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B6-hTFRC/htau
Product ID:
I001209
Strain:
C57BL/6Cya
Status:
Description:
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
Product ID:
C001923
Strain:
C57BL/6Cya
Status:
Description:
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.
huAPP-Aβ-NL-G-F-I
Product ID:
C002033
Strain:
C57BL/6JCya
Status:
Description:
The APP gene encodes the Amyloid Precursor Protein, a type I transmembrane glycoprotein that is ubiquitously expressed but reaches its highest levels in the central nervous system, particularly in the cerebral cortex and hippocampus. Following translation, the APP protein is proteolytically processed via two primary pathways: the non-amyloidogenic pathway, which prevents Aβ formation, and the amyloidogenic pathway, where sequential cleavage by β-secretase (BACE1) and γ-secretase releases amyloid-beta (Aβ) peptides [1]. While its precise physiological role remains an area of active research, APP is known to function in synaptic formation and repair, anterograde neuronal transport, and cell-to-cell adhesion [2]. Pathological mutations or duplications of the APP gene are primary drivers of Alzheimer’s Disease (AD) and Cerebral Amyloid Angiopathy (CAA), characterized by the extracellular accumulation of Aβ plaques and vascular deposits that lead to neurodegeneration and cognitive decline [3].
Pathogenic point mutations in the APP gene typically disrupt these proteolytic pathways, favoring the production or aggregation of neurotoxic peptides. The p.K670N/p.M671L (Swedish) double mutation (AAGATG to AATCTG) occurs at the β-secretase cleavage site, significantly increasing the production of total Aβ by enhancing BACE1 affinity [4]. In contrast, the p.E693G (Arctic) mutation (GAA to GGA) is located within the Aβ sequence itself; it does not increase peptide quantity but dramatically accelerates the formation of protofibrils [5]. Mutations near the γ-secretase cleavage site, such as p.I716F (Iberian) (ATC to TTC) and p.V717I (London) (GTC to ATC), shift the cleavage precision to increase the ratio of the highly aggregate-prone Aβ42 isoform over Aβ40, thereby facilitating early-onset amyloid plaque deposition [6].
The huAPP-Aβ-NL-G-F-I mouse is an Alzheimer's disease research model generated by replacing the sequence from upstream of exon 16 to downstream of exon 17 in the murine App gene with the corresponding sequence from the human APP gene. Simultaneously, the p.K670N/p.M671L (AAGATG to AATCTG), p.I716F (ATC to TTC), p.E693G (GAA to GGA) and p.V717I (GTC to ATC) point mutations were introduced into exon 16 and exon 17 of human APP gene. This model is suitable for studying neurodegenerative diseases such as Alzheimer's disease (AD), as well as for the research, development, and efficacy evaluation of AD therapeutic strategies targeting APP.
Cyagen Biosciences offers a variety of APP gene-edited mouse models: hAPP-NL-F mice (Catalog No.: C002124): Generated using a different APP humanization strategy and lacking the p.E693G and p.V717I mutations. hAPP-NL-G-F mice (Catalog No.: C002125): Generated using a different APP humanization strategy and lacking the p.V717I mutation.
The APP gene encodes the Amyloid Precursor Protein, a type I transmembrane glycoprotein that is ubiquitously expressed but reaches its highest levels in the central nervous system, particularly in the cerebral cortex and hippocampus. Following translation, the APP protein is proteolytically processed via two primary pathways: the non-amyloidogenic pathway, which prevents Aβ formation, and the amyloidogenic pathway, where sequential cleavage by β-secretase (BACE1) and γ-secretase releases amyloid-beta (Aβ) peptides [1]. While its precise physiological role remains an area of active research, APP is known to function in synaptic formation and repair, anterograde neuronal transport, and cell-to-cell adhesion [2]. Pathological mutations or duplications of the APP gene are primary drivers of Alzheimer’s Disease (AD) and Cerebral Amyloid Angiopathy (CAA), characterized by the extracellular accumulation of Aβ plaques and vascular deposits that lead to neurodegeneration and cognitive decline [3].
Pathogenic point mutations in the APP gene typically disrupt these proteolytic pathways, favoring the production or aggregation of neurotoxic peptides. The p.K670N/p.M671L (Swedish) double mutation (AAGATG to AATCTG) occurs at the β-secretase cleavage site, significantly increasing the production of total Aβ by enhancing BACE1 affinity [4]. In contrast, the p.E693G (Arctic) mutation (GAA to GGA) is located within the Aβ sequence itself; it does not increase peptide quantity but dramatically accelerates the formation of protofibrils [5]. Mutations near the γ-secretase cleavage site, such as p.I716F (Iberian) (ATC to TTC) and p.V717I (London) (GTC to ATC), shift the cleavage precision to increase the ratio of the highly aggregate-prone Aβ42 isoform over Aβ40, thereby facilitating early-onset amyloid plaque deposition [6].
