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B6-hXDH
製品ID :
C001586
系統:
C57BL/6NCya
状況:
説明:
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-hLPA(CKI)/Alb-cre/hPCSK9
製品ID :
I002079
系統:
C57BL/6NCya
状況:
説明:
Lipoprotein A (LPA) is a type of particle similar to low-density lipoprotein (LDL) that is considered one of the risk factors for cardiovascular disease (CVD), such as atherosclerosis, coronary heart disease, stroke, etc [1]. LP(a) is similar in size and lipid content to LDL (low-density lipoprotein) and also contains the lipoprotein ApoB-100. However, unlike LDL, LP(a) additionally contains a variable-length lipoprotein called Apo(a), which covalently binds to ApoB-100 through a single disulfide bond. LP(a) plays an important role in systemic lipid transport, guiding inflammatory cells into blood vessel walls and leading to smooth muscle cell proliferation. Furthermore, it is involved in wound healing and tissue repair, interacting with the components of blood vessel walls and the extracellular matrix [2]. However, LP(a) can also cause arterial narrowing by adhering to the arterial wall, accelerating the formation of blood clots, and thereby triggering a series of pathological changes related to coronary heart disease, cardiovascular disease, atherosclerosis, thrombus formation, and stroke [3].
The plasma concentration of LP(a) is closely related to genetic factors and is primarily regulated by the LPA gene. Therefore, the LPA gene is an important potential target for cardiovascular disease treatment. The LPA gene encodes a serine protease that inhibits the activity of tissue-type plasminogen activator I. Fragments of this protein, generated through protein hydrolysis, can adhere to atherosclerotic lesions in arteries, promoting blood clot formation. The LPA gene is expressed in both humans and non-human primates but is not expressed in mice. Constructing mouse models expressing the human LPA gene is of significant importance for developing lipid-lowering drugs, which can drive the development of novel therapies for cardiovascular diseases. Currently, various novel therapies targeting the transcription rate of the LPA gene are under development, including small interfering RNA (siRNA) and antisense oligonucleotides (ASO) [4].
Proprotein convertase subtilisin/kexin 9 (PCSK9) is a serine protease primarily produced in the liver but expressed in other tissues, including the intestine, heart, and neurons. The N-terminal domain of the PCSK9 protein is responsible for protein localization and stability, while the C-terminal domain is responsible for protein enzymatic activity [5]. The Low-density lipoprotein receptor (LDLR) is a receptor that is responsible for clearing low-density lipoprotein cholesterol (LDL-C) from the blood. PCSK9 cleaves the intracellular domain of LDLR on the cell surface, causing it to detach from the cell membrane and be transported to the lysosome for degradation, promoting LDLR degradation, and increasing plasma LDL-C. Overexpression or gain-of-function mutations of the PCSK9 gene can lead to LDL-C accumulation by reducing LDLR levels. This can cause hypercholesterolemia, which increases the risk of cardiovascular diseases, such as atherosclerosis and coronary heart disease, and neurodegenerative diseases, such as Alzheimer's disease [6]. PCSK9 has emerged as a key target for the development of lipid-lowering drugs. Several PCSK9-targeted antibodies or small nucleic acid drugs have been approved for marketing worldwide, including evolocumab from Amgen, alirocumab from Sanofi and Regeneron, and inclisiran from Novartis. These drugs primarily work by inhibiting PCSK9 activity or preventing PCSK9 protein from binding to LDLR, lowering LDL-C levels in the blood to treat hypercholesterolemia [7-8]. In addition, PCSK9 can promote tumor growth and development by regulating cell proliferation, migration, and invasion. It can also regulate the expression of inflammatory factors that contribute to inflammation. Therefore, targeting the expression of PCSK9 has been investigated in tumor immunotherapy and autoimmune disease therapy [9-10].
The B6-hLPA (CKI)/Alb-cre/hPCSK9 mouse model is generated by crossing B6-hLPA (CKI) mice (Catalog No.: C001521, a mouse strain with conditional expression of the human LPA gene), Alb-Cre mice (liver-specific Cre-expressing mice), and B6-hPCSK9 mice (Catalog No.: C001617). This model harbors two cardiovascular disease risk factors, namely Lp (a) (lipoprotein (a)) and PCSK9, making it suitable for research on hyperlipidemia, stroke, coronary heart disease, and other atherosclerotic cardiovascular diseases (ASCVD).
