필터
에 대한 검색 결과 105 건
정렬 기준:
알파벳순 (A-Z)
베스트셀러
Abcd1-KO
제품 ID:
C001777
계통(Strain):
C57BL/6JCya
상태:
설명:
The ABCD1 (ATP-binding cassette subfamily D member 1) gene, located on the X chromosome (Xq28), encodes a peroxisomal transmembrane protein responsible for transporting very long-chain fatty acids (VLCFAs) into peroxisomes for β-oxidation. Widely expressed but particularly prominent in the brain, adrenal glands, and liver, ABCD1 is critical for maintaining lipid homeostasis. Mutations in ABCD1 cause X-linked adrenoleukodystrophy (X-ALD), a neurodegenerative disorder characterized by VLCFA accumulation, demyelination, adrenal insufficiency, and progressive neurological decline. Clinical manifestations vary widely, ranging from asymptomatic carriers to a severe, fatal childhood form. Primarily affecting males (with an estimated incidence of ~1 in 17,000 newborns), X-ALD has been included in newborn screening programs in many U.S. states [1-2]. The correlation between specific mutations and symptoms remains unclear, and VLCFA measurement cannot reliably predict disease-specific outcomes such as adrenal insufficiency or neurological decline. Current therapeutic approaches focus on gene repair or mitigating secondary effects like oxidative stress [3].
The Abcd1-KO mouse, a gene knockout model generated by deleting exon 2 of the mouse Abcd1 gene (homologous to human ABCD1), serves as a valuable tool for studying the pathogenesis of X-ALD and developing therapeutic interventions.
The ABCD1 (ATP-binding cassette subfamily D member 1) gene, located on the X chromosome (Xq28), encodes a peroxisomal transmembrane protein responsible for transporting very long-chain fatty acids (VLCFAs) into peroxisomes for β-oxidation. Widely expressed but particularly prominent in the brain, adrenal glands, and liver, ABCD1 is critical for maintaining lipid homeostasis. Mutations in ABCD1 cause X-linked adrenoleukodystrophy (X-ALD), a neurodegenerative disorder characterized by VLCFA accumulation, demyelination, adrenal insufficiency, and progressive neurological decline. Clinical manifestations vary widely, ranging from asymptomatic carriers to a severe, fatal childhood form. Primarily affecting males (with an estimated incidence of ~1 in 17,000 newborns), X-ALD has been included in newborn screening programs in many U.S. states [1-2]. The correlation between specific mutations and symptoms remains unclear, and VLCFA measurement cannot reliably predict disease-specific outcomes such as adrenal insufficiency or neurological decline. Current therapeutic approaches focus on gene repair or mitigating secondary effects like oxidative stress [3].
The Abcd1-KO mouse, a gene knockout model generated by deleting exon 2 of the mouse Abcd1 gene (homologous to human ABCD1), serves as a valuable tool for studying the pathogenesis of X-ALD and developing therapeutic interventions.
Abcb1a/Abcb1b-DKO(FVB)
제품 ID:
C001493
계통(Strain):
FVB/NJCya
상태:
설명:
P-glycoprotein (P-gp), also known as multidrug resistance protein 1 (MDR1), is an ATP-binding cassette transporter that acts as a biological barrier by expelling toxins and foreign substances from cells. P-gp is capable of transporting many structurally and functionally different compounds out of cells [1]. However, the mechanism of MDR1 also prevents the uptake of many cancer treatment drugs by cells, leading to multidrug resistance (MDR) [2]. In normal organisms, MDR1’s distribution in the blood-brain barrier and blood-placenta barrier prevents exogenous drugs and toxins from entering the central nervous system and placenta of the organism, thereby protecting the organism and enabling it to perform normal physiological functions. In pathological conditions, however, the MDR1 in the blood-brain barrier prevents drugs from entering the central nervous system, and in tumor cells, leads to the development of MDR. The evolution of MDR remains one of the major obstacles to controlling or curing cancer [3-4].