The huAPP-Aβ-NL-G-F-I mouse is an Alzheimer's disease research model generated by replacing the sequence from upstream of exon 16 to downstream of exon 17 in the murine App gene with the corresponding sequence from the human APP gene. Simultaneously, the p.K670N/p.M671L (AAGATG to AATCTG), p.I716F (ATC to TTC), p.E693G (GAA to GGA) and p.V717I (GTC to ATC) point mutations were introduced into exon 16 and exon 17 of human APP gene. This model is suitable for studying neurodegenerative diseases such as Alzheimer's disease (AD), as well as for the research, development, and efficacy evaluation of AD therapeutic strategies targeting APP.
Cyagen Biosciences offers a variety of APP gene-edited mouse models: hAPP-NL-F mice (Catalog No.: C002124): Generated using a different APP humanization strategy and lacking the p.E693G and p.V717I mutations. hAPP-NL-G-F mice (Catalog No.: C002125): Generated using a different APP humanization strategy and lacking the p.V717I mutation.
hAPP-NL-F
Product ID:
C002124
Strain:
C57BL/6Cya
Status:
Description:
The APP gene encodes the Amyloid Precursor Protein, a type I transmembrane glycoprotein that is ubiquitously expressed but reaches its highest levels in the central nervous system, particularly in the cerebral cortex and hippocampus. Following translation, APP is proteolytically processed via two primary pathways: the non-amyloidogenic pathway, which precludes Aβ formation, and the amyloidogenic pathway, in which sequential cleavage by β-secretase (BACE1) and γ-secretase releases amyloid-β (Aβ) peptides [1]. Although the precise physiological functions of APP remain under active investigation, it is known to participate in synaptic formation and repair, anterograde neuronal transport, and cell-cell adhesion [2]. Pathological mutations or duplications of the APP gene are primary drivers of Alzheimer’s Disease (AD) and Cerebral Amyloid Angiopathy (CAA), characterized by the extracellular accumulation of Aβ plaques and vascular deposits that lead to neurodegeneration and cognitive decline [3].
Pathogenic point mutations in the APP gene typically disrupt these proteolytic pathways, favoring the production or aggregation of neurotoxic peptides. The p.K670N/p.M671L (Swedish) double mutation (AAGATG to AATCTG) occurs at the β-secretase cleavage site, significantly increasing total Aβ production by enhancing BACE1 binding affinity [4]. In contrast, the p.I716F (Iberian) mutation (ATC to TTC), located near the γ-secretase cleavage site, alters cleavage specificity to increase the ratio of the highly aggregation-prone Aβ42 isoform relative to Aβ40, thereby facilitating early-onset amyloid plaque deposition [5].
The hAPP-NL-F mouse is an Alzheimer's disease research model generated by replacing the region from downstream of the mouse App signal peptide-coding sequence through part of intron 1 with the "Mutant Human APP CDS-3'UTR of Human APP-WPRE-BGH pA" cassette, while retaining the mouse App signal peptide-coding sequence. The following mutations were introduced into the mutant human APP CDS: p.K670N/p.M671L (AAGATG→AATCTG) and p.I716F (ATC→TTC). This model can be used for research on Alzheimer's disease and other neurodegenerative diseases, as well as for the development and efficacy evaluation of AD therapeutic strategies targeting APP.
Cyagen Biosciences offers a variety of APP gene-edited mouse models: hAPP-NL-G-F mice (Catalog No.: C002125): Generated using a construction strategy similar to that of the present model but additionally carrying the p.E693G (Arctic) mutation. huAPP-Aβ-NL-G-F-I mice (Catalog No.: C002033): Generated using a different APP humanization strategy and additionally carrying the p.E693G and p.V717I mutations.
