cholesterol carrier in the brain. ApoE is essential for transporting cholesterol from astrocytes to neurons [7-10]. In addition, ApoE forms a complex with activated C1q, becoming a checkpoint inhibitor target of the classical complement pathway [11]. Polymorphisms of the APOE are associated with Alzheimer's disease and lipid accumulation, hyperlipidemia, atherosclerosis, high cholesterolemia, etc., and are related to the risk of various cardiovascular diseases.
The B6-hPCSK9/Apoe KO mice are obtained by crossing B6-hPCSK9 mice (Catalog No.: C001617) with B6J-Apoe KO mice (Catalog No.: C001507). B6J-Apoe KO mice exhibit elevated cholesterol levels and spontaneous atherosclerosis phenotypes due to the disruption of ApoE protein synthesis, further exacerbated under a high-fat diet (HFD). On the other hand, B6-hPCSK9 mice have the mouse Pcsk9 gene sequence replaced with the human PCSK9 gene sequence through gene editing technology, expressing the human PCSK9 protein. They can be used for the development of PCSK9-targeted drugs in hyperlipidemia, stroke, coronary heart disease, and other atherosclerotic cardiovascular diseases (ASCVD). The B6-hPCSK9/Apoe KO mice, while expressing the human PCSK9 protein, exhibit significantly elevated cholesterol levels and spontaneous atherosclerosis characteristics. These mice provide an ideal platform for the PCSK9-targeted drug development in hyperlipidemia and cardiovascular diseases, demonstrating good clinical and pathological relevance.
B6-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-hFGFR1c
製品ID :
C001684
系統:
C57BL/6NCya
状況:
説明:
The FGFR1 gene encodes fibroblast growth factor receptor 1 (FGFR1), a pivotal transmembrane receptor tyrosine kinase widely expressed across diverse cell types, including epithelial, mesenchymal, and neuronal lineages, playing fundamental roles in development, angiogenesis, cell proliferation, differentiation, and migration through activation of intracellular signaling cascades like MAPK/ERK, PI3K/AKT, and STAT [1]. Aberrant FGFR1 expression or mutations are associated with developmental syndromes and various cancers, driving tumor growth, metastasis, and therapeutic resistance; its expression is tightly regulated by diverse cellular signals [2]. A key splice isoform is FGFR1c, predominantly expressed in epithelial cells and characterized by a specific extracellular immunoglobulin-like domain III, conferring high-affinity binding to a subset of FGF ligands crucial for epithelial-mesenchymal interactions during development and adult tissue homeostasis [3]. Dysregulation of FGFR1c signaling is implicated in the pathogenesis of cancers such as breast, prostate, and lung carcinomas, contributing to tumor initiation, progression, angiogenesis, and potentially therapy resistance, highlighting the importance of understanding isoform-specific functions for targeted therapeutic interventions [3-4].
B6-hFGFR1c mice are humanized models generated by gene editing technology, in which the p.22R to partial intron 2 of the mouse Fgfr1 gene was replaced in situ with p.22R to 376E from the coding sequence of the human FGFR1 gene, p.377I to 823X from the coding sequence of the mouse Fgfr1 gene, and the 3'UTR of the mouse Fgfr1 gene. This model can be used to study the pathological mechanisms and therapeutic methods of cancers, metabolic diseases such as obesity, diabetes, and metabolic-associated steatohepatitis (MASH), as well as the screening and development of FGFR1c-targeted drugs, and preclinical efficacy and safety evaluations.
The FGFR1 gene encodes fibroblast growth factor receptor 1 (FGFR1), a pivotal transmembrane receptor tyrosine kinase widely expressed across diverse cell types, including epithelial, mesenchymal, and neuronal lineages, playing fundamental roles in development, angiogenesis, cell proliferation, differentiation, and migration through activation of intracellular signaling cascades like MAPK/ERK, PI3K/AKT, and STAT [1]. Aberrant FGFR1 expression or mutations are associated with developmental syndromes and various cancers, driving tumor growth, metastasis, and therapeutic resistance; its expression is tightly regulated by diverse cellular signals [2]. A key splice isoform is FGFR1c, predominantly expressed in epithelial cells and characterized by a specific extracellular immunoglobulin-like domain III, conferring high-affinity binding to a subset of FGF ligands crucial for epithelial-mesenchymal interactions during development and adult tissue homeostasis [3]. Dysregulation of FGFR1c signaling is implicated in the pathogenesis of cancers such as breast, prostate, and lung carcinomas, contributing to tumor initiation, progression, angiogenesis, and potentially therapy resistance, highlighting the importance of understanding isoform-specific functions for targeted therapeutic interventions [3-4].