In humans, the MDR1 protein is encoded by the ABCB1 gene. In mice, two closely located genes, Abcb1a and Abcb1b, encode the MDR1a and MDR1b subtypes of this protein. Mouse MDR1a and MDR1b have 80% homology with human MDR1. MDR1a and MDR1b have the same function as human MDR1 protein in resisting anticancer drugs. Although mouse MDR1a and MDR1b proteins are distributed in different tissues of the body, their overall distribution is consistent with that of human MDR1 protein [5-6]. In summary, the distribution and function of mouse MDR1a and MDR1b are consistent with those of human MDR1.
This strain is an MDR1 knockout model, in which the human ABCB1 gene’s homologous genes, Abcb1a and Abcb1b, were knocked out in mice using gene editing technology. This model lacks the expression of MDR1 protein and can be used for research in areas such as blood-brain barrier permeability-related diseases and multidrug resistance of anti-tumor drugs.
P-glycoprotein (P-gp), also known as multidrug resistance protein 1 (MDR1), is an ATP-binding cassette transporter that acts as a biological barrier by expelling toxins and foreign substances from cells. P-gp is capable of transporting many structurally and functionally different compounds out of cells [1]. However, the mechanism of MDR1 also prevents the uptake of many cancer treatment drugs by cells, leading to multidrug resistance (MDR) [2]. In normal organisms, MDR1’s distribution in the blood-brain barrier and blood-placenta barrier prevents exogenous drugs and toxins from entering the central nervous system and placenta of the organism, thereby protecting the organism and enabling it to perform normal physiological functions. In pathological conditions, however, the MDR1 in the blood-brain barrier prevents drugs from entering the central nervous system, and in tumor cells, leads to the development of MDR. The evolution of MDR remains one of the major obstacles to controlling or curing cancer [3-4].
In humans, the MDR1 protein is encoded by the ABCB1 gene. In mice, two closely located genes, Abcb1a and Abcb1b, encode the MDR1a and MDR1b subtypes of this protein. Mouse MDR1a and MDR1b have 80% homology with human MDR1. MDR1a and MDR1b have the same function as human MDR1 protein in resisting anticancer drugs. Although mouse MDR1a and MDR1b proteins are distributed in different tissues of the body, their overall distribution is consistent with that of human MDR1 protein [5-6]. In summary, the distribution and function of mouse MDR1a and MDR1b are consistent with those of human MDR1.
This strain is an MDR1 knockout model, in which the human ABCB1 gene’s homologous genes, Abcb1a and Abcb1b, were knocked out in mice using gene editing technology. This model lacks the expression of MDR1 protein and can be used for research in areas such as blood-brain barrier permeability-related diseases and multidrug resistance of anti-tumor drugs.
B6-hTFRC/htau
제품 ID:
I001209
계통(Strain):
C57BL/6Cya
상태:
설명:
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 [1]. 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 [2]. 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 [1]. 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 [3].
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, the 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 [4]. 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 [5].
The B6-hTFRC/htau mice are a model expressing human TFRC protein and tau protein, generated by crossing B6-hTFRC(CDS) mice (Catalog No.: C001584) with B6-htau mice (Catalog No.: C001410). These mice can be used for research on neurodegenerative diseases and iron metabolism disorders, as well as for the development and preclinical evaluation of TFRC/MAPT-targeted therapeutic agents.
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 [1]. 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 [2]. 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 [1]. 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 [3].
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, the 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 [4]. 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 [5].
The B6-hTFRC/htau mice are a model expressing human TFRC protein and tau protein, generated by crossing B6-hTFRC(CDS) mice (Catalog No.: C001584) with B6-htau mice (Catalog No.: C001410). These mice can be used for research on neurodegenerative diseases and iron metabolism disorders, as well as for the development and preclinical evaluation of TFRC/MAPT-targeted therapeutic agents.