The APP gene encodes the Amyloid Precursor Protein, a type I transmembrane glycoprotein that is ubiquitously expressed but reaches its highest levels in the central nervous system, particularly in the cerebral cortex and hippocampus. Following translation, APP is proteolytically processed via two primary pathways: the non-amyloidogenic pathway, which precludes Aβ formation, and the amyloidogenic pathway, in which sequential cleavage by β-secretase (BACE1) and γ-secretase releases amyloid-β (Aβ) peptides [1]. Although the precise physiological functions of APP remain under active investigation, it is known to participate in synaptic formation and repair, anterograde neuronal transport, and cell-cell adhesion [2]. Pathological mutations or duplications of the APP gene are primary drivers of Alzheimer’s Disease (AD) and Cerebral Amyloid Angiopathy (CAA), characterized by the extracellular accumulation of Aβ plaques and vascular deposits that lead to neurodegeneration and cognitive decline [3].
Pathogenic point mutations in the APP gene typically disrupt these proteolytic pathways, favoring the production or aggregation of neurotoxic peptides. The p.K670N/p.M671L (Swedish) double mutation (AAGATG to AATCTG) occurs at the β-secretase cleavage site, significantly increasing total Aβ production by enhancing BACE1 binding affinity [4]. In contrast, the p.I716F (Iberian) mutation (ATC to TTC), located near the γ-secretase cleavage site, alters cleavage specificity to increase the ratio of the highly aggregation-prone Aβ42 isoform relative to Aβ40, thereby facilitating early-onset amyloid plaque deposition [5].
The hAPP-NL-F mouse is an Alzheimer's disease research model generated by replacing the region from downstream of the mouse App signal peptide-coding sequence through part of intron 1 with the "Mutant Human APP CDS-3'UTR of Human APP-WPRE-BGH pA" cassette, while retaining the mouse App signal peptide-coding sequence. The following mutations were introduced into the mutant human APP CDS: p.K670N/p.M671L (AAGATG→AATCTG) and p.I716F (ATC→TTC). This model can be used for research on Alzheimer's disease and other neurodegenerative diseases, as well as for the development and efficacy evaluation of AD therapeutic strategies targeting APP.
Cyagen Biosciences offers a variety of APP gene-edited mouse models: hAPP-NL-G-F mice (Catalog No.: C002125): Generated using a construction strategy similar to that of the present model but additionally carrying the p.E693G (Arctic) mutation. huAPP-Aβ-NL-G-F-I mice (Catalog No.: C002033): Generated using a different APP humanization strategy and additionally carrying the p.E693G and p.V717I mutations.
hAPP-NL-G-F
Product ID:
C002125
Strain:
C57BL/6Cya
Status:
Description:
The APP gene encodes the Amyloid Precursor Protein, a type I transmembrane glycoprotein that is ubiquitously expressed but reaches its highest levels in the central nervous system, particularly in the cerebral cortex and hippocampus. Following translation, the APP protein is proteolytically processed via two primary pathways: the non-amyloidogenic pathway, which prevents Aβ formation, and the amyloidogenic pathway, where sequential cleavage by β-secretase (BACE1) and γ-secretase releases amyloid-beta (Aβ) peptides [1]. While its precise physiological role remains an area of active research, APP is known to function in synaptic formation and repair, anterograde neuronal transport, and cell-to-cell adhesion [2]. Pathological mutations or duplications of the APP gene are primary drivers of Alzheimer’s Disease (AD) and Cerebral Amyloid Angiopathy (CAA), characterized by the extracellular accumulation of Aβ plaques and vascular deposits that lead to neurodegeneration and cognitive decline [3].
Pathogenic point mutations in the APP gene typically disrupt these proteolytic pathways, favoring the production or aggregation of neurotoxic peptides. The p.K670N/p.M671L (Swedish) double mutation (AAGATG to AATCTG) occurs at the β-secretase cleavage site, significantly increasing the production of total Aβ by enhancing BACE1 affinity [4]. In contrast, the p.E693G (Arctic) mutation (GAA to GGA) is located within the Aβ sequence itself; it does not increase peptide quantity but dramatically accelerates the formation of protofibrils [5]. The p.I716F (Iberian) mutation (ATC to TTC), located near the γ-secretase cleavage site, shifts the cleavage precision to increase the ratio of the highly aggregate-prone Aβ42 isoform over Aβ40, thereby facilitating early-onset amyloid plaque deposition [6].
The hAPP-NL-G-F mouse is an Alzheimer's disease research model generated by replacing the region from downstream of the mouse App signal peptide-coding sequence through part of intron 1 with the "Mutant Human APP CDS-3'UTR of Human APP-WPRE-BGH pA" cassette, while retaining the mouse App signal peptide-coding sequence. In addition, the following point mutations were introduced into the mutant human APP CDS: p.K670N/p.M671L (AAGATG→AATCTG), p.E693G (GAA to GGA) and p.I716F (ATC→TTC). This model can be used for research on Alzheimer's disease and other neurodegenerative diseases, as well as for the development and efficacy evaluation of AD therapeutic strategies targeting APP.