Lipoprotein A (LPA) is a type of particle similar to low-density lipoprotein (LDL) that is considered one of the risk factors for cardiovascular disease (CVD), such as atherosclerosis, coronary heart disease, stroke, etc [1]. LP(a) is similar in size and lipid content to LDL (low-density lipoprotein) and also contains the lipoprotein ApoB-100. However, unlike LDL, LP(a) additionally contains a variable-length lipoprotein called Apo(a), which covalently binds to ApoB-100 through a single disulfide bond. LP(a) plays an important role in systemic lipid transport, guiding inflammatory cells into blood vessel walls and leading to smooth muscle cell proliferation. Furthermore, it is involved in wound healing and tissue repair, interacting with the components of blood vessel walls and the extracellular matrix [2]. However, LP(a) can also cause arterial narrowing by adhering to the arterial wall, accelerating the formation of blood clots, and thereby triggering a series of pathological changes related to coronary heart disease, cardiovascular disease, atherosclerosis, thrombus formation, and stroke [3].
The plasma concentration of LP(a) is closely related to genetic factors and is primarily regulated by the LPA gene. Therefore, the LPA gene is an important potential target for cardiovascular disease treatment. The LPA gene encodes a serine protease that inhibits the activity of tissue-type plasminogen activator I. Fragments of this protein, generated through protein hydrolysis, can adhere to atherosclerotic lesions in arteries, promoting blood clot formation. The LPA gene is expressed in both humans and non-human primates but is not expressed in mice. Constructing mouse models expressing the human LPA gene is of significant importance for developing lipid-lowering drugs, which can drive the development of novel therapies for cardiovascular diseases. Currently, various novel therapies targeting the transcription rate of the LPA gene are under development, including small interfering RNA (siRNA) and antisense oligonucleotides (ASO) [4].
Proprotein convertase subtilisin/kexin 9 (PCSK9) is a serine protease primarily produced in the liver but expressed in other tissues, including the intestine, heart, and neurons. The N-terminal domain of the PCSK9 protein is responsible for protein localization and stability, while the C-terminal domain is responsible for protein enzymatic activity [5]. The Low-density lipoprotein receptor (LDLR) is a receptor that is responsible for clearing low-density lipoprotein cholesterol (LDL-C) from the blood. PCSK9 cleaves the intracellular domain of LDLR on the cell surface, causing it to detach from the cell membrane and be transported to the lysosome for degradation, promoting LDLR degradation, and increasing plasma LDL-C. Overexpression or gain-of-function mutations of the PCSK9 gene can lead to LDL-C accumulation by reducing LDLR levels. This can cause hypercholesterolemia, which increases the risk of cardiovascular diseases, such as atherosclerosis and coronary heart disease, and neurodegenerative diseases, such as Alzheimer's disease [6]. PCSK9 has emerged as a key target for the development of lipid-lowering drugs. Several PCSK9-targeted antibodies or small nucleic acid drugs have been approved for marketing worldwide, including evolocumab from Amgen, alirocumab from Sanofi and Regeneron, and inclisiran from Novartis. These drugs primarily work by inhibiting PCSK9 activity or preventing PCSK9 protein from binding to LDLR, lowering LDL-C levels in the blood to treat hypercholesterolemia [7-8]. In addition, PCSK9 can promote tumor growth and development by regulating cell proliferation, migration, and invasion. It can also regulate the expression of inflammatory factors that contribute to inflammation. Therefore, targeting the expression of PCSK9 has been investigated in tumor immunotherapy and autoimmune disease therapy [9-10].
The B6-hLPA (CKI)/Alb-cre/hPCSK9 mouse model is generated by crossing B6-hLPA (CKI) mice (Catalog No.: C001521, a mouse strain with conditional expression of the human LPA gene), Alb-Cre mice (liver-specific Cre-expressing mice), and B6-hPCSK9 mice (Catalog No.: C001617). This model harbors two cardiovascular disease risk factors, namely Lp (a) (lipoprotein (a)) and PCSK9, making it suitable for research on hyperlipidemia, stroke, coronary heart disease, and other atherosclerotic cardiovascular diseases (ASCVD).
