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Alb-Cre+/hMYC-IRES-EGFP+
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+/hMYC-IRES-EGFP+ 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+/hMYC-IRES-EGFP+ 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.
hSCN9A(SD)
製品ID :
CR013
系統:
SD
状況:
説明:
The SCN9A gene, which encodes the voltage-gated sodium channel protein Nav1.7, is an important pathogenic factor underlying peripheral neuropathic pain and related rare diseases. Nav1.7 sodium channels mediate the influx of positively charged sodium ions into cells and play a critical role in the generation and propagation of action potentials. Studies have shown that genetic variants in SCN9A are closely associated with multiple inherited pain disorders, including erythromelalgia, small fiber neuropathy, and congenital insensitivity to pain [1-2]. As a voltage-gated sodium channel, the Nav1.7 protein is predominantly expressed in sensory and sympathetic neurons of the peripheral nervous system, with particularly high expression in dorsal root ganglia, where it plays an essential role in the generation and transmission of pain signals [3]. Research indicates that down-regulation of SCN9A expression or selective inhibition of Nav1.7 holds promise as a novel and highly effective analgesic strategy for the treatment of acute, inflammatory, and neuropathic pain [4].
Currently, drug development targeting SCN9A/Nav1.7 continues to advance and encompasses multiple modalities, including small-molecule inhibitors, epigenetic regulation, gene therapy, and biologic agents. Several companies have established relevant pipelines; for example, raxatrigine from GSK has entered Phase III clinical trials for trigeminal neuralgia, while Xenon Pharmaceuticals, Vertex Pharmaceuticals, and others are actively progressing selective Nav1.7 inhibitors in preclinical and early clinical stages [5].
hSCN9A(SD) rat is a humanized Scn9a model generated by gene-editing technology. The coding sequence of exon 2 to partial intron 7 of rat Scn9a was replaced with the Kozak-Human SCN9A CDS-3'UTR of Human SCN9A-WPRE-BGH pA cassette. This model can be used for investigating the pathogenic mechanisms of inherited pain disorders such as erythromelalgia, small fiber neuropathy, and congenital insensitivity to pain, as well as for the preclinical research, screening, and evaluation of Nav1.7-targeted analgesic candidates.
The SCN9A gene, which encodes the voltage-gated sodium channel protein Nav1.7, is an important pathogenic factor underlying peripheral neuropathic pain and related rare diseases. Nav1.7 sodium channels mediate the influx of positively charged sodium ions into cells and play a critical role in the generation and propagation of action potentials. Studies have shown that genetic variants in SCN9A are closely associated with multiple inherited pain disorders, including erythromelalgia, small fiber neuropathy, and congenital insensitivity to pain [1-2]. As a voltage-gated sodium channel, the Nav1.7 protein is predominantly expressed in sensory and sympathetic neurons of the peripheral nervous system, with particularly high expression in dorsal root ganglia, where it plays an essential role in the generation and transmission of pain signals [3]. Research indicates that down-regulation of SCN9A expression or selective inhibition of Nav1.7 holds promise as a novel and highly effective analgesic strategy for the treatment of acute, inflammatory, and neuropathic pain [4].
Currently, drug development targeting SCN9A/Nav1.7 continues to advance and encompasses multiple modalities, including small-molecule inhibitors, epigenetic regulation, gene therapy, and biologic agents. Several companies have established relevant pipelines; for example, raxatrigine from GSK has entered Phase III clinical trials for trigeminal neuralgia, while Xenon Pharmaceuticals, Vertex Pharmaceuticals, and others are actively progressing selective Nav1.7 inhibitors in preclinical and early clinical stages [5].