B6-hFGFR1c mice are humanized models generated by gene editing technology, in which the p.22R to partial intron 2 of the mouse Fgfr1 gene was replaced in situ with p.22R to 376E from the coding sequence of the human FGFR1 gene, p.377I to 823X from the coding sequence of the mouse Fgfr1 gene, and the 3'UTR of the mouse Fgfr1 gene. This model can be used to study the pathological mechanisms and therapeutic methods of cancers, metabolic diseases such as obesity, diabetes, and metabolic-associated steatohepatitis (MASH), as well as the screening and development of FGFR1c-targeted drugs, and preclinical efficacy and safety evaluations.
B6-hCD47
製品ID :
C001419
系統:
C57BL/6JCya
状況:
説明:
CD47, also known as Integrin Associated Protein (IAP), is a transmembrane protein that belongs to the immunoglobulin superfamily. It is widely expressed on the surface of almost all normal cells and is highly expressed in tumor cells [1].
SIRPα, a signal regulatory protein mainly expressed on macrophages, inhibits their phagocytosis of target cells by transmitting inhibitory signals when binding to CD47 on other cells. However, some tumor cells can evade phagocytosis and cause tumor immune escape by highly expressing CD47 and binding to SIRPα on macrophages, sending a “don’t eat me” signal. Targeting CD47 antibodies can initiate anti-tumor T cell immune responses and promote cancer-specific lymphocyte activation through macrophage-mediated phagocytosis of tumors. As a result, the CD47-SIRPα signaling pathway has great therapeutic potential and is a highly competitive target in tumor immunotherapy after PD-1/PD-L1 [1-2].
CD47 is a transmembrane protein with its extracellular domain serving as the receptor/ligand binding region and its intracellular domain responsible for signal transduction [3]. B6-hCD47 mice are obtained by replacing the fragment encoding the extracellular domain of CD47 protein in the mouse Cd47 gene with the corresponding human CD47 gene sequence, resulting in a model expressing the extracellular domain of human CD47 protein and the intracellular domain of mouse CD47 protein. This ensures normal binding with human antibodies and other protein drugs while completely retaining the intracellular part of mouse CD47 protein, maintaining normal intracellular signal transduction. B6-hCD47 mice can successfully express human CD47 protein and can be used for research on CD47-targeted inhibitors or antibody drug development and screening, pharmacology and safety evaluation, tumor immunotherapy evaluation, and mechanisms of tumor immune escape systems.
CD47, also known as Integrin Associated Protein (IAP), is a transmembrane protein that belongs to the immunoglobulin superfamily. It is widely expressed on the surface of almost all normal cells and is highly expressed in tumor cells [1].
SIRPα, a signal regulatory protein mainly expressed on macrophages, inhibits their phagocytosis of target cells by transmitting inhibitory signals when binding to CD47 on other cells. However, some tumor cells can evade phagocytosis and cause tumor immune escape by highly expressing CD47 and binding to SIRPα on macrophages, sending a “don’t eat me” signal. Targeting CD47 antibodies can initiate anti-tumor T cell immune responses and promote cancer-specific lymphocyte activation through macrophage-mediated phagocytosis of tumors. As a result, the CD47-SIRPα signaling pathway has great therapeutic potential and is a highly competitive target in tumor immunotherapy after PD-1/PD-L1 [1-2].
CD47 is a transmembrane protein with its extracellular domain serving as the receptor/ligand binding region and its intracellular domain responsible for signal transduction [3]. B6-hCD47 mice are obtained by replacing the fragment encoding the extracellular domain of CD47 protein in the mouse Cd47 gene with the corresponding human CD47 gene sequence, resulting in a model expressing the extracellular domain of human CD47 protein and the intracellular domain of mouse CD47 protein. This ensures normal binding with human antibodies and other protein drugs while completely retaining the intracellular part of mouse CD47 protein, maintaining normal intracellular signal transduction. B6-hCD47 mice can successfully express human CD47 protein and can be used for research on CD47-targeted inhibitors or antibody drug development and screening, pharmacology and safety evaluation, tumor immunotherapy evaluation, and mechanisms of tumor immune escape systems.