B6-huTFRC/htau
제품 ID:
C001923
계통(Strain):
C57BL/6Cya
상태:
설명:
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 [1]. 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 [2]. 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 [1]. 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 [3]. As a target for antibody-mediated cancer therapy, TFR1 can be leveraged through two approaches: one involves the use of antibodies conjugated to anti-cancer drugs, which are indirectly internalized via receptor-mediated endocytosis; the other employs antibodies that directly disrupt receptor function or induce Fc effector functions such as antibody-dependent cellular cytotoxicity (ADCC), antibody-dependent cellular phagocytosis (ADCP), or complement-dependent cytotoxicity (CDC). Various clinical drugs targeting TFR1 are currently under development, including antisense oligonucleotides (ASOs), antibody-drug conjugates (ADCs), and antibody-oligonucleotide conjugates, applicable to diseases such as cancer, anemia, and neurodegenerative disorders. Research indicates that enhancing antibody transport across the blood-brain barrier via TFR1, by forming specific bispecific antibodies with anti-β-amyloid antibodies, can improve therapeutic outcomes in Alzheimer's patients [4-5]. As research progresses, TFR1 is expected to become an effective clinical target for multiple diseases and a synergistic target for drug delivery across the blood-brain barrier (BBB).
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, the 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 [6]. 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 [7-8].
The B6-huTFRC/htau mouse is a dual-gene humanized model obtained by mating B6-huTFRC mice (catalog number: C001860) with B6-htau mice (catalog number: C001410). This model can be used for research on neurodegenerative diseases and iron metabolism diseases, as well as pre-clinical studies of TFRC/MAPT-targeted therapeutic drugs.
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 [1]. 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 [2]. 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 [1]. 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 [3]. As a target for antibody-mediated cancer therapy, TFR1 can be leveraged through two approaches: one involves the use of antibodies conjugated to anti-cancer drugs, which are indirectly internalized via receptor-mediated endocytosis; the other employs antibodies that directly disrupt receptor function or induce Fc effector functions such as antibody-dependent cellular cytotoxicity (ADCC), antibody-dependent cellular phagocytosis (ADCP), or complement-dependent cytotoxicity (CDC). Various clinical drugs targeting TFR1 are currently under development, including antisense oligonucleotides (ASOs), antibody-drug conjugates (ADCs), and antibody-oligonucleotide conjugates, applicable to diseases such as cancer, anemia, and neurodegenerative disorders. Research indicates that enhancing antibody transport across the blood-brain barrier via TFR1, by forming specific bispecific antibodies with anti-β-amyloid antibodies, can improve therapeutic outcomes in Alzheimer's patients [4-5]. As research progresses, TFR1 is expected to become an effective clinical target for multiple diseases and a synergistic target for drug delivery across the blood-brain barrier (BBB).
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, the 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 [6]. 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 [7-8].
The B6-huTFRC/htau mouse is a dual-gene humanized model obtained by mating B6-huTFRC mice (catalog number: C001860) with B6-htau mice (catalog number: C001410). This model can be used for research on neurodegenerative diseases and iron metabolism diseases, as well as pre-clinical studies of TFRC/MAPT-targeted therapeutic drugs.
B6-huTFRC/huACVR2B
제품 ID:
C001906
계통(Strain):
C57BL/6NCya
상태:
설명:
The B6-huTFRC/huACVR2B mouse is a dual-gene humanized model obtained by mating B6-huTFRC mice (catalog No.: C001860) with B6-huACVR2B mice (catalog No.: C001904). This model can be used in the research of muscle atrophy and growth regulation, tumorigenesis and development, reproduction and gonadal function, iron metabolism diseases, and neurodegenerative diseases, and it helps with the development of TFRC/ACVR2B-targeted drugs and preclinical pharmacological and efficacy evaluations.
The B6-huTFRC/huACVR2B mouse is a dual-gene humanized model obtained by mating B6-huTFRC mice (catalog No.: C001860) with B6-huACVR2B mice (catalog No.: C001904). This model can be used in the research of muscle atrophy and growth regulation, tumorigenesis and development, reproduction and gonadal function, iron metabolism diseases, and neurodegenerative diseases, and it helps with the development of TFRC/ACVR2B-targeted drugs and preclinical pharmacological and efficacy evaluations.