hSCN9A(SD) rat is a humanized Scn9a model generated by gene-editing technology. The coding sequence of exon 2 to partial intron 7 of rat Scn9a was replaced with the Kozak-Human SCN9A CDS-3'UTR of Human SCN9A-WPRE-BGH pA cassette. This model can be used for investigating the pathogenic mechanisms of inherited pain disorders such as erythromelalgia, small fiber neuropathy, and congenital insensitivity to pain, as well as for the preclinical research, screening, and evaluation of Nav1.7-targeted analgesic candidates.
huCALCRL
製品ID :
C001497
系統:
C57BL/6JCya
状況:
説明:
Calcitonin receptor-like receptor (CALCRL) is a seven-transmembrane G protein-coupled receptor encoded by the CALCRL gene. It mediates the pleiotropic effects of calcitonin gene-related peptide (CGRP) and adrenal medullary peptide (ADM), two structurally related neuropeptides that are potent vasodilators and play an important role in blood pressure regulation [1]. In addition, CALCRL is involved in various other biological processes, including cell proliferation, cell death regulation, vascular biology, and inflammation [2]. CALCRL is currently being investigated as a new target for the treatment of migraine [3]. In solid tumors, antibodies that target CALCRL have been shown to reduce tumor growth by either disrupting angiogenesis or by directly inhibiting cancer cell proliferation [4]. CALCRL is also expressed in normal CD34+ hematopoietic progenitor cells, and CGRP and ADM can directly stimulate these cells to form colonies in vitro, suggesting a role for CALCRL in physiological bone marrow generation [5].
This strain represents a humanized mouse model of the Calcrl gene. Using gene editing technology, the sequence encoding the extracellular domain of the mouse Calcrl gene was replaced with the corresponding sequence from the human CALCRL gene. This model can be used to study the mechanisms of various physiological and pathological processes, such as blood pressure regulation, cell proliferation, cell death, vascular biology, physiological bone marrow generation, inflammation, and tumor growth, as well as the development of CALCRL-targeted migraine drugs and therapies. Homozygous huCALCRL mice are viable and fertile.
Calcitonin receptor-like receptor (CALCRL) is a seven-transmembrane G protein-coupled receptor encoded by the CALCRL gene. It mediates the pleiotropic effects of calcitonin gene-related peptide (CGRP) and adrenal medullary peptide (ADM), two structurally related neuropeptides that are potent vasodilators and play an important role in blood pressure regulation [1]. In addition, CALCRL is involved in various other biological processes, including cell proliferation, cell death regulation, vascular biology, and inflammation [2]. CALCRL is currently being investigated as a new target for the treatment of migraine [3]. In solid tumors, antibodies that target CALCRL have been shown to reduce tumor growth by either disrupting angiogenesis or by directly inhibiting cancer cell proliferation [4]. CALCRL is also expressed in normal CD34+ hematopoietic progenitor cells, and CGRP and ADM can directly stimulate these cells to form colonies in vitro, suggesting a role for CALCRL in physiological bone marrow generation [5].
This strain represents a humanized mouse model of the Calcrl gene. Using gene editing technology, the sequence encoding the extracellular domain of the mouse Calcrl gene was replaced with the corresponding sequence from the human CALCRL gene. This model can be used to study the mechanisms of various physiological and pathological processes, such as blood pressure regulation, cell proliferation, cell death, vascular biology, physiological bone marrow generation, inflammation, and tumor growth, as well as the development of CALCRL-targeted migraine drugs and therapies. Homozygous huCALCRL mice are viable and fertile.
huCALCA
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 huCALCA 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 huCALCA 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.