Cyagen Biosciences offers a variety of APP gene-edited mouse models: hAPP-NL-F mice (Catalog No.: C002124): Generated using a construction strategy similar to that of the present model but without the p.E693G (Arctic) mutation. huAPP-Aβ-NL-G-F-I mice (Catalog No.: C002033): Generated using a different APP humanization strategy and additionally carrying the p.V717I mutation.
The APP gene encodes the Amyloid Precursor Protein, a type I transmembrane glycoprotein that is ubiquitously expressed but reaches its highest levels in the central nervous system, particularly in the cerebral cortex and hippocampus. Following translation, the APP protein is proteolytically processed via two primary pathways: the non-amyloidogenic pathway, which prevents Aβ formation, and the amyloidogenic pathway, where sequential cleavage by β-secretase (BACE1) and γ-secretase releases amyloid-beta (Aβ) peptides [1]. While its precise physiological role remains an area of active research, APP is known to function in synaptic formation and repair, anterograde neuronal transport, and cell-to-cell adhesion [2]. Pathological mutations or duplications of the APP gene are primary drivers of Alzheimer’s Disease (AD) and Cerebral Amyloid Angiopathy (CAA), characterized by the extracellular accumulation of Aβ plaques and vascular deposits that lead to neurodegeneration and cognitive decline [3].
Pathogenic point mutations in the APP gene typically disrupt these proteolytic pathways, favoring the production or aggregation of neurotoxic peptides. The p.K670N/p.M671L (Swedish) double mutation (AAGATG to AATCTG) occurs at the β-secretase cleavage site, significantly increasing the production of total Aβ by enhancing BACE1 affinity [4]. In contrast, the p.E693G (Arctic) mutation (GAA to GGA) is located within the Aβ sequence itself; it does not increase peptide quantity but dramatically accelerates the formation of protofibrils [5]. The p.I716F (Iberian) mutation (ATC to TTC), located near the γ-secretase cleavage site, shifts the cleavage precision to increase the ratio of the highly aggregate-prone Aβ42 isoform over Aβ40, thereby facilitating early-onset amyloid plaque deposition [6].
The hAPP-NL-G-F mouse is an Alzheimer's disease research model generated by replacing the region from downstream of the mouse App signal peptide-coding sequence through part of intron 1 with the "Mutant Human APP CDS-3'UTR of Human APP-WPRE-BGH pA" cassette, while retaining the mouse App signal peptide-coding sequence. In addition, the following point mutations were introduced into the mutant human APP CDS: p.K670N/p.M671L (AAGATG→AATCTG), p.E693G (GAA to GGA) and p.I716F (ATC→TTC). This model can be used for research on Alzheimer's disease and other neurodegenerative diseases, as well as for the development and efficacy evaluation of AD therapeutic strategies targeting APP.
Cyagen Biosciences offers a variety of APP gene-edited mouse models: hAPP-NL-F mice (Catalog No.: C002124): Generated using a construction strategy similar to that of the present model but without the p.E693G (Arctic) mutation. huAPP-Aβ-NL-G-F-I mice (Catalog No.: C002033): Generated using a different APP humanization strategy and additionally carrying the p.V717I mutation.
hAPP
Product ID:
C002123
Strain:
C57BL/6Cya
Status:
Description:
The APP gene encodes the Amyloid Precursor Protein, a type I transmembrane glycoprotein that is ubiquitously expressed but reaches its highest levels in the central nervous system, particularly in the cerebral cortex and hippocampus. Following translation, APP is proteolytically processed via two primary pathways: the non-amyloidogenic pathway, which precludes Aβ formation, and the amyloidogenic pathway, in which sequential cleavage by β-secretase (BACE1) and γ-secretase releases amyloid-β (Aβ) peptides [1]. Although the precise physiological functions of APP remain under active investigation, it is known to participate in synaptic formation and repair, anterograde neuronal transport, and cell-cell adhesion [2]. Pathological mutations or duplications of the APP gene are primary drivers of Alzheimer’s Disease (AD) and Cerebral Amyloid Angiopathy (CAA), characterized by the extracellular accumulation of Aβ plaques and vascular deposits that lead to neurodegeneration and cognitive decline [3].
