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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-hTL1A/hNLRP3
Product ID:
C001690
Strain:
C57BL/6N;6JCya
Status:
Description:
TNF-like ligand 1A (TL1A), also known as TNF superfamily member 15 (TNFSF15), is a member of the tumor necrosis factor (TNF) family encoded by the TNFSF15 gene in humans. TL1A acts as a ligand for death receptor 3 (DR3) and decoy receptor 3 (DcR3), providing a stimulatory signal for downstream pathways. It regulates the proliferation, activation, and apoptosis of effector cells, as well as cytokine and chemokine production. TL1A is expressed in various immune cells, including monocytes, macrophages, dendritic cells, and T cells, as well as in non-immune cells such as synovial fibroblasts and endothelial cells. It plays a crucial role in modulating immune responses by promoting the differentiation and survival of T cells, particularly Th17 cells involved in inflammatory processes [1]. TL1A enhances IL-2 responses in anti-CD3/CD28-stimulated T cells and synergizes with IL-12 and IL-18 to augment IFN-γ release in human T and NK cells, biasing T cell differentiation toward a Th1 phenotype [2]. Dysregulation of TL1A expression is implicated in autoimmune diseases, including inflammatory bowel disease (IBD), rheumatoid arthritis (RA), primary biliary cholangitis (PBC), systemic lupus erythematosus (SLE), and ankylosing spondylitis (AS) [1]. TL1A has emerged as a promising therapeutic target, with ongoing research focused on developing monoclonal antibodies and other biologics to neutralize TL1A and reduce inflammation in autoimmune disorders. Clinical trial