B6-hDPP4 (line1)
製品ID :
I001187
系統:
C57BL/6NCya
状況:
説明:
The DPP4 gene (CD26) encodes dipeptidyl peptidase 4, an intrinsic type II transmembrane glycoprotein and a serine exopeptidase involved in glucose and insulin metabolism and immune regulation. The DPP4 protein is a functional receptor for the Middle East Respiratory Syndrome Coronavirus (MERS-CoV). The spike protein of MERS-CoV binds to DPP4, mediating the virus's attachment to host cells and promoting virus-cell fusion, thereby initiating infection [1-2]. Studies have found that the DPP4 protein may interact with the S1 domain of the spike glycoprotein of COVID-19, aiding in enhancing the transmission efficiency of viral particles [3]. Experimental evidence has shown that hDPP4 transgenic mice infected with MERS-CoV experience high mortality and severe pneumonia [4]. These mice infected with Manis javanica HKU4-related coronavirus (MjHKU4r-CoV-1) develop mild to moderate pulmonary histological damage [5]. Thus, gene-edited mice expressing human DPP4 protein are important tools for studying coronavirus infections. Additionally, DPP4 expression is severely dysregulated in diseases such as inflammation, cancer, obesity, and diabetes. DPP4 is highly expressed in the intestine, where it selectively cleaves N-terminal dipeptides from various substrates, including incretins, to inactivate multiple bioactive peptides. Since incretins like glucagon-like peptide-1 (GLP-1) and glucose-dependent insulinotropic polypeptide (GIP) are crucial for regulating postprandial insulin secretion, inhibiting DPP4 to elevate endogenous GLP-1 and GIP levels to increase insulin levels has become an important treatment method for type 2 diabetes (T2D) [6].
The B6-hDPP4(line 1) mouse is a humanized model constructed by gene editing technology to replace a partial region of the mouse Dpp4 gene with the human DPP4 gene CDS sequence. This model can be used to study the infection mechanisms of viruses such as MERS-CoV and COVID-19, as well as to develop related virus vaccines. Additionally, this model can be utilized to develop DPP4 inhibitor therapies. Additionally, Cyagen Biosciences has developed B6-hDPP4(line 2) mice (Catalog ID: I001188) on the C57BL/6JCya background strain and BALB/c-hDPP4(line 2) mice (Catalog ID: I001189) on the BALB/cAnCya background strain. These two models replace the mouse Dpp4 gene p.S29 to part of intron 2 with the "Human DPP4 CDS-rBG pA" expression cassette, meeting the experimental needs for different strain backgrounds.
The DPP4 gene (CD26) encodes dipeptidyl peptidase 4, an intrinsic type II transmembrane glycoprotein and a serine exopeptidase involved in glucose and insulin metabolism and immune regulation. The DPP4 protein is a functional receptor for the Middle East Respiratory Syndrome Coronavirus (MERS-CoV). The spike protein of MERS-CoV binds to DPP4, mediating the virus's attachment to host cells and promoting virus-cell fusion, thereby initiating infection [1-2]. Studies have found that the DPP4 protein may interact with the S1 domain of the spike glycoprotein of COVID-19, aiding in enhancing the transmission efficiency of viral particles [3]. Experimental evidence has shown that hDPP4 transgenic mice infected with MERS-CoV experience high mortality and severe pneumonia [4]. These mice infected with Manis javanica HKU4-related coronavirus (MjHKU4r-CoV-1) develop mild to moderate pulmonary histological damage [5]. Thus, gene-edited mice expressing human DPP4 protein are important tools for studying coronavirus infections. Additionally, DPP4 expression is severely dysregulated in diseases such as inflammation, cancer, obesity, and diabetes. DPP4 is highly expressed in the intestine, where it selectively cleaves N-terminal dipeptides from various substrates, including incretins, to inactivate multiple bioactive peptides. Since incretins like glucagon-like peptide-1 (GLP-1) and glucose-dependent insulinotropic polypeptide (GIP) are crucial for regulating postprandial insulin secretion, inhibiting DPP4 to elevate endogenous GLP-1 and GIP levels to increase insulin levels has become an important treatment method for type 2 diabetes (T2D) [6].
The B6-hDPP4(line 1) mouse is a humanized model constructed by gene editing technology to replace a partial region of the mouse Dpp4 gene with the human DPP4 gene CDS sequence. This model can be used to study the infection mechanisms of viruses such as MERS-CoV and COVID-19, as well as to develop related virus vaccines. Additionally, this model can be utilized to develop DPP4 inhibitor therapies. Additionally, Cyagen Biosciences has developed B6-hDPP4(line 2) mice (Catalog ID: I001188) on the C57BL/6JCya background strain and BALB/c-hDPP4(line 2) mice (Catalog ID: I001189) on the BALB/cAnCya background strain. These two models replace the mouse Dpp4 gene p.S29 to part of intron 2 with the "Human DPP4 CDS-rBG pA" expression cassette, meeting the experimental needs for different strain backgrounds.
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