B6-huSLC16A1
製品ID :
C001915
系統:
C57BL/6NCya
状況:
説明:
The SLC16A1 gene encodes the Monocarboxylate Transporter 1 (MCT1) protein, a vital proton-coupled symporter that facilitates the rapid transmembrane movement of metabolic substrates, including lactate, pyruvate, and ketone bodies (acetoacetate and β-hydroxybutyrate). This gene is ubiquitously expressed across nearly all human tissues to maintain energy balance and pH homeostasis, with notably high levels labeled in the heart, oxidative skeletal muscle fibers, erythrocytes (red blood cells), and the brain (specifically in oligodendrocytes and the blood-brain barrier), while being uniquely "disallowed" or suppressed in normal pancreatic beta-cells to prevent inappropriate insulin release [1]. Functionally, MCT1 is central to the "lactate shuttle" mechanism, allowing tissues to coordinate metabolic fuel exchange by facilitating either the influx or efflux of substrates depending on the concentration gradient and proton motive force [2]. Mutations in SLC16A1 are clinically linked to Erythrocyte Lactate Transporter Defect, which causes exercise-induced muscle cramping and fatigue, and Monocarboxylate Transporter 1 Deficiency, a rare disorder characterized by recurrent episodes of severe ketoacidosis and vomiting triggered by fasting or infection [3]. Conversely, gain-of-function mutations in the gene's promoter lead to familial hyperinsulinemia type 7 (HHF7), where exercise triggers excessive insulin secretion, while its widespread overexpression in various cancers (such as melanoma and lung cancer) supports the Warburg effect by managing lactate efflux to prevent intracellular acidification and fueling tumor progression [4].
The B6-huSLC16A1 mouse is a humanized model constructed through gene-editing technology, in which the sequences from the ATG start codon to the TGA stop codon of the endogenous mouse Slc16a1 gene are replaced with the sequences from the ATG start codon to the TGA stop codon of the human SLC16A1 gene. This model can be used for research on diseases such as Erythrocyte Lactate Transporter Defect, Monocarboxylate Transporter 1 Deficiency, familial hyperinsulinemia type 7 (HHF7), and various cancers, as well as for screening, development, and preclinical evaluation of SLC16A1-targeted therapeutics.
The SLC16A1 gene encodes the Monocarboxylate Transporter 1 (MCT1) protein, a vital proton-coupled symporter that facilitates the rapid transmembrane movement of metabolic substrates, including lactate, pyruvate, and ketone bodies (acetoacetate and β-hydroxybutyrate). This gene is ubiquitously expressed across nearly all human tissues to maintain energy balance and pH homeostasis, with notably high levels labeled in the heart, oxidative skeletal muscle fibers, erythrocytes (red blood cells), and the brain (specifically in oligodendrocytes and the blood-brain barrier), while being uniquely "disallowed" or suppressed in normal pancreatic beta-cells to prevent inappropriate insulin release [1]. Functionally, MCT1 is central to the "lactate shuttle" mechanism, allowing tissues to coordinate metabolic fuel exchange by facilitating either the influx or efflux of substrates depending on the concentration gradient and proton motive force [2]. Mutations in SLC16A1 are clinically linked to Erythrocyte Lactate Transporter Defect, which causes exercise-induced muscle cramping and fatigue, and Monocarboxylate Transporter 1 Deficiency, a rare disorder characterized by recurrent episodes of severe ketoacidosis and vomiting triggered by fasting or infection [3]. Conversely, gain-of-function mutations in the gene's promoter lead to familial hyperinsulinemia type 7 (HHF7), where exercise triggers excessive insulin secretion, while its widespread overexpression in various cancers (such as melanoma and lung cancer) supports the Warburg effect by managing lactate efflux to prevent intracellular acidification and fueling tumor progression [4].