Dmd-Q995*(DBA2;B6)
제품 ID:
C001773
계통(Strain):
DBA/2Cya
상태:
설명:
Duchenne muscular dystrophy (DMD) is a severe, progressive, and debilitating X-linked disorder characterized by muscle wasting. This condition precipitates difficulties with movement, eventually necessitating assisted ventilation, and often leads to premature death. The primary cause of DMD is mutations in the dystrophin muscular dystrophy (DMD) gene, which encodes the dystrophin protein. These mutations effectively eliminate the production of dystrophin protein in muscle tissues, instigating muscle atrophy and a myriad of complications [1]. The absence of dystrophin protein culminates in the disintegration of the dystrophin-associated protein complex (DAPC) within the muscle membrane. This disintegration disrupts the interaction between actin and the extracellular matrix, rendering muscles devoid of dystrophin more susceptible to damage. This susceptibility results in the progressive loss of muscle tissue and function, as well as the development of cardiomyopathy [2].
Dmd-Q995*(DBA2;B6) mice carry a c.2983C>T (p.Q995*) mutation in the Dmd gene, which introduces a premature termination codon (PTC) triggering nonsense-mediated mRNA decay (NMD) in eukaryotes. NMD degrades PTC-containing aberrant mRNAs to minimize gene expression errors, as these mRNAs may translate into harmful gain-of-function or dominant-negative proteins disrupting physiological mechanisms. The mutation combined with the murine NMD mechanism leads to the degradation of most Dmd transcripts in Dmd-Q995*(DBA2;B6) mice, with remaining transcripts encoding nonfunctional truncated dystrophin, resulting in loss of dystrophin function [3-5]. Additionally, the inherent muscle regeneration dysfunction in the DBA/2 strain exacerbates myopathic phenotypes, including significant muscle atrophy, fibrosis, and pronounced muscle weakness, more accurately mimicking human DMD progression and severity [6]. This makes Dmd-Q995*(DBA2;B6) mice, with their lack of functional dystrophin, ideal for modeling Duchenne muscular dystrophy (DMD) and evaluating therapeutic strategies.
Duchenne muscular dystrophy (DMD) is a severe, progressive, and debilitating X-linked disorder characterized by muscle wasting. This condition precipitates difficulties with movement, eventually necessitating assisted ventilation, and often leads to premature death. The primary cause of DMD is mutations in the dystrophin muscular dystrophy (DMD) gene, which encodes the dystrophin protein. These mutations effectively eliminate the production of dystrophin protein in muscle tissues, instigating muscle atrophy and a myriad of complications [1]. The absence of dystrophin protein culminates in the disintegration of the dystrophin-associated protein complex (DAPC) within the muscle membrane. This disintegration disrupts the interaction between actin and the extracellular matrix, rendering muscles devoid of dystrophin more susceptible to damage. This susceptibility results in the progressive loss of muscle tissue and function, as well as the development of cardiomyopathy [2].
Dmd-Q995*(DBA2;B6) mice carry a c.2983C>T (p.Q995*) mutation in the Dmd gene, which introduces a premature termination codon (PTC) triggering nonsense-mediated mRNA decay (NMD) in eukaryotes. NMD degrades PTC-containing aberrant mRNAs to minimize gene expression errors, as these mRNAs may translate into harmful gain-of-function or dominant-negative proteins disrupting physiological mechanisms. The mutation combined with the murine NMD mechanism leads to the degradation of most Dmd transcripts in Dmd-Q995*(DBA2;B6) mice, with remaining transcripts encoding nonfunctional truncated dystrophin, resulting in loss of dystrophin function [3-5]. Additionally, the inherent muscle regeneration dysfunction in the DBA/2 strain exacerbates myopathic phenotypes, including significant muscle atrophy, fibrosis, and pronounced muscle weakness, more accurately mimicking human DMD progression and severity [6]. This makes Dmd-Q995*(DBA2;B6) mice, with their lack of functional dystrophin, ideal for modeling Duchenne muscular dystrophy (DMD) and evaluating therapeutic strategies.