huAPOC3-Tg
製品ID :
C001588
系統:
C57BL/6NCya
状況:
説明:
Apolipoprotein C-III (ApoC-III), encoded by the APOC3 gene, is a 79-amino acid glycoprotein primarily synthesized in the liver, with minor production in the intestine. ApoC-III is a key component of triglyceride-rich lipoproteins (TRLs), including chylomicrons and very low-density lipoprotein (VLDL). Its primary functions include inhibiting lipoprotein lipase (LPL)-mediated hydrolysis of triglycerides within TRLs and modulating hepatic uptake of TRL remnants, thereby elevating plasma triglyceride levels. Consequently, ApoC-III is crucial in regulating plasma triglyceride levels [1-2]. Elevated APOC3 expression leads to increased ApoC-III levels, which is associated with hypertriglyceridemia (a risk factor for cardiovascular disease) and conditions such as familial hypertriglyceridemia, metabolic syndrome, and type 2 diabetes. Therefore, targeting the reduction of APOC3 expression or blocking its protein function offers a therapeutic avenue for hypertriglyceridemia and mitigating cardiovascular disease risk [3].
The huAPOC3-Tg mouse is a humanized model generated by integrating the human APOC3 gene sequence, encompassing the upstream and downstream untranslated regions (UTRs), into the mouse genome, enabling the expression of human ApoC-III protein in vivo. This model is valuable for developing therapeutics targeting human APOC3, such as small interfering RNA (siRNA) and antisense oligonucleotides (ASOs), for the treatment of hypertriglyceridemia.
Apolipoprotein C-III (ApoC-III), encoded by the APOC3 gene, is a 79-amino acid glycoprotein primarily synthesized in the liver, with minor production in the intestine. ApoC-III is a key component of triglyceride-rich lipoproteins (TRLs), including chylomicrons and very low-density lipoprotein (VLDL). Its primary functions include inhibiting lipoprotein lipase (LPL)-mediated hydrolysis of triglycerides within TRLs and modulating hepatic uptake of TRL remnants, thereby elevating plasma triglyceride levels. Consequently, ApoC-III is crucial in regulating plasma triglyceride levels [1-2]. Elevated APOC3 expression leads to increased ApoC-III levels, which is associated with hypertriglyceridemia (a risk factor for cardiovascular disease) and conditions such as familial hypertriglyceridemia, metabolic syndrome, and type 2 diabetes. Therefore, targeting the reduction of APOC3 expression or blocking its protein function offers a therapeutic avenue for hypertriglyceridemia and mitigating cardiovascular disease risk [3].
The huAPOC3-Tg mouse is a humanized model generated by integrating the human APOC3 gene sequence, encompassing the upstream and downstream untranslated regions (UTRs), into the mouse genome, enabling the expression of human ApoC-III protein in vivo. This model is valuable for developing therapeutics targeting human APOC3, such as small interfering RNA (siRNA) and antisense oligonucleotides (ASOs), for the treatment of hypertriglyceridemia.
huALB(HSA)/hTFRC
製品ID :
C001730
系統:
C57BL/6NCya
状況:
説明:
The ALB gene encodes albumin, mainly produced in the liver, and is the most abundant protein in human plasma, accounting for 60% to 65% of total plasma protein. The proprotein encoded by ALB is processed to produce a functional protein, and the EPI-X4 peptide derived from this protein is an endogenous inhibitor of the CXCR4 chemokine receptor. Albumin plays a role in regulating plasma colloid osmotic pressure, helping to maintain blood circulation and isolating and transporting many metabolites within the body, especially insoluble hydrophobic metabolites [1]. Human Serum Albumin (HSA) is an important carrier protein involved in the transport of a variety of endogenous molecules, including hormones, fatty acids, and metabolic products, as well as exogenous drugs. As a natural carrier protein, HSA has multiple ligand binding sites and a plasma half-life of up to 19 days, making it a promising drug carrier. Several HSA-based drug delivery systems have been approved for clinical trials [2-3]. In addition, albumin is also the main transporter of zinc, calcium, and magnesium in plasma, binding approximately 80% of all plasma zinc and approximately 45% of circulating calcium and magnesium, with an affinity ranking of zinc > calcium > magnesium [4]. Diseases associated with the ALB gene include hyperthyroxinemia, familial serum albumin abnormality, and analbuminemia [5].