The B6-huSLC16A1 mouse is a humanized model constructed through gene-editing technology, in which the sequences from the ATG start codon to the TGA stop codon of the endogenous mouse Slc16a1 gene are replaced with the sequences from the ATG start codon to the TGA stop codon of the human SLC16A1 gene. This model can be used for research on diseases such as Erythrocyte Lactate Transporter Defect, Monocarboxylate Transporter 1 Deficiency, familial hyperinsulinemia type 7 (HHF7), and various cancers, as well as for screening, development, and preclinical evaluation of SLC16A1-targeted therapeutics.
B6-Uox KO/huURAT1
製品ID :
C001937
系統:
C57BL/6Cya
状況:
説明:
B6-Uox KO/huURAT1 mice are humanized disease models obtained by crossing Uox KO mice (catalog No.: C001232) with B6-huURAT1 mice (catalog No.: C001704). This model can be used for studying the pathological mechanisms and treatment methods of uric acid metabolism-related diseases such as hyperuricemia and gout, as well as for screening and developing URAT1-targeted therapies and evaluating preclinical efficacy and safety. It is worth noting that heterozygous Uox KO mice can survive and are fertile, while homozygous Uox KO mice need to be maintained with drugs such as Allopurinol after birth.
B6-Uox KO/huURAT1 mice are humanized disease models obtained by crossing Uox KO mice (catalog No.: C001232) with B6-huURAT1 mice (catalog No.: C001704). This model can be used for studying the pathological mechanisms and treatment methods of uric acid metabolism-related diseases such as hyperuricemia and gout, as well as for screening and developing URAT1-targeted therapies and evaluating preclinical efficacy and safety. It is worth noting that heterozygous Uox KO mice can survive and are fertile, while homozygous Uox KO mice need to be maintained with drugs such as Allopurinol after birth.
B6-Uox KO/huXDH
製品ID :
C001938
系統:
C57BL/6Cya
状況:
説明:
The B6-Uox KO/huXDH mice are humanized disease models obtained by mating Uox KO mice (catalog No.: C001232) with B6-huXDH mice (catalog No.: C001586). This model is suitable for studying the pathological mechanisms of hyperuricemia and gout, and provides an ideal preclinical research platform for the development of novel xanthine oxidase inhibitors and small nucleic acid therapies. It is worth noting that heterozygous Uox KO mice can survive and are fertile, while homozygous Uox KO mice require drugs such as Allopurinol to maintain their survival after birth.
The B6-Uox KO/huXDH mice are humanized disease models obtained by mating Uox KO mice (catalog No.: C001232) with B6-huXDH mice (catalog No.: C001586). This model is suitable for studying the pathological mechanisms of hyperuricemia and gout, and provides an ideal preclinical research platform for the development of novel xanthine oxidase inhibitors and small nucleic acid therapies. It is worth noting that heterozygous Uox KO mice can survive and are fertile, while homozygous Uox KO mice require drugs such as Allopurinol to maintain their survival after birth.
huMSTN(GDF8)
製品ID :
C001636
系統:
C57BL/6NCya
状況:
説明:
The MSTN gene, also known as growth differentiation factor 8 (GDF8), encodes myostatin, a secreted protein belonging to the transforming growth factor-β (TGF-β) superfamily [1]. MSTN is primarily expressed in skeletal muscle, with low-level expression also detected in myocardium, adipose tissue, and brain tissue. It encodes the myostatin protein, a key negative regulator of skeletal muscle development [1]. Myostatin, through autocrine and paracrine signaling, inhibits muscle cell proliferation and differentiation, thereby limiting excessive skeletal muscle growth and maintaining muscle mass homeostasis [1-4]. Thus, MSTN plays a critical role in regulating body muscle development and maintaining normal muscle mass [3]. Furthermore, myostatin is implicated in adipogenesis regulation, exerting an inhibitory effect on fat cell differentiation [2]. Mutations in MSTN are associated with myostatin-related muscle hypertrophy, characterized by significant increases in muscle volume and strength, typically without severe medical consequences [5]. Consequently, inhibitors targeting myostatin are considered potential therapeutic targets for diseases such as muscular dystrophy and sarcopenia, and have shown promise in improving metabolic syndrome [1-5].
