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B6-hMASP2
Product ID:
C001592
Strain:
C57BL/6NCya
Status:
Description:
The MASP2 gene encodes MASP-2, a serum serine protease that serves as a key mediator in complement system activation. MASP-2 initiates the lectin pathway by forming complexes with pattern recognition molecules such as mannose-binding lectin (MBL) and ficolins. Upon pathogen recognition by MBL, MASP-2 is activated and subsequently cleaves complement components C4 and C2, leading to the generation of C3 convertase and triggering downstream complement activation. Beyond its role in the complement cascade, MASP-2 also contributes to the coagulation pathway by cleaving prothrombin to generate thrombin, thereby linking innate immunity and hemostasis [1]. Emerging evidence highlights the clinical significance of MASP2 gene polymorphisms, which are associated with altered susceptibility to infectious diseases and immune-related disorders. Reduced plasma levels of MASP-2 have been linked to increased vulnerability to HIV infection, while elevated MASP-2 activity may exacerbate inflammatory responses [2]. Given its pivotal role in immune regulation, MASP-2 has emerged as a promising therapeutic target. Inhibition of MASP-2 is currently under investigation as a potential strategy for treating a range of conditions, including IgA nephropathy (IgAN) [3], atypical hemolytic uremic syndrome (aHUS), and transplant-associated thrombotic microangiopathy (TA-TMA) [4].
The B6-hMASP2 mouse model, generated through precise gene editing technology, features the in situ replacement of part of the endogenous mouse Masp2 gene with the coding sequence (CDS) of human MASP2. Homozygous B6-hMASP2 mice are viable and fertile, providing a robust platform for studying the pathophysiology of autoimmune and infectious diseases. This model also serves as a valuable tool for the development and preclinical evaluation of MASP-2-targeted therapeutics, offering insights into both mechanistic and translational aspects of complement-mediated diseases.
The MASP2 gene encodes MASP-2, a serum serine protease that serves as a key mediator in complement system activation. MASP-2 initiates the lectin pathway by forming complexes with pattern recognition molecules such as mannose-binding lectin (MBL) and ficolins. Upon pathogen recognition by MBL, MASP-2 is activated and subsequently cleaves complement components C4 and C2, leading to the generation of C3 convertase and triggering downstream complement activation. Beyond its role in the complement cascade, MASP-2 also contributes to the coagulation pathway by cleaving prothrombin to generate thrombin, thereby linking innate immunity and hemostasis [1]. Emerging evidence highlights the clinical significance of MASP2 gene polymorphisms, which are associated with altered susceptibility to infectious diseases and immune-related disorders. Reduced plasma levels of MASP-2 have been linked to increased vulnerability to HIV infection, while elevated MASP-2 activity may exacerbate inflammatory responses [2]. Given its pivotal role in immune regulation, MASP-2 has emerged as a promising therapeutic target. Inhibition of MASP-2 is currently under investigation as a potential strategy for treating a range of conditions, including IgA nephropathy (IgAN) [3], atypical hemolytic uremic syndrome (aHUS), and transplant-associated thrombotic microangiopathy (TA-TMA) [4].
The B6-hMASP2 mouse model, generated through precise gene editing technology, features the in situ replacement of part of the endogenous mouse Masp2 gene with the coding sequence (CDS) of human MASP2. Homozygous B6-hMASP2 mice are viable and fertile, providing a robust platform for studying the pathophysiology of autoimmune and infectious diseases. This model also serves as a valuable tool for the development and preclinical evaluation of MASP-2-targeted therapeutics, offering insights into both mechanistic and translational aspects of complement-mediated diseases.
B6-hFGFR1c
Product ID:
C001684
Strain:
C57BL/6NCya
Status:
Description:
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-hLPA (CKI)
Product ID:
C001521
Strain:
C57BL/6NCya
Status:
Description:
Lipoprotein A (LPA) is a type of particle similar to low-density lipoprotein (LDL) that is considered one of the risk factors for cardiovascular disease (CVD) such as atherosclerosis, coronary heart disease, stroke, etc [1]. LP(a) is similar in size and lipid content to LDL (low-density lipoprotein) and 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-hDPP4 (line1)
Product ID:
I001187
Strain:
C57BL/6NCya
Status:
Description:
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.