The Transferrin receptor (TFRC) gene encodes Transferrin Receptor 1 (TFR1), a protein that is expressed at low levels in most normal cells but shows increased expression in highly proliferative cells, such as basal epidermal cells, intestinal epithelium, and certain activated immune cells. Brain capillary endothelial cells, which constitute the blood-brain barrier (BBB), also express this receptor at high levels [6]. TFR1 plays a critical role in maintaining iron metabolism and homeostasis by facilitating receptor-mediated endocytosis of iron-bound transferrin (Tf) via Tf cycling, thereby promoting iron uptake [7]. Cellular iron deficiency can lead to apoptosis, while cellular transformation requires substantial iron to sustain proliferation, with iron overload contributing to tumor progression. The high expression of TFR1 in many tumors makes it a potential tumor marker, offering a target for therapies to inhibit tumor growth and metastasis [6]. Moreover, TFR1 is implicated in anemia and iron metabolism disorders. Studies have shown that elevated TFR1 expression in cardiomyocytes is associated with exacerbated inflammation in myocarditis patients [8].
huALB(HSA)/hTFRC mice are a dual gene humanized model of Alb and Tfrc, obtained by crossing huALB(HSA) mice (Catalog number: C001492) with hTFRC mice (Catalog number: C001584). This model can be used for the development of ALB/TFRC-targeted therapeutic drugs, as well as for the research on drug development using human serum albumin (HSA) as a carrier or drug delivery across the blood-brain barrier (BBB), and for in vivo pharmacodynamic and pharmacokinetic studies.
The ALB gene encodes albumin, mainly produced in the liver, and is the most abundant protein in human plasma, accounting for 60% to 65% of total plasma protein. The proprotein encoded by ALB is processed to produce a functional protein, and the EPI-X4 peptide derived from this protein is an endogenous inhibitor of the CXCR4 chemokine receptor. Albumin plays a role in regulating plasma colloid osmotic pressure, helping to maintain blood circulation and isolating and transporting many metabolites within the body, especially insoluble hydrophobic metabolites [1]. Human Serum Albumin (HSA) is an important carrier protein involved in the transport of a variety of endogenous molecules, including hormones, fatty acids, and metabolic products, as well as exogenous drugs. As a natural carrier protein, HSA has multiple ligand binding sites and a plasma half-life of up to 19 days, making it a promising drug carrier. Several HSA-based drug delivery systems have been approved for clinical trials [2-3]. In addition, albumin is also the main transporter of zinc, calcium, and magnesium in plasma, binding approximately 80% of all plasma zinc and approximately 45% of circulating calcium and magnesium, with an affinity ranking of zinc > calcium > magnesium [4]. Diseases associated with the ALB gene include hyperthyroxinemia, familial serum albumin abnormality, and analbuminemia [5].
The Transferrin receptor (TFRC) gene encodes Transferrin Receptor 1 (TFR1), a protein that is expressed at low levels in most normal cells but shows increased expression in highly proliferative cells, such as basal epidermal cells, intestinal epithelium, and certain activated immune cells. Brain capillary endothelial cells, which constitute the blood-brain barrier (BBB), also express this receptor at high levels [6]. TFR1 plays a critical role in maintaining iron metabolism and homeostasis by facilitating receptor-mediated endocytosis of iron-bound transferrin (Tf) via Tf cycling, thereby promoting iron uptake [7]. Cellular iron deficiency can lead to apoptosis, while cellular transformation requires substantial iron to sustain proliferation, with iron overload contributing to tumor progression. The high expression of TFR1 in many tumors makes it a potential tumor marker, offering a target for therapies to inhibit tumor growth and metastasis [6]. Moreover, TFR1 is implicated in anemia and iron metabolism disorders. Studies have shown that elevated TFR1 expression in cardiomyocytes is associated with exacerbated inflammation in myocarditis patients [8].