The huMSTN(GDF8) mouse is a humanized model constructed using gene editing technology, where the mouse Mstn genomic DNA was replaced with the human MSTN genomic DNA. The murine signal peptide was preserved. This model can be used for studying the pathological mechanisms and therapeutic approaches of muscular dystrophy, sarcopenia, and metabolic syndrome, and for the development of MSTN-targeted drugs.
The MSTN gene, also known as growth differentiation factor 8 (GDF8), encodes myostatin, a secreted protein belonging to the transforming growth factor-β (TGF-β) superfamily [1]. MSTN is primarily expressed in skeletal muscle, with low-level expression also detected in myocardium, adipose tissue, and brain tissue. It encodes the myostatin protein, a key negative regulator of skeletal muscle development [1]. Myostatin, through autocrine and paracrine signaling, inhibits muscle cell proliferation and differentiation, thereby limiting excessive skeletal muscle growth and maintaining muscle mass homeostasis [1-4]. Thus, MSTN plays a critical role in regulating body muscle development and maintaining normal muscle mass [3]. Furthermore, myostatin is implicated in adipogenesis regulation, exerting an inhibitory effect on fat cell differentiation [2]. Mutations in MSTN are associated with myostatin-related muscle hypertrophy, characterized by significant increases in muscle volume and strength, typically without severe medical consequences [5]. Consequently, inhibitors targeting myostatin are considered potential therapeutic targets for diseases such as muscular dystrophy and sarcopenia, and have shown promise in improving metabolic syndrome [1-5].
The huMSTN(GDF8) mouse is a humanized model constructed using gene editing technology, where the mouse Mstn genomic DNA was replaced with the human MSTN genomic DNA. The murine signal peptide was preserved. This model can be used for studying the pathological mechanisms and therapeutic approaches of muscular dystrophy, sarcopenia, and metabolic syndrome, and for the development of MSTN-targeted drugs.
H11-Alb-hHSD17B13(2)
製品ID :
C002122
系統:
C57BL/6Cya
状況:
説明:
17β-hydroxysteroid dehydrogenase 13 (HSD17B13) is a liver-enriched lipid droplet (LD)-associated protein that catalyzes the interconversion between 17-ketosteroids and 17-hydroxysteroids. HSD17B13 protein is selectively expressed in liver cells and localizes exclusively to the surface of lipid droplets, with similar tissue distribution and subcellular localization observed in both humans and mice [1]. HSD17B13 may play a significant role in regulating the biogenesis, growth, and degradation of lipid droplets in the liver. Metabolic-associated fatty liver disease (MAFLD) is pathologically defined by abnormal accumulation of neutral lipids (such as triglycerides and cholesterol esters) within hepatocellular lipid droplets. Its inflammatory form, metabolic-associated steatohepatitis (MASH), is closely associated with the pathogenesis of chronic liver diseases. Research has found that HSD17B13 protein expression is markedly elevated in the livers of MAFLD patients compared to healthy individuals [2-3]. Abnormal expression and dysfunction of HSD17B13 may be one of the pathogenic mechanisms of chronic liver disease, particularly in the MAFLD. As a potential therapeutic target for MAFLD and MASH, there are currently clinical-stage drug pipelines targeting the HSD17B13 gene, including siRNA drug Rapirosiran developed by Regeneron Pharmaceuticals.
The H11-Alb-hHSD17B13(2) mouse model is generated by integrating the "Alb promoter-5'UTR of Human HSD17B13-Human HSD17B13 CDS-3'UTR of Human HSD17B13-WPRE-BGH pA" cassette into the mouse H11 safe harbor locus. This model can be used to study the pathogenic mechanisms of the HSD17B13 gene in metabolic-associated fatty liver disease (MAFLD) and related chronic liver diseases, as well as for evaluating targeted drug development.