B6-hDPP4 (line 2)
Product ID:
I001188
Strain:
C57BL/6JCya
Status:
Description:
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 2) 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. Similar models include the B6-hDPP4(line 1) mouse (Catalog ID: I001187), constructed on the C57BL/6NCya background strain, which replaces the sequence of the mouse Dpp4 gene with the human DPP4 gene CDS sequence, and the BALB/c-hDPP4(line 2) mouse (Catalog ID: I001189), constructed on the BALB/cAnCya background strain. These models meet the experimental needs of 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 2) 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. Similar models include the B6-hDPP4(line 1) mouse (Catalog ID: I001187), constructed on the C57BL/6NCya background strain, which replaces the sequence of the mouse Dpp4 gene with the human DPP4 gene CDS sequence, and the BALB/c-hDPP4(line 2) mouse (Catalog ID: I001189), constructed on the BALB/cAnCya background strain. These models meet the experimental needs of different strain backgrounds.
BALB/c-hDPP4 (line 2)
Product ID:
I001189
Strain:
BALB/cAnCya
Status:
Description:
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 BALB/c-hDPP4(line 2) 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. Similar models include the B6-hDPP4(line 1) mouse (Catalog ID: I001187), constructed on the C57BL/6NCya background strain, which replaces the sequence of the mouse Dpp4 gene with the human DPP4 gene CDS sequence, and the B6-hDPP4(line 2) mouse (Catalog ID: I001188), constructed on the C57BL/6JCya background strain. These models meet the experimental needs of 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 BALB/c-hDPP4(line 2) 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. Similar models include the B6-hDPP4(line 1) mouse (Catalog ID: I001187), constructed on the C57BL/6NCya background strain, which replaces the sequence of the mouse Dpp4 gene with the human DPP4 gene CDS sequence, and the B6-hDPP4(line 2) mouse (Catalog ID: I001188), constructed on the C57BL/6JCya background strain. These models meet the experimental needs of different strain backgrounds.
B6-hKHK
Product ID:
C001642
Strain:
C57BL/6NCya
Status:
Description:
The KHK gene encodes ketohexokinase, an enzyme mainly expressed in the liver, kidneys, and small intestine, and plays a crucial role in fructose metabolism. KHK catalyzes the phosphorylation of fructose into fructose-1-phosphate, which is the first step in the fructose metabolic pathway, enabling its conversion into intermediate products that can enter the glycolytic or gluconeogenic pathways. This gene generates two isoforms (KHK-A and KHK-C). Among them, KHK-C has higher catalytic activity and is mainly expressed in the liver, while KHK-A is widely distributed in various tissues, but its function is not fully understood. The expression and activity of KHK are closely related to fructose intake. Excessive fructose intake will lead to the upregulation of KHK activity, which triggers metabolic disorders, such as metabolic dysfunction-associated steatotic liver disease (MASLD), insulin resistance, and obesity [1]. The excessive activation of KHK-C is closely associated with fructose-induced metabolic dysfunction, and blocking KHK-C can significantly ameliorate metabolic abnormalities in fructose-sensitive mice [2]. In addition, fructose metabolism may play an important role in cancer and other proliferative diseases, providing signaling cues that sustain the proliferation of cancer cells. Many cancer cells overexpress KHK. Moreover, the genetic disorder (essential fructosuria) caused by loss-of-function mutations in KHK is clinically asymptomatic and harmless, which further supports the view that inhibiting KHK in cancer patients may be well tolerated [3]. Therefore, KHK has emerged as a potential target for treating metabolic diseases and cancer. Inhibitors targeting KHK are currently under development and have shown the potential to improve metabolic syndrome and inhibit tumor progression.
The B6-hKHK mice are a humanized model constructed through gene editing technology, in which the sequence of the mouse Khk gene is replaced in situ with the corresponding sequence of the human KHK gene. Homozygous B6-hKHK mice are viable and fertile. This model can be used for the study of the pathological mechanisms and treatment methods of metabolic diseases such as metabolic dysfunction-associated steatotic liver disease (MASLD), insulin resistance, and obesity, as well as cancer. It can also be applied to the screening, research and development, and safety evaluation of KHK-targeted drugs.