huALB(HSA)/hTFRC mice are a dual gene humanized model of Alb and Tfrc, obtained by crossing huALB(HSA) mice (Catalog number: C001492) with hTFRC mice (Catalog number: C001584). This model can be used for the development of ALB/TFRC-targeted therapeutic drugs, as well as for the research on drug development using human serum albumin (HSA) as a carrier or drug delivery across the blood-brain barrier (BBB), and for in vivo pharmacodynamic and pharmacokinetic studies.
hTFRC/Ube3a-KO
製品ID :
C001737
系統:
C57BL/6NCya
状況:
説明:
The UBE3A gene encodes ubiquitin-protein ligase E3A, a critical enzyme in the ubiquitin-proteasome degradation system responsible for catalyzing substrate ubiquitination and regulating proteasomal clearance. This process is indispensable for maintaining proteostasis, particularly in neurons, where UBE3A governs synaptic plasticity, neural signaling, and neurodevelopment by modulating the levels of specific substrates. As an imprinted gene, UBE3A exhibits parent-of-origin-specific expression in brain neurons. The paternal allele is epigenetically silenced via cis-acting repression by a long noncoding antisense transcript (UBE3A-ATS) [1]. Consequently, only the maternal UBE3A allele is functionally active in neuronal populations. Loss of maternal UBE3A function disrupts ubiquitin-mediated proteolysis, leading to aberrant accumulation of neurodevelopmental regulators and subsequent dysregulation of synaptic maturation and circuit formation. These molecular deficits underlie the pathogenesis of Angelman syndrome (AS), a severe neurogenetic disorder. Patients with Angelman Syndrome commonly exhibit severe motor and intellectual developmental delays, ataxia, hypotonia, epilepsy, speech impairment, and distinctive facial features [2].
The Transferrin receptor (TFRC) gene encodes Transferrin Receptor 1 (TFR1), a protein that is expressed at low levels in most normal cells but shows increased expression in highly proliferative cells, such as basal epidermal cells, intestinal epithelium, and certain activated immune cells. Brain capillary endothelial cells, which constitute the blood-brain barrier (BBB), also express this receptor at high levels [3]. TFR1 plays a critical role in maintaining iron metabolism and homeostasis by facilitating receptor-mediated endocytosis of iron-bound transferrin (Tf) via Tf cycling, thereby promoting iron uptake [4]. Cellular iron deficiency can lead to apoptosis, while cellular transformation requires substantial iron to sustain proliferation, with iron overload contributing to tumor progression. The high expression of TFR1 in many tumors makes it a potential tumor marker, offering a target for therapies to inhibit tumor growth and metastasis [3]. Moreover, TFR1 is implicated in anemia and iron metabolism disorders. Studies have shown that elevated TFR1 expression in cardiomyocytes is associated with exacerbated inflammation in myocarditis patients [5].
The hTFRC/Ube3a-KO mice are generated by crossing hTFRC mice with Ube3a-KO mice. These mice can be used for studying the pathogenesis of Angelman syndrome (AS), developing related therapeutic approaches, and conducting preclinical research on TFRC-targeted drugs.
The UBE3A gene encodes ubiquitin-protein ligase E3A, a critical enzyme in the ubiquitin-proteasome degradation system responsible for catalyzing substrate ubiquitination and regulating proteasomal clearance. This process is indispensable for maintaining proteostasis, particularly in neurons, where UBE3A governs synaptic plasticity, neural signaling, and neurodevelopment by modulating the levels of specific substrates. As an imprinted gene, UBE3A exhibits parent-of-origin-specific expression in brain neurons. The paternal allele is epigenetically silenced via cis-acting repression by a long noncoding antisense transcript (UBE3A-ATS) [1]. Consequently, only the maternal UBE3A allele is functionally active in neuronal populations. Loss of maternal UBE3A function disrupts ubiquitin-mediated proteolysis, leading to aberrant accumulation of neurodevelopmental regulators and subsequent dysregulation of synaptic maturation and circuit formation. These molecular deficits underlie the pathogenesis of Angelman syndrome (AS), a severe neurogenetic disorder. Patients with Angelman Syndrome commonly exhibit severe motor and intellectual developmental delays, ataxia, hypotonia, epilepsy, speech impairment, and distinctive facial features [2].