17β-hydroxysteroid dehydrogenase 13 (HSD17B13) is a liver-enriched lipid droplet (LD)-associated protein that catalyzes the interconversion between 17-ketosteroids and 17-hydroxysteroids. HSD17B13 protein is selectively expressed in liver cells and localizes exclusively to the surface of lipid droplets, with similar tissue distribution and subcellular localization observed in both humans and mice [1]. HSD17B13 may play a significant role in regulating the biogenesis, growth, and degradation of lipid droplets in the liver. Metabolic-associated fatty liver disease (MAFLD) is pathologically defined by abnormal accumulation of neutral lipids (such as triglycerides and cholesterol esters) within hepatocellular lipid droplets. Its inflammatory form, metabolic-associated steatohepatitis (MASH), is closely associated with the pathogenesis of chronic liver diseases. Research has found that HSD17B13 protein expression is markedly elevated in the livers of MAFLD patients compared to healthy individuals [2-3]. Abnormal expression and dysfunction of HSD17B13 may be one of the pathogenic mechanisms of chronic liver disease, particularly in the MAFLD. As a potential therapeutic target for MAFLD and MASH, there are currently clinical-stage drug pipelines targeting the HSD17B13 gene, including siRNA drug Rapirosiran developed by Regeneron Pharmaceuticals.
The H11-Alb-hHSD17B13(2) mouse model is generated by integrating the "Alb promoter-5'UTR of Human HSD17B13-Human HSD17B13 CDS-3'UTR of Human HSD17B13-WPRE-BGH pA" cassette into the mouse H11 safe harbor locus. This model can be used to study the pathogenic mechanisms of the HSD17B13 gene in metabolic-associated fatty liver disease (MAFLD) and related chronic liver diseases, as well as for evaluating targeted drug development.
H11-Alb-hLPA
製品ID :
C001542
系統:
C57BL/6NCya
状況:
説明:
Lipoprotein(a) (Lp(a)) is a lipoprotein particle consisting of apolipoprotein(a) (Apo(a)) bound to low-density lipoprotein (LDL) containing apolipoprotein B (ApoB), where the LPA gene encoding for Apo(a) is only found in the genomes of humans and some non-human primates. LP(a) is similar in size and lipid content to low-density lipoprotein (LDL) and is considered a new risk factor for several cardiovascular diseases (CVD), including atherosclerosis, coronary heart disease, and stroke [1]. Lp(a) differs from LDL in that it contains an additional variable-length Apo(a), which covalently binds to ApoB-100 via a single disulfide bond. Lp(a) plays a crucial role in systemic lipid transport, guiding inflammatory cells into blood vessel walls and promoting smooth muscle cell proliferation. Additionally, it participates in wound healing and tissue repair, interacting with components of the blood vessel wall and extracellular matrix [2]. However, Lp(a) can also cause arterial narrowing by adhering to the arterial wall, accelerating blood clot formation, and triggering pathological changes related to coronary heart disease, atherosclerosis, thrombosis, and stroke [3]. The plasma concentration of Lp(a) is closely related to genetic factors, primarily regulated by the LPA gene. Consequently, the LPA gene represents an important potential target for cardiovascular disease treatment. Currently, several novel therapies aimed at modulating LPA gene transcription rates are under development, including small interfering RNA (siRNA) and antisense oligonucleotide (ASO) drugs [4]. Given that the LPA gene is expressed only in humans and some non-human primates but not in mice, constructing a mouse model expressing the human LPA gene is crucial for the preclinical evaluation of lipid-lowering drugs.
The H11-Alb-hLPA mouse is a humanized model where the human LPA protein coding sequence (CDS) is integrated into the mouse H11 safe harbor locus. In this model, the human LPA gene is specifically expressed in the liver under the control of the mouse Alb promoter. It can be used to study the pathogenic mechanisms of the LPA gene in hyperlipidemia and related cardiovascular diseases, as well as to evaluate targeted drug development. Additionally, Cyagen has developed a conditionally inducible LPA humanization model (catalog number: C001521) using the CAG promoter. When crossed with Alb-Cre mice (liver-specific Cre mice), the resulting LPA-humanized mice (catalog number: C001522) exhibit significantly higher LPA protein levels compared to the H11-Alb-hLPA mice. Therefore, researchers please choose the appropriate mouse strain based on their specific requirements for LPA protein expression levels and genetic characteristics.