The KHK gene encodes ketohexokinase, an enzyme mainly expressed in the liver, kidneys, and small intestine, and plays a crucial role in fructose metabolism. KHK catalyzes the phosphorylation of fructose into fructose-1-phosphate, which is the first step in the fructose metabolic pathway, enabling its conversion into intermediate products that can enter the glycolytic or gluconeogenic pathways. This gene generates two isoforms (KHK-A and KHK-C). Among them, KHK-C has higher catalytic activity and is mainly expressed in the liver, while KHK-A is widely distributed in various tissues, but its function is not fully understood. The expression and activity of KHK are closely related to fructose intake. Excessive fructose intake will lead to the upregulation of KHK activity, which triggers metabolic disorders, such as metabolic dysfunction-associated steatotic liver disease (MASLD), insulin resistance, and obesity [1]. The excessive activation of KHK-C is closely associated with fructose-induced metabolic dysfunction, and blocking KHK-C can significantly ameliorate metabolic abnormalities in fructose-sensitive mice [2]. In addition, fructose metabolism may play an important role in cancer and other proliferative diseases, providing signaling cues that sustain the proliferation of cancer cells. Many cancer cells overexpress KHK. Moreover, the genetic disorder (essential fructosuria) caused by loss-of-function mutations in KHK is clinically asymptomatic and harmless, which further supports the view that inhibiting KHK in cancer patients may be well tolerated [3]. Therefore, KHK has emerged as a potential target for treating metabolic diseases and cancer. Inhibitors targeting KHK are currently under development and have shown the potential to improve metabolic syndrome and inhibit tumor progression.
The B6-hKHK mice are a humanized model constructed through gene editing technology, in which the sequence of the mouse Khk gene is replaced in situ with the corresponding sequence of the human KHK gene. Homozygous B6-hKHK mice are viable and fertile. This model can be used for the study of the pathological mechanisms and treatment methods of metabolic diseases such as metabolic dysfunction-associated steatotic liver disease (MASLD), insulin resistance, and obesity, as well as cancer. It can also be applied to the screening, research and development, and safety evaluation of KHK-targeted drugs.
B6-hXDH
Product ID:
C001586
Strain:
C57BL/6NCya
Status:
Description:
Hyperuricemia is a metabolic disorder characterized by abnormally elevated levels of uric acid (UA) in the blood. Uric acid, the end product of purine metabolism, may crystallize as urate in joints, leading to gouty arthritis or form stones in the kidneys when its concentration is excessively high. The clinical manifestations of gout include hyperuricemia, recurrent acute gouty arthritis, deposition of tophi, chronic tophaceous arthritis, and joint deformities. It commonly affects the kidneys, causing chronic interstitial nephritis and uric acid nephrolithiasis [1-3]. By 2020, the global prevalence of hyperuricemia and gout surpassed 1.1 billion cases. In China, the number of patients is projected to reach 200 million for hyperuricemia and 43.25 million for gout by 2024 [2-3]. With the increasing disease burden, the demand for pharmacological interventions for hyperuricemia and gout continues to grow.
Hyperuricemia is closely related to uric acid levels in the body, and current therapeutic agents mainly target the reduction of uric acid synthesis or the promotion of uric acid excretion to manage the condition. Xanthine oxidoreductase (XOR) plays a critical role in purine metabolism by catalyzing the oxidation of hypoxanthine to xanthine and subsequently to uric acid. It is thus a key regulatory point in uric acid synthesis and an important target for hyperuricemia treatment [4-5]. XOR exists in two forms: the reduced xanthine dehydrogenase (XDH) and the oxidized xanthine oxidase (XO). XDH, in its reduced state, catalyzes the conversion of hypoxanthine to xanthine and uric acid, generating reduced nicotinamide adenine dinucleotide (NADH). In contrast, XO, in its oxidized state, converts xanthine to uric acid and hydrogen peroxide. The inhibition of XO by xanthine oxidase inhibitors (XOIs) to reduce uric acid production is a widely adopted therapeutic strategy for hyperuricemia and gout [6]. However, safety concerns remain with existing XOIs, highlighting the urgent need for novel therapeutics with improved safety profiles. Small interfering RNA (siRNA) represents a promising research focus in this area.