The hAPP mouse is a humanized model generated using gene-editing technology. The region downstream of the mouse App signal peptide-coding sequence to a portion of intron 1 was replaced with the “Human APP CDS-3'UTR of Human APP-WPRE-BGH pA” cassette, while the mouse App signal peptide-coding sequence was retained. This model is suitable for studying neurodegenerative diseases such as Alzheimer's disease (AD), as well as for the research, development, and efficacy evaluation of AD therapeutic strategies targeting APP. Cyagen also offers huAPP-Aβ mice (Catalog No.: C002031), providing an alternative model for APP/Aβ-related research. The two models feature distinct humanization designs: the hAPP mouse incorporates a human APP CDS expression cassette, whereas the huAPP-Aβ mouse carries a genomic replacement in which the corresponding mouse App genomic region was replaced with its human APP genomic counterpart. The appropriate model can be selected based on the humanized region and construct design, according to the specific drug target and research objectives.
The APP gene encodes the Amyloid Precursor Protein, a type I transmembrane glycoprotein that is ubiquitously expressed but reaches its highest levels in the central nervous system, particularly in the cerebral cortex and hippocampus. Following translation, APP is proteolytically processed via two primary pathways: the non-amyloidogenic pathway, which precludes Aβ formation, and the amyloidogenic pathway, in which sequential cleavage by β-secretase (BACE1) and γ-secretase releases amyloid-β (Aβ) peptides [1]. Although the precise physiological functions of APP remain under active investigation, it is known to participate in synaptic formation and repair, anterograde neuronal transport, and cell-cell adhesion [2]. Pathological mutations or duplications of the APP gene are primary drivers of Alzheimer’s Disease (AD) and Cerebral Amyloid Angiopathy (CAA), characterized by the extracellular accumulation of Aβ plaques and vascular deposits that lead to neurodegeneration and cognitive decline [3].
The hAPP mouse is a humanized model generated using gene-editing technology. The region downstream of the mouse App signal peptide-coding sequence to a portion of intron 1 was replaced with the “Human APP CDS-3'UTR of Human APP-WPRE-BGH pA” cassette, while the mouse App signal peptide-coding sequence was retained. This model is suitable for studying neurodegenerative diseases such as Alzheimer's disease (AD), as well as for the research, development, and efficacy evaluation of AD therapeutic strategies targeting APP. Cyagen also offers huAPP-Aβ mice (Catalog No.: C002031), providing an alternative model for APP/Aβ-related research. The two models feature distinct humanization designs: the hAPP mouse incorporates a human APP CDS expression cassette, whereas the huAPP-Aβ mouse carries a genomic replacement in which the corresponding mouse App genomic region was replaced with its human APP genomic counterpart. The appropriate model can be selected based on the humanized region and construct design, according to the specific drug target and research objectives.
hEGFR
Product ID:
C001782
Strain:
C57BL/6NCya
Status:
Description:
The Epidermal Growth Factor Receptor (EGFR) gene (also known as ERBB1 or HER1) encodes a transmembrane glycoprotein that belongs to the protein kinase superfamily. It is widely expressed in various cellular tissues, including epithelial and mesenchymal cells, bone cells, blood and immune cells, heart cells, glia, and stem neural cells, and is particularly abundant in the placenta [1]. Its primary function is to act as a receptor for members of the epidermal growth factor family, such as EGF and TGF-alpha. Upon ligand binding, EGFR undergoes dimerization and tyrosine autophosphorylation, initiating crucial downstream signaling pathways (like RAS-RAF-MEK-ERK and PI3 kinase-AKT) that regulate essential cellular processes including proliferation, survival, differentiation, and migration [2]. Aberrant gene expression, particularly overexpression, amplification, or activating mutations in EGFR, leads to its constitutive activation, promoting uncontrolled cell growth and survival [3]. This dysregulation is a significant factor in the development and progression of numerous cancers, most notably non-small cell lung cancer (especially adenocarcinoma), glioblastoma, colorectal carcinoma, and breast carcinoma, making EGFR a key target for personalized cancer therapies [4].
The hEGFR mouse is a humanized model constructed by replacing exon 2 and part of intron 2 of the mouse Egfr gene with the EGFR Chimeric cDNA-WPRE BGH pA cassette. The murine signal peptide and partial extracellular domain are preserved. hEGFR mice can be used for research into the pathogenesis of various cancers, including non-small cell lung cancer (adenocarcinoma), glioblastoma, colorectal cancer, and breast cancer, as well as for the screening, development, and safety assessment of EGFR-targeted therapies.