Lipoprotein(a) (Lp(a)) is a lipoprotein particle consisting of apolipoprotein(a) (Apo(a)) bound to low-density lipoprotein (LDL) containing apolipoprotein B (ApoB), where the LPA gene encoding for Apo(a) is only found in the genomes of humans and some non-human primates. LP(a) is similar in size and lipid content to low-density lipoprotein (LDL) and is considered a new risk factor for several cardiovascular diseases (CVD), including atherosclerosis, coronary heart disease, and stroke [1]. Lp(a) differs from LDL in that it contains an additional variable-length Apo(a), which covalently binds to ApoB-100 via a single disulfide bond. Lp(a) plays a crucial role in systemic lipid transport, guiding inflammatory cells into blood vessel walls and promoting smooth muscle cell proliferation. Additionally, it participates in wound healing and tissue repair, interacting with components of the blood vessel wall and extracellular matrix [2]. However, Lp(a) can also cause arterial narrowing by adhering to the arterial wall, accelerating blood clot formation, and triggering pathological changes related to coronary heart disease, atherosclerosis, thrombosis, and stroke [3]. The plasma concentration of Lp(a) is closely related to genetic factors, primarily regulated by the LPA gene. Consequently, the LPA gene represents an important potential target for cardiovascular disease treatment. Currently, several novel therapies aimed at modulating LPA gene transcription rates are under development, including small interfering RNA (siRNA) and antisense oligonucleotide (ASO) drugs [4]. Given that the LPA gene is expressed only in humans and some non-human primates but not in mice, constructing a mouse model expressing the human LPA gene is crucial for the preclinical evaluation of lipid-lowering drugs.
The H11-Alb-hLPA mouse is a humanized model where the human LPA protein coding sequence (CDS) is integrated into the mouse H11 safe harbor locus. In this model, the human LPA gene is specifically expressed in the liver under the control of the mouse Alb promoter. It can be used to study the pathogenic mechanisms of the LPA gene in hyperlipidemia and related cardiovascular diseases, as well as to evaluate targeted drug development. Additionally, Cyagen has developed a conditionally inducible LPA humanization model (catalog number: C001521) using the CAG promoter. When crossed with Alb-Cre mice (liver-specific Cre mice), the resulting LPA-humanized mice (catalog number: C001522) exhibit significantly higher LPA protein levels compared to the H11-Alb-hLPA mice. Therefore, researchers please choose the appropriate mouse strain based on their specific requirements for LPA protein expression levels and genetic characteristics.
huURAT1
製品ID :
C001704
系統:
C57BL/6NCya
状況:
説明:
The solute carrier family 22 member 12 gene ( SLC22A12) encodes the Urate Transporter 1 (URAT1), a critical transmembrane protein localized to the apical membrane of renal proximal tubule epithelial cells [1]. As the primary mediator of urate reabsorption from the glomerular filtrate, URAT1 plays a pivotal role in maintaining systemic urate homeostasis, a process essential for preventing hyperuricemia and its associated pathologies [2]. Genetic studies have identified numerous variants within SLC22A12 that are strongly linked to renal hypouricemia, characterized by impaired urate reabsorption and an increased risk of exercise-induced acute kidney injury [3]. Furthermore, polymorphisms in SLC22A12 influence the efficacy of uricosuric agents, highlighting its clinical relevance in the management of gout, a common inflammatory arthritis resulting from urate crystal deposition [4]. The functional importance of URAT1 underscores SLC22A12 as a key genetic determinant of urate metabolism and a significant factor in kidney health and disease.
huURAT1 mice are humanized models in which the sequences from upstream of exon 1 to exon 10 of the mouse Slc22a12 gene were replaced with the sequences from upstream of exon 1 to exon 10 of the human SLC22A12 gene. This model can be used to study the pathological mechanisms and therapeutic methods of renal hypouricemia, gout, and other uric acid metabolism-related diseases, as well as the screening and development of URAT1-targeted drugs, and preclinical efficacy and safety evaluations.