This strain is a humanized mouse model of the Xdh gene, generated by replacing the mouse Xdh gene with the complete human XDH gene sequence, including its untranslated regions (UTRs), exons, and introns. The B6-hXDH mice express the human XDH gene and xanthine oxidase protein in a pattern similar to the endogenous Xdh gene in mice, making their genetic, protein expression, and biochemical features highly comparable to humans. This strain serves as an ideal preclinical platform for studying the pathological mechanisms of hyperuricemia and gout and for developing novel xanthine oxidase inhibitors and nucleic acid therapies.
Hyperuricemia is a metabolic disorder characterized by abnormally elevated levels of uric acid (UA) in the blood. Uric acid, the end product of purine metabolism, may crystallize as urate in joints, leading to gouty arthritis or form stones in the kidneys when its concentration is excessively high. The clinical manifestations of gout include hyperuricemia, recurrent acute gouty arthritis, deposition of tophi, chronic tophaceous arthritis, and joint deformities. It commonly affects the kidneys, causing chronic interstitial nephritis and uric acid nephrolithiasis [1-3]. By 2020, the global prevalence of hyperuricemia and gout surpassed 1.1 billion cases. In China, the number of patients is projected to reach 200 million for hyperuricemia and 43.25 million for gout by 2024 [2-3]. With the increasing disease burden, the demand for pharmacological interventions for hyperuricemia and gout continues to grow.
Hyperuricemia is closely related to uric acid levels in the body, and current therapeutic agents mainly target the reduction of uric acid synthesis or the promotion of uric acid excretion to manage the condition. Xanthine oxidoreductase (XOR) plays a critical role in purine metabolism by catalyzing the oxidation of hypoxanthine to xanthine and subsequently to uric acid. It is thus a key regulatory point in uric acid synthesis and an important target for hyperuricemia treatment [4-5]. XOR exists in two forms: the reduced xanthine dehydrogenase (XDH) and the oxidized xanthine oxidase (XO). XDH, in its reduced state, catalyzes the conversion of hypoxanthine to xanthine and uric acid, generating reduced nicotinamide adenine dinucleotide (NADH). In contrast, XO, in its oxidized state, converts xanthine to uric acid and hydrogen peroxide. The inhibition of XO by xanthine oxidase inhibitors (XOIs) to reduce uric acid production is a widely adopted therapeutic strategy for hyperuricemia and gout [6]. However, safety concerns remain with existing XOIs, highlighting the urgent need for novel therapeutics with improved safety profiles. Small interfering RNA (siRNA) represents a promising research focus in this area.
This strain is a humanized mouse model of the Xdh gene, generated by replacing the mouse Xdh gene with the complete human XDH gene sequence, including its untranslated regions (UTRs), exons, and introns. The B6-hXDH mice express the human XDH gene and xanthine oxidase protein in a pattern similar to the endogenous Xdh gene in mice, making their genetic, protein expression, and biochemical features highly comparable to humans. This strain serves as an ideal preclinical platform for studying the pathological mechanisms of hyperuricemia and gout and for developing novel xanthine oxidase inhibitors and nucleic acid therapies.
B6-htau/hGLP-1R
Product ID:
I001221
Strain:
C57BL/6Cya
Status:
Description:
The tau protein, a microtubule-associated protein encoded by MAPT is primarily localized to neuronal axons and plays a critical role in microtubule stability and assembly. By binding to microtubules, tau protein helps to maintain neuronal cell shape. Mutations in MAPT can promote tau aggregation, leading to pathological tau protein accumulation and death of glutamatergic cortical neurons [1]. Additionally, certain MAPT mutations can affect pre-mRNA exon splicing, altering the ratio of 3R to 4R tau protein isoforms and increasing the relative production of 4R-tau protein, which is more prone to fibril formation [2].