The Transferrin receptor (TFRC) gene encodes Transferrin Receptor 1 (TFR1), a protein that is expressed at low levels in most normal cells but shows increased expression in highly proliferative cells, such as basal epidermal cells, intestinal epithelium, and certain activated immune cells. Brain capillary endothelial cells, which constitute the blood-brain barrier (BBB), also express this receptor at high levels [3]. TFR1 plays a critical role in maintaining iron metabolism and homeostasis by facilitating receptor-mediated endocytosis of iron-bound transferrin (Tf) via Tf cycling, thereby promoting iron uptake [4]. Cellular iron deficiency can lead to apoptosis, while cellular transformation requires substantial iron to sustain proliferation, with iron overload contributing to tumor progression. The high expression of TFR1 in many tumors makes it a potential tumor marker, offering a target for therapies to inhibit tumor growth and metastasis [3]. Moreover, TFR1 is implicated in anemia and iron metabolism disorders. Studies have shown that elevated TFR1 expression in cardiomyocytes is associated with exacerbated inflammation in myocarditis patients [5].
The hTFRC/Ube3a-KO mice are generated by crossing hTFRC mice with Ube3a-KO mice. These mice can be used for studying the pathogenesis of Angelman syndrome (AS), developing related therapeutic approaches, and conducting preclinical research on TFRC-targeted drugs.
hSEZ6
製品ID :
C001916
系統:
C57BL/6NCya
状況:
説明:
The Sez6 gene primarily encodes a Seizure-related homolog protein 6 (SEZ6), a cell-surface type I transmembrane glycoprotein that is an N-glycosylated protein containing five short consensus repeat (SCR)/sushi domains and two or three CUB domains in its extracellular domain [1]. Gene expression is highly restricted in normal adult tissues, found almost exclusively in the central nervous system (CNS), particularly in neurons (e.g., in the cerebral cortex, hippocampus), with low expression in the testis and some gastrointestinal tissues. SEZ6 is involved in neuronal development and function, notably in regulating dendrite elongation and branching, synaptic plasticity, and may also function as a complement regulator by inhibiting C3 convertases, in addition to being a novel trafficking protein of the kainate receptor (KAR) [2]. Associated diseases include neurodevelopmental and psychiatric disorders such as epilepsy (especially febrile seizures), schizophrenia, and Alzheimer's disease. Furthermore, SEZ6 overexpression has been detected in various high-grade neuroendocrine malignancies (e.g., small cell lung cancer (SCLC), medullary thyroid carcinomas), making it a novel therapeutic target in cancer [1].
The hSEZ6 mouse is a humanized model constructed by gene-editing technology, in which the p.20 to partial intron 3 of mouse Sez6 is replaced with Human-Mouse chimeric CDS (Human SEZ6 Extracellular + Mouse Sez6 Intracellular)-3'UTR of Mouse Sez6-WPRE-BGH pA cassette. The murine signal peptide is remained. This model can be used for the research of the pathological mechanisms of neurodevelopmental and psychiatric disorders such as epilepsy (especially febrile seizures), schizophrenia, and Alzheimer's disease, and some cancers, as well as the development of relevant treatment methods, and the screening, development, and pre-clinical evaluation of SEZ6-targeted drugs.