Dmd-Q995*
제품 ID:
C001518
계통(Strain):
C57BL/6JCya
상태:
설명:
Duchenne muscular dystrophy (DMD) is a severe, progressive, and debilitating X-linked disorder characterized by muscle wasting. This condition precipitates difficulties with movement, eventually necessitating assisted ventilation, and often leads to premature death. The primary cause of DMD is mutations in the dystrophin muscular dystrophy (DMD) gene, which encodes the dystrophin protein. These mutations effectively eliminate the production of dystrophin protein in muscle tissues, instigating muscle atrophy and a myriad of complications [1]. The absence of dystrophin protein culminates in the disintegration of the dystrophin-associated protein complex (DAPC) within the muscle membrane. This disintegration disrupts the interaction between actin and the extracellular matrix, rendering muscles devoid of dystrophin more susceptible to damage. This susceptibility results in the progressive loss of muscle tissue and function, as well as the development of cardiomyopathy [2].
Dmd-Q995* mice carry a c.2983C>T (p.Q995) mutation in the Dmd gene, which results in the production of a premature termination codon (PTC). In eukaryotes, the nonsense-mediated mRNA decay (NMD) pathway degrades mRNAs containing PTCs to reduce errors in gene expression. These abnormal mRNAs may encode harmful gain-of-function or dominant-negative proteins that can damage normal human physiological mechanisms. In Dmd-Q995* mice, the mutation and the NMD pathway together result in the degradation of most Dmd transcripts. The remaining transcripts can only encode truncated dystrophin proteins that lack normal function, leading to the loss of dystrophin function [3-5]. This model, due to the lack of normal dystrophin expression, exhibits a series of muscle disease phenotypes similar to the clinical presentation of Duchenne muscular dystrophy (DMD), and can be used for research on DMD. Homozygous female mice and heterozygous males of this strain are viable and fertile.
Duchenne muscular dystrophy (DMD) is a severe, progressive, and debilitating X-linked disorder characterized by muscle wasting. This condition precipitates difficulties with movement, eventually necessitating assisted ventilation, and often leads to premature death. The primary cause of DMD is mutations in the dystrophin muscular dystrophy (DMD) gene, which encodes the dystrophin protein. These mutations effectively eliminate the production of dystrophin protein in muscle tissues, instigating muscle atrophy and a myriad of complications [1]. The absence of dystrophin protein culminates in the disintegration of the dystrophin-associated protein complex (DAPC) within the muscle membrane. This disintegration disrupts the interaction between actin and the extracellular matrix, rendering muscles devoid of dystrophin more susceptible to damage. This susceptibility results in the progressive loss of muscle tissue and function, as well as the development of cardiomyopathy [2].
Dmd-Q995* mice carry a c.2983C>T (p.Q995) mutation in the Dmd gene, which results in the production of a premature termination codon (PTC). In eukaryotes, the nonsense-mediated mRNA decay (NMD) pathway degrades mRNAs containing PTCs to reduce errors in gene expression. These abnormal mRNAs may encode harmful gain-of-function or dominant-negative proteins that can damage normal human physiological mechanisms. In Dmd-Q995* mice, the mutation and the NMD pathway together result in the degradation of most Dmd transcripts. The remaining transcripts can only encode truncated dystrophin proteins that lack normal function, leading to the loss of dystrophin function [3-5]. This model, due to the lack of normal dystrophin expression, exhibits a series of muscle disease phenotypes similar to the clinical presentation of Duchenne muscular dystrophy (DMD), and can be used for research on DMD. Homozygous female mice and heterozygous males of this strain are viable and fertile.
hSCN9A(SD)
제품 ID:
CR013
계통(Strain):
SD
상태:
설명:
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.
huAPOE4/hutau-P301S
제품 ID:
C002138
계통(Strain):
C57BL/6Cya
상태:
설명:
Apolipoprotein E (APOE) is a critical apolipoprotein involved in lipid transport mediated by lipoproteins. As a core component of plasma lipoproteins, APOE facilitates the transport of lipids through plasma and interstitial fluid between organs, and it plays a pivotal role in the generation, conversion, and clearance of lipoproteins. In humans, the APOE gene has three isoforms (E2, E3, E4) associated with atherosclerosis and Alzheimer’s disease (AD), with the E4 allele present in approximately 14% of the population [1]. The ApoE4 isoform is a major genetic risk factor for late-onset Alzheimer’s disease (AD), exacerbating neurodegeneration. ApoE4-associated damage to vascular systems in the brain could have a key role in AD pathogenesis [2]. Beyond AD, APOE4 is linked to cardiovascular diseases due to its influence on lipid homeostasis [3].