The GLP-1 receptor (GLP-1R) gene encodes a protein that serves as the receptor for the glucagon-like peptide 1 (GLP-1) hormone, belonging to the glucagon receptor subfamily within the class B G-protein-coupled receptors (GPCRs). G proteins are a class of intracellular signal transduction proteins typically associated with seven-transmembrane receptors (GPCRs). When a GPCR binds to its ligand, it activates the G protein, causing it to dissociate from the Gβγ subunit and initiate downstream effects through interactions with membrane-bound effector molecules. This signaling process is known as canonical G protein signaling. GLP-1R is a multi-transmembrane protein characterized by a typical seven-transmembrane core domain and a relatively large extracellular domain, which can stimulate glucose-induced insulin secretion [3]. GLP-1R is a cell surface receptor protein widely expressed in tissues such as the brain, small intestine, heart, and lungs. It internalizes in response to GLP-1 and GLP-1 analogs and plays a crucial role in the insulin secretion signaling cascade. Additionally, data from animal models indicate its neuroprotective effects [4-5]. Polymorphisms of this gene are closely associated with diabetes. The GLP1R protein is an important drug target for treating type 2 diabetes and stroke. Glucagon-like peptide-1 receptor agonists (GLP-1RAs) are a new class of antidiabetic drugs in recent years. They activate GLP1R to enhance insulin secretion, suppress glucagon secretion, delay gastric emptying, and reduce food intake through central appetite suppression, lowering blood glucose and weight loss [6].
The B6-htau/hGLP-1R mouse is obtained by mating B6-htau mice (Catalog No.: C001410) with B6-hGLP-1R mice (Catalog No.: C001421). This model can be used for research on neurodegenerative diseases such as frontotemporal dementia (FTD) and Alzheimer's disease (AD), as well as metabolic diseases such as obesity and type 2 diabetes. It is also useful for developing GLP-1 receptor agonist (GLP-1RA) drugs or for the preclinical evaluation of the potential therapeutic effects of GLP-1RA drugs in tauopathy-related diseases like Alzheimer's disease (AD).
The tau protein, a microtubule-associated protein encoded by MAPT is primarily localized to neuronal axons and plays a critical role in microtubule stability and assembly. By binding to microtubules, tau protein helps to maintain neuronal cell shape. Mutations in MAPT can promote tau aggregation, leading to pathological tau protein accumulation and death of glutamatergic cortical neurons [1]. Additionally, certain MAPT mutations can affect pre-mRNA exon splicing, altering the ratio of 3R to 4R tau protein isoforms and increasing the relative production of 4R-tau protein, which is more prone to fibril formation [2].
The GLP-1 receptor (GLP-1R) gene encodes a protein that serves as the receptor for the glucagon-like peptide 1 (GLP-1) hormone, belonging to the glucagon receptor subfamily within the class B G-protein-coupled receptors (GPCRs). G proteins are a class of intracellular signal transduction proteins typically associated with seven-transmembrane receptors (GPCRs). When a GPCR binds to its ligand, it activates the G protein, causing it to dissociate from the Gβγ subunit and initiate downstream effects through interactions with membrane-bound effector molecules. This signaling process is known as canonical G protein signaling. GLP-1R is a multi-transmembrane protein characterized by a typical seven-transmembrane core domain and a relatively large extracellular domain, which can stimulate glucose-induced insulin secretion [3]. GLP-1R is a cell surface receptor protein widely expressed in tissues such as the brain, small intestine, heart, and lungs. It internalizes in response to GLP-1 and GLP-1 analogs and plays a crucial role in the insulin secretion signaling cascade. Additionally, data from animal models indicate its neuroprotective effects [4-5]. Polymorphisms of this gene are closely associated with diabetes. The GLP1R protein is an important drug target for treating type 2 diabetes and stroke. Glucagon-like peptide-1 receptor agonists (GLP-1RAs) are a new class of antidiabetic drugs in recent years. They activate GLP1R to enhance insulin secretion, suppress glucagon secretion, delay gastric emptying, and reduce food intake through central appetite suppression, lowering blood glucose and weight loss [6].