The Epidermal Growth Factor Receptor (EGFR) gene (also known as ERBB1 or HER1) encodes a transmembrane glycoprotein that belongs to the protein kinase superfamily. It is widely expressed in various cellular tissues, including epithelial and mesenchymal cells, bone cells, blood and immune cells, heart cells, glia, and stem neural cells, and is particularly abundant in the placenta [1]. Its primary function is to act as a receptor for members of the epidermal growth factor family, such as EGF and TGF-alpha. Upon ligand binding, EGFR undergoes dimerization and tyrosine autophosphorylation, initiating crucial downstream signaling pathways (like RAS-RAF-MEK-ERK and PI3 kinase-AKT) that regulate essential cellular processes including proliferation, survival, differentiation, and migration [2]. Aberrant gene expression, particularly overexpression, amplification, or activating mutations in EGFR, leads to its constitutive activation, promoting uncontrolled cell growth and survival [3]. This dysregulation is a significant factor in the development and progression of numerous cancers, most notably non-small cell lung cancer (especially adenocarcinoma), glioblastoma, colorectal carcinoma, and breast carcinoma, making EGFR a key target for personalized cancer therapies [4].
The hEGFR mouse is a humanized model constructed by replacing exon 2 and part of intron 2 of the mouse Egfr gene with the EGFR Chimeric cDNA-WPRE BGH pA cassette. The murine signal peptide and partial extracellular domain are preserved. hEGFR mice can be used for research into the pathogenesis of various cancers, including non-small cell lung cancer (adenocarcinoma), glioblastoma, colorectal cancer, and breast cancer, as well as for the screening, development, and safety assessment of EGFR-targeted therapies.
hACE2-EGFP
Product ID:
C001226
Strain:
C57BL/6NCya
Status:
Description:
Angiotensin-converting enzyme 2 (ACE2) is a member of the angiotensin-converting enzyme (ACE) family of dipeptidyl carboxypeptidases. ACE2 is expressed in a variety of human tissues and has a high affinity for angiotensin I (Ang I) and angiotensin II (Ang II) receptors. ACE2 catalyzes the cleavage of Ang I to angiotensin 1-9 (Ang 1-9) and Ang II to angiotensin 1-7 (Ang 1-7), which have vasodilatory and hypotensive effects [1]. ACE2 plays a role in regulating blood pressure, fluid balance, inflammation, cell proliferation, hypertrophy, and fibrosis, as well as in the regulation of cardiovascular and renal function and fertility [2]. ACE2 is also the common functional receptor for the spike protein of human coronaviruses HCoV-NL63, SARS-CoV, and SARS-CoV-2 [3]. However, due to species differences, the SARS-CoV-2 virus cannot bind to the ACE2 receptor of wild-type rodents [4-5]. Replacement of mouse Ace2 with human ACE2 by gene editing techniques resulted in humanized ACE2 mice (hACE2) that stably express human ACE2 receptors for COVID-19 studies.
In this strain, the mouse endogenous Ace2 gene sequence was replaced with the coding sequence (CDS) of the human ACE2 gene, while retaining the sequence encoding the mouse ACE2 protein signal peptide. This resulted in the expression of the hACE2 protein under the control of the endogenous mouse Ace2 regulatory elements. In addition, an enhanced green fluorescent protein (EGFP) expression cassette was inserted into the model to allow tracking of hACE2 expression. The integration site of the hACE2 is located on the mouse chromosome X. Homozygous female and hemizygous male hACE2-EGFP mice are viable and fertile.
Angiotensin-converting enzyme 2 (ACE2) is a member of the angiotensin-converting enzyme (ACE) family of dipeptidyl carboxypeptidases. ACE2 is expressed in a variety of human tissues and has a high affinity for angiotensin I (Ang I) and angiotensin II (Ang II) receptors. ACE2 catalyzes the cleavage of Ang I to angiotensin 1-9 (Ang 1-9) and Ang II to angiotensin 1-7 (Ang 1-7), which have vasodilatory and hypotensive effects [1]. ACE2 plays a role in regulating blood pressure, fluid balance, inflammation, cell proliferation, hypertrophy, and fibrosis, as well as in the regulation of cardiovascular and renal function and fertility [2]. ACE2 is also the common functional receptor for the spike protein of human coronaviruses HCoV-NL63, SARS-CoV, and SARS-CoV-2 [3]. However, due to species differences, the SARS-CoV-2 virus cannot bind to the ACE2 receptor of wild-type rodents [4-5]. Replacement of mouse Ace2 with human ACE2 by gene editing techniques resulted in humanized ACE2 mice (hACE2) that stably express human ACE2 receptors for COVID-19 studies.