The Sez6 gene primarily encodes a Seizure-related homolog protein 6 (SEZ6), a cell-surface type I transmembrane glycoprotein that is an N-glycosylated protein containing five short consensus repeat (SCR)/sushi domains and two or three CUB domains in its extracellular domain [1]. Gene expression is highly restricted in normal adult tissues, found almost exclusively in the central nervous system (CNS), particularly in neurons (e.g., in the cerebral cortex, hippocampus), with low expression in the testis and some gastrointestinal tissues. SEZ6 is involved in neuronal development and function, notably in regulating dendrite elongation and branching, synaptic plasticity, and may also function as a complement regulator by inhibiting C3 convertases, in addition to being a novel trafficking protein of the kainate receptor (KAR) [2]. Associated diseases include neurodevelopmental and psychiatric disorders such as epilepsy (especially febrile seizures), schizophrenia, and Alzheimer's disease. Furthermore, SEZ6 overexpression has been detected in various high-grade neuroendocrine malignancies (e.g., small cell lung cancer (SCLC), medullary thyroid carcinomas), making it a novel therapeutic target in cancer [1].
The hSEZ6 mouse is a humanized model constructed by gene-editing technology, in which the p.20 to partial intron 3 of mouse Sez6 is replaced with Human-Mouse chimeric CDS (Human SEZ6 Extracellular + Mouse Sez6 Intracellular)-3'UTR of Mouse Sez6-WPRE-BGH pA cassette. The murine signal peptide is remained. This model can be used for the research of the pathological mechanisms of neurodevelopmental and psychiatric disorders such as epilepsy (especially febrile seizures), schizophrenia, and Alzheimer's disease, and some cancers, as well as the development of relevant treatment methods, and the screening, development, and pre-clinical evaluation of SEZ6-targeted drugs.
hMRGPRX2
製品ID :
C001846
系統:
C57BL/6NCya
状況:
説明:
The MRGPRX2 gene, a member of the G protein-coupled receptor (GPCR) family, encodes a unique receptor protein with a pivotal role in immunological and neurological signaling [1]. Primarily expressed on mast cells and sensory neurons, the MRGPRX2 protein functions as a non-canonical receptor that circumvents traditional IgE-mediated pathways. Its ligand repertoire is remarkably broad, encompassing a diverse array of stimuli, including endogenous neuropeptides (e.g., substance P) and exogenous cationic drugs (e.g., fluoroquinolones, neuromuscular blocking agents) [2]. Ligand binding to MRGPRX2 initiates mast cell degranulation, a process that releases potent pro-inflammatory mediators such as histamine and tryptase. This activation mechanism is a central driver of pseudo-allergic reactions, a class of drug hypersensitivities that mimic true allergic responses without involving IgE [3]. Emerging evidence further implicates MRGPRX2 in the pathophysiology of various inflammatory and pruritic diseases, including chronic spontaneous urticaria and atopic dermatitis, underscoring its therapeutic potential as a target for modulating mast cell activity [4].
The hMRGPRX2 mouse is a humanized model, constructed by replacing the sequences from exon 1 to partial intron 1 of mouse Mrgprx2 with the Kozak-human MRGPRX2 CDS-3'UTR of mouse Mrgprx2-WPRE-BGH pA cassette. hMRGPRX2 mice can be used for research into the pathogenesis of various inflammatory and pruritic diseases, including chronic spontaneous urticaria and atopic dermatitis. They are also useful for the development of MRGPRX2-targeted drugs.
The MRGPRX2 gene, a member of the G protein-coupled receptor (GPCR) family, encodes a unique receptor protein with a pivotal role in immunological and neurological signaling [1]. Primarily expressed on mast cells and sensory neurons, the MRGPRX2 protein functions as a non-canonical receptor that circumvents traditional IgE-mediated pathways. Its ligand repertoire is remarkably broad, encompassing a diverse array of stimuli, including endogenous neuropeptides (e.g., substance P) and exogenous cationic drugs (e.g., fluoroquinolones, neuromuscular blocking agents) [2]. Ligand binding to MRGPRX2 initiates mast cell degranulation, a process that releases potent pro-inflammatory mediators such as histamine and tryptase. This activation mechanism is a central driver of pseudo-allergic reactions, a class of drug hypersensitivities that mimic true allergic responses without involving IgE [3]. Emerging evidence further implicates MRGPRX2 in the pathophysiology of various inflammatory and pruritic diseases, including chronic spontaneous urticaria and atopic dermatitis, underscoring its therapeutic potential as a target for modulating mast cell activity [4].