The B6-htau/hGLP-1R mouse is obtained by mating B6-htau mice (Catalog No.: C001410) with B6-hGLP-1R mice (Catalog No.: C001421). This model can be used for research on neurodegenerative diseases such as frontotemporal dementia (FTD) and Alzheimer's disease (AD), as well as metabolic diseases such as obesity and type 2 diabetes. It is also useful for developing GLP-1 receptor agonist (GLP-1RA) drugs or for the preclinical evaluation of the potential therapeutic effects of GLP-1RA drugs in tauopathy-related diseases like Alzheimer's disease (AD).
B6-hGPR75 (1)
Product ID:
C001613
Strain:
C57BL/6JCya
Status:
Description:
The GPR75 gene encodes a transmembrane protein belonging to the G protein-coupled receptor (GPCR) family. This receptor is primarily expressed in the brain, particularly enriched in the cilia of hypothalamic neurons that regulate appetite. It couples with Gαq proteins to activate downstream signaling pathways (such as MAPK, NF-κB, etc.), participating in the regulation of energy balance, feeding behavior, and fat metabolism [1][2]. The encoded protein comprises 540 amino acids with a typical 7-transmembrane structure. Upon binding with ligands like 20-hydroxyeicosatetraenoic acid (20-HETE), it can trigger physiological effects such as inflammation, vasoconstriction, and lipid accumulation [2][3]. Research has found that loss-of-function or mutations in GPR75 (e.g., the L144P variant) can significantly reduce body weight and fat mass, resist high-fat diet-induced obesity and non-alcoholic fatty liver disease (NAFLD), and improve insulin sensitivity [1][3][4]. Furthermore, GPR75 mediates 20-HETE-induced cardiomyocyte apoptosis in the cardiovascular system, which is associated with hypertension and endothelial dysfunction [2][3]. In cancer, GPR75 may promote cachexia progression by regulating white adipose tissue browning [5]. Whole-exome sequencing has revealed that rare variants in GPR75 are closely related to low BMI and reduced obesity risk in humans, making it a promising therapeutic target for obesity, metabolic syndrome, and cardiovascular diseases [3].
The B6-hGPR75 (1) mouse is a humanized model generated through gene editing technology, in which part of the mouse Gpr75 gene sequence is replaced in situ with the human GPR75 gene sequence. Homozygous B6-hGPR75 (1) mice are viable and fertile. This model can be used to study the pathological mechanisms and therapeutic interventions for obesity, metabolic diseases, and cardiovascular diseases, as well as for screening, developing, and evaluating the safety of GPR75-targeted drugs.
The GPR75 gene encodes a transmembrane protein belonging to the G protein-coupled receptor (GPCR) family. This receptor is primarily expressed in the brain, particularly enriched in the cilia of hypothalamic neurons that regulate appetite. It couples with Gαq proteins to activate downstream signaling pathways (such as MAPK, NF-κB, etc.), participating in the regulation of energy balance, feeding behavior, and fat metabolism [1][2]. The encoded protein comprises 540 amino acids with a typical 7-transmembrane structure. Upon binding with ligands like 20-hydroxyeicosatetraenoic acid (20-HETE), it can trigger physiological effects such as inflammation, vasoconstriction, and lipid accumulation [2][3]. Research has found that loss-of-function or mutations in GPR75 (e.g., the L144P variant) can significantly reduce body weight and fat mass, resist high-fat diet-induced obesity and non-alcoholic fatty liver disease (NAFLD), and improve insulin sensitivity [1][3][4]. Furthermore, GPR75 mediates 20-HETE-induced cardiomyocyte apoptosis in the cardiovascular system, which is associated with hypertension and endothelial dysfunction [2][3]. In cancer, GPR75 may promote cachexia progression by regulating white adipose tissue browning [5]. Whole-exome sequencing has revealed that rare variants in GPR75 are closely related to low BMI and reduced obesity risk in humans, making it a promising therapeutic target for obesity, metabolic syndrome, and cardiovascular diseases [3].
The B6-hGPR75 (1) mouse is a humanized model generated through gene editing technology, in which part of the mouse Gpr75 gene sequence is replaced in situ with the human GPR75 gene sequence. Homozygous B6-hGPR75 (1) mice are viable and fertile. This model can be used to study the pathological mechanisms and therapeutic interventions for obesity, metabolic diseases, and cardiovascular diseases, as well as for screening, developing, and evaluating the safety of GPR75-targeted drugs.
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