In this strain, the mouse endogenous Ace2 gene sequence was replaced with the coding sequence (CDS) of the human ACE2 gene, while retaining the sequence encoding the mouse ACE2 protein signal peptide. This resulted in the expression of the hACE2 protein under the control of the endogenous mouse Ace2 regulatory elements. In addition, an enhanced green fluorescent protein (EGFP) expression cassette was inserted into the model to allow tracking of hACE2 expression. The integration site of the hACE2 is located on the mouse chromosome X. Homozygous female and hemizygous male hACE2-EGFP mice are viable and fertile.
hIGF1R(BALB/c)
Product ID:
C001624
Strain:
BALB/cAnCya
Status:
Description:
The Insulin-like Growth Factor 1 Receptor (IGF-1R), encoded by the IGF1R gene, is a receptor tyrosine kinase expressed in most tissues and cells. Its expression is developmentally regulated and influenced by nutrition, hormones, and intracellular factors, with high expression during growth and development, declining in adulthood [1]. The IGF1R protein is a heterotetramer (α2β2) of α and β subunits derived from a precursor protein, forming transmembrane αβ chains. The α chain is located extracellularly, while the β chain spans the cell membrane and is responsible for intracellular signal transduction after ligand stimulation. IGF1R binds Insulin-like Growth Factor-1 (IGF-1) with high affinity, mediating IGF-1's growth-promoting effects and regulating cell growth, differentiation, survival, and metabolism [1-4], and IGF1R defects are linked to growth retardation and diabetes [2-4]. Furthermore, IGF1R overexpression in tumors promotes proliferation, invasion, and metastasis, making it a cancer therapy target [3]. In thyroid eye disease (TED), an autoimmune disorder, activating IGF1R antibodies can be detected. IGF1R is overexpressed in T cells, B cells, and orbital fibroblasts of patients, forming a signal transduction complex with the thyroid-stimulating hormone receptor, thereby enhancing the effect of thyroid-stimulating hormone [5]. Therefore, targeting IGF1R to inhibit thyroid-stimulating hormone action is a therapeutic strategy for TED, improving exophthalmos [6].
hIGF1R(BALB/c) mice are humanized models generated using gene editing technology by integrating the protein-coding sequence (CDS) encoding the extracellular domain of human IGF1R protein and the intracellular domain of mouse IGF1R protein into the mouse Igf1r gene locus, while retaining the endogenous gene sequence encoding the signal peptide of mouse IGF1R protein. Homozygous hIGF1R(BALB/c) mice are viable and fertile, and can be used for studying the pathological mechanisms and treatments of growth retardation, diabetes, and cancer, as well as for screening, developing, and preclinical efficacy and safety evaluation of IGF1R-targeted drugs.
The Insulin-like Growth Factor 1 Receptor (IGF-1R), encoded by the IGF1R gene, is a receptor tyrosine kinase expressed in most tissues and cells. Its expression is developmentally regulated and influenced by nutrition, hormones, and intracellular factors, with high expression during growth and development, declining in adulthood [1]. The IGF1R protein is a heterotetramer (α2β2) of α and β subunits derived from a precursor protein, forming transmembrane αβ chains. The α chain is located extracellularly, while the β chain spans the cell membrane and is responsible for intracellular signal transduction after ligand stimulation. IGF1R binds Insulin-like Growth Factor-1 (IGF-1) with high affinity, mediating IGF-1's growth-promoting effects and regulating cell growth, differentiation, survival, and metabolism [1-4], and IGF1R defects are linked to growth retardation and diabetes [2-4]. Furthermore, IGF1R overexpression in tumors promotes proliferation, invasion, and metastasis, making it a cancer therapy target [3]. In thyroid eye disease (TED), an autoimmune disorder, activating IGF1R antibodies can be detected. IGF1R is overexpressed in T cells, B cells, and orbital fibroblasts of patients, forming a signal transduction complex with the thyroid-stimulating hormone receptor, thereby enhancing the effect of thyroid-stimulating hormone [5]. Therefore, targeting IGF1R to inhibit thyroid-stimulating hormone action is a therapeutic strategy for TED, improving exophthalmos [6].