The hMRGPRX2 mouse is a humanized model, constructed by replacing the sequences from exon 1 to partial intron 1 of mouse Mrgprx2 with the Kozak-human MRGPRX2 CDS-3'UTR of mouse Mrgprx2-WPRE-BGH pA cassette. hMRGPRX2 mice can be used for research into the pathogenesis of various inflammatory and pruritic diseases, including chronic spontaneous urticaria and atopic dermatitis. They are also useful for the development of MRGPRX2-targeted drugs.
hHTT-Qn(FVB)
製品ID :
C001404
系統:
FVB/NJCya
状況:
説明:
Huntingtin (HTT) is a disease-associated gene that is widely expressed in various tissues and organs, including the central nervous system, and is essential for normal development. The coding region of the HTT gene contains a polymorphic trinucleotide (cytosine-adenine-guanine, CAG) repeat sequence near the 5’ UTR, which forms a polyglutamine (polyQ) tract during translation. Huntington’s disease (HD) is a neurodegenerative disorder characterized by the loss of striatal neurons, caused by the aberrant expression of the CAG repeat sequence in the HTT gene. When the CAG repeat expands beyond 35 copies, it leads to abnormal polyQ expansion, resulting in incorrect folding of HTT protein fragments, dysregulation of protein-protein interactions, and accumulation in the cell nucleus and neuronal terminals. This ultimately affects neural signaling, intracellular protein transport, and mitochondrial function [1]. Currently, there are no effective drugs or methods to prevent or treat Huntington’s disease, and there is a great need for further research into its mechanisms and the development of therapeutic approaches [2].
This strain is an hHTT gene knock-in mouse model generated by gene editing technology, in which a mutated human HTT gene sequence carrying over 100 CAG repeats is inserted into the mouse genome. Mice carrying these mutations have been reported to exhibit pathological characteristics and functional impairment phenotypes of Huntington’s disease, and can be used for the development and screening of therapeutic drugs for Huntington’s disease, as well as for safety evaluation [3]. The detection data show that this model can successfully express the mutated human HTT gene and protein.
Huntingtin (HTT) is a disease-associated gene that is widely expressed in various tissues and organs, including the central nervous system, and is essential for normal development. The coding region of the HTT gene contains a polymorphic trinucleotide (cytosine-adenine-guanine, CAG) repeat sequence near the 5’ UTR, which forms a polyglutamine (polyQ) tract during translation. Huntington’s disease (HD) is a neurodegenerative disorder characterized by the loss of striatal neurons, caused by the aberrant expression of the CAG repeat sequence in the HTT gene. When the CAG repeat expands beyond 35 copies, it leads to abnormal polyQ expansion, resulting in incorrect folding of HTT protein fragments, dysregulation of protein-protein interactions, and accumulation in the cell nucleus and neuronal terminals. This ultimately affects neural signaling, intracellular protein transport, and mitochondrial function [1]. Currently, there are no effective drugs or methods to prevent or treat Huntington’s disease, and there is a great need for further research into its mechanisms and the development of therapeutic approaches [2].
This strain is an hHTT gene knock-in mouse model generated by gene editing technology, in which a mutated human HTT gene sequence carrying over 100 CAG repeats is inserted into the mouse genome. Mice carrying these mutations have been reported to exhibit pathological characteristics and functional impairment phenotypes of Huntington’s disease, and can be used for the development and screening of therapeutic drugs for Huntington’s disease, as well as for safety evaluation [3]. The detection data show that this model can successfully express the mutated human HTT gene and protein.
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