The solute carrier family 22 member 12 gene ( SLC22A12) encodes the Urate Transporter 1 (URAT1), a critical transmembrane protein localized to the apical membrane of renal proximal tubule epithelial cells [1]. As the primary mediator of urate reabsorption from the glomerular filtrate, URAT1 plays a pivotal role in maintaining systemic urate homeostasis, a process essential for preventing hyperuricemia and its associated pathologies [2]. Genetic studies have identified numerous variants within SLC22A12 that are strongly linked to renal hypouricemia, characterized by impaired urate reabsorption and an increased risk of exercise-induced acute kidney injury [3]. Furthermore, polymorphisms in SLC22A12 influence the efficacy of uricosuric agents, highlighting its clinical relevance in the management of gout, a common inflammatory arthritis resulting from urate crystal deposition [4]. The functional importance of URAT1 underscores SLC22A12 as a key genetic determinant of urate metabolism and a significant factor in kidney health and disease.
huURAT1 mice are humanized models in which the sequences from upstream of exon 1 to exon 10 of the mouse Slc22a12 gene were replaced with the sequences from upstream of exon 1 to exon 10 of the human SLC22A12 gene. This model can be used to study the pathological mechanisms and therapeutic methods of renal hypouricemia, gout, and other uric acid metabolism-related diseases, as well as the screening and development of URAT1-targeted drugs, and preclinical efficacy and safety evaluations.
huSCAP
製品ID :
C001950
系統:
C57BL/6NCya
状況:
説明:
The SCAP gene (SREBP cleavage-activating protein) encodes a critical regulatory protein that functions as a sterol sensor and escort within the cell. Primarily expressed in the liver, brain, and endocrine tissues, the SCAP protein resides in the endoplasmic reticulum (ER) membrane, where it forms a complex with SREBP (Sterol Regulatory Element-Binding Protein) [1]. When cellular cholesterol levels are low, SCAP undergoes a conformational change that allows it to escort SREBPs to the Golgi apparatus for activation, thereby triggering the expression of genes involved in lipid synthesis [2]. Conversely, high sterol levels cause SCAP to bind to INSIG proteins, anchoring the complex in the ER and halting lipid production [3]. Due to its central role in metabolic homeostasis, dysregulation of the SCAP gene is associated with metabolic syndrome, non-alcoholic fatty liver disease (NAFLD), and hyperlipidemia, while specific mutations have been linked to autosomal dominant hypercholesterolemia.
huSCAP mice are humanized models generated using gene editing technology by replacing the sequences from upstream of exon 1 to 3’UTR of the mouse Scap gene with the sequences from upstream of exon 1 to 3’UTR of the human SCAP gene. This strain can be used for studying the pathological mechanisms and treatments of metabolic syndrome, non-alcoholic fatty liver disease (NAFLD), autosomal dominant hypercholesterolemia, and hyperlipidemia, as well as for the development of SCAP-targeted drugs.
The SCAP gene (SREBP cleavage-activating protein) encodes a critical regulatory protein that functions as a sterol sensor and escort within the cell. Primarily expressed in the liver, brain, and endocrine tissues, the SCAP protein resides in the endoplasmic reticulum (ER) membrane, where it forms a complex with SREBP (Sterol Regulatory Element-Binding Protein) [1]. When cellular cholesterol levels are low, SCAP undergoes a conformational change that allows it to escort SREBPs to the Golgi apparatus for activation, thereby triggering the expression of genes involved in lipid synthesis [2]. Conversely, high sterol levels cause SCAP to bind to INSIG proteins, anchoring the complex in the ER and halting lipid production [3]. Due to its central role in metabolic homeostasis, dysregulation of the SCAP gene is associated with metabolic syndrome, non-alcoholic fatty liver disease (NAFLD), and hyperlipidemia, while specific mutations have been linked to autosomal dominant hypercholesterolemia.
huSCAP mice are humanized models generated using gene editing technology by replacing the sequences from upstream of exon 1 to 3’UTR of the mouse Scap gene with the sequences from upstream of exon 1 to 3’UTR of the human SCAP gene. This strain can be used for studying the pathological mechanisms and treatments of metabolic syndrome, non-alcoholic fatty liver disease (NAFLD), autosomal dominant hypercholesterolemia, and hyperlipidemia, as well as for the development of SCAP-targeted drugs.
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