hIGF1R(BALB/c) mice are humanized models generated using gene editing technology by integrating the protein-coding sequence (CDS) encoding the extracellular domain of human IGF1R protein and the intracellular domain of mouse IGF1R protein into the mouse Igf1r gene locus, while retaining the endogenous gene sequence encoding the signal peptide of mouse IGF1R protein. Homozygous hIGF1R(BALB/c) mice are viable and fertile, and can be used for studying the pathological mechanisms and treatments of growth retardation, diabetes, and cancer, as well as for screening, developing, and preclinical efficacy and safety evaluation of IGF1R-targeted drugs.
hIGF1R
Product ID:
C001623
Strain:
C57BL/6NCya
Status:
Description:
The Insulin-like Growth Factor 1 Receptor (IGF-1R), encoded by the IGF1R gene, is a receptor tyrosine kinase expressed in most tissues and cells. Its expression is developmentally regulated and influenced by nutrition, hormones, and intracellular factors, with high expression during growth and development, declining in adulthood [1]. The IGF1R protein is a heterotetramer (α2β2) of α and β subunits derived from a precursor protein, forming transmembrane αβ chains. The α chain is located extracellularly, while the β chain spans the cell membrane and is responsible for intracellular signal transduction after ligand stimulation. IGF1R binds Insulin-like Growth Factor-1 (IGF-1) with high affinity, mediating IGF-1's growth-promoting effects and regulating cell growth, differentiation, survival, and metabolism [1-4], and IGF1R defects are linked to growth retardation and diabetes [2-4]. Furthermore, IGF1R overexpression in tumors promotes proliferation, invasion, and metastasis, making it a cancer therapy target [3]. In thyroid eye disease (TED), an autoimmune disorder, activating IGF1R antibodies can be detected. IGF1R is overexpressed in T cells, B cells, and orbital fibroblasts of patients, forming a signal transduction complex with the thyroid-stimulating hormone receptor, thereby enhancing the effect of thyroid-stimulating hormone [5]. Therefore, targeting IGF1R to inhibit thyroid-stimulating hormone action is a therapeutic strategy for TED, improving exophthalmos [6].
hIGF1R mice are humanized models generated using gene editing technology by integrating the protein-coding sequence (CDS) encoding the extracellular domain of the human IGF1R protein and the intracellular domain of the mouse IGF1R protein into the mouse Igf1r gene locus, while retaining the endogenous gene sequence encoding the signal peptide of mouse IGF1R protein. Homozygous hIGF1R mice are viable and fertile, and can be used for studying the pathological mechanisms and treatments of growth retardation, diabetes, and cancer, as well as for screening, developing, and preclinical efficacy and safety evaluation of IGF1R-targeted drugs.
The Insulin-like Growth Factor 1 Receptor (IGF-1R), encoded by the IGF1R gene, is a receptor tyrosine kinase expressed in most tissues and cells. Its expression is developmentally regulated and influenced by nutrition, hormones, and intracellular factors, with high expression during growth and development, declining in adulthood [1]. The IGF1R protein is a heterotetramer (α2β2) of α and β subunits derived from a precursor protein, forming transmembrane αβ chains. The α chain is located extracellularly, while the β chain spans the cell membrane and is responsible for intracellular signal transduction after ligand stimulation. IGF1R binds Insulin-like Growth Factor-1 (IGF-1) with high affinity, mediating IGF-1's growth-promoting effects and regulating cell growth, differentiation, survival, and metabolism [1-4], and IGF1R defects are linked to growth retardation and diabetes [2-4]. Furthermore, IGF1R overexpression in tumors promotes proliferation, invasion, and metastasis, making it a cancer therapy target [3]. In thyroid eye disease (TED), an autoimmune disorder, activating IGF1R antibodies can be detected. IGF1R is overexpressed in T cells, B cells, and orbital fibroblasts of patients, forming a signal transduction complex with the thyroid-stimulating hormone receptor, thereby enhancing the effect of thyroid-stimulating hormone [5]. Therefore, targeting IGF1R to inhibit thyroid-stimulating hormone action is a therapeutic strategy for TED, improving exophthalmos [6].
hIGF1R mice are humanized models generated using gene editing technology by integrating the protein-coding sequence (CDS) encoding the extracellular domain of the human IGF1R protein and the intracellular domain of the mouse IGF1R protein into the mouse Igf1r gene locus, while retaining the endogenous gene sequence encoding the signal peptide of mouse IGF1R protein. Homozygous hIGF1R mice are viable and fertile, and can be used for studying the pathological mechanisms and treatments of growth retardation, diabetes, and cancer, as well as for screening, developing, and preclinical efficacy and safety evaluation of IGF1R-targeted drugs.
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