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, the 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 [4]. 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. Common mutations include P301L, P301S, and Intron10+3 G>A [5]. Research indicates that the P301S mutation significantly reduces the ability of recombinant tau protein to promote microtubule assembly. Patients with this mutation exhibit clinical heterogeneity [6-7]. Similar to the P301L mutation, the P301S mutation also leads to pathological aggregation of the tau protein, resulting in neurodegenerative diseases. Therapies targeting the MAPT gene primarily consist of small molecule drugs and monoclonal antibodies, with indications including Alzheimer’s disease (AD) and Frontotemporal Dementia (FTD). MAPT is the earliest discovered and most frequently implicated gene in FTD. Mutations in the MAPT gene are detectable in roughly 30% of familial FTD cases [8].
The huAPOE4/hutau-P301S mouse is a dual-gene humanized model obtained by crossing the huAPOE4 mouse (Catalog No.: C001867) with the hutau-P301S mouse (Catalog No.: C001836). The huAPOE4/hutau-P301S mouse can be utilized for the screening, pharmacodynamic evaluation, safety assessment, and mechanism of action studies of dual-target therapeutics targeting APOE4 and MAPT (tau), for investigating how APOE4 exacerbates tauopathy and neurodegeneration. It serves as an ideal preclinical research platform for developing innovative therapies for Alzheimer's disease (AD) and other neurodegenerative diseases.
Apolipoprotein E (APOE) is a critical apolipoprotein involved in lipid transport mediated by lipoproteins. As a core component of plasma lipoproteins, APOE facilitates the transport of lipids through plasma and interstitial fluid between organs, and it plays a pivotal role in the generation, conversion, and clearance of lipoproteins. In humans, the APOE gene has three isoforms (E2, E3, E4) associated with atherosclerosis and Alzheimer’s disease (AD), with the E4 allele present in approximately 14% of the population [1]. The ApoE4 isoform is a major genetic risk factor for late-onset Alzheimer’s disease (AD), exacerbating neurodegeneration. ApoE4-associated damage to vascular systems in the brain could have a key role in AD pathogenesis [2]. Beyond AD, APOE4 is linked to cardiovascular diseases due to its influence on lipid homeostasis [3].
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, the 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 [4]. 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. Common mutations include P301L, P301S, and Intron10+3 G>A [5]. Research indicates that the P301S mutation significantly reduces the ability of recombinant tau protein to promote microtubule assembly. Patients with this mutation exhibit clinical heterogeneity [6-7]. Similar to the P301L mutation, the P301S mutation also leads to pathological aggregation of the tau protein, resulting in neurodegenerative diseases. Therapies targeting the MAPT gene primarily consist of small molecule drugs and monoclonal antibodies, with indications including Alzheimer’s disease (AD) and Frontotemporal Dementia (FTD). MAPT is the earliest discovered and most frequently implicated gene in FTD. Mutations in the MAPT gene are detectable in roughly 30% of familial FTD cases [8].
The huAPOE4/hutau-P301S mouse is a dual-gene humanized model obtained by crossing the huAPOE4 mouse (Catalog No.: C001867) with the hutau-P301S mouse (Catalog No.: C001836). The huAPOE4/hutau-P301S mouse can be utilized for the screening, pharmacodynamic evaluation, safety assessment, and mechanism of action studies of dual-target therapeutics targeting APOE4 and MAPT (tau), for investigating how APOE4 exacerbates tauopathy and neurodegeneration. It serves as an ideal preclinical research platform for developing innovative therapies for Alzheimer's disease (AD) and other neurodegenerative diseases.
hutau/hGLP1R
제품 ID:
I001221
계통(Strain):
C57BL/6Cya
상태:
설명:
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 hutau/hGLP1R mouse is obtained by mating hutau(MAPT) mice (Catalog No.: C001410) with hGLP1R 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 hutau/hGLP1R mouse is obtained by mating hutau(MAPT) mice (Catalog No.: C001410) with hGLP1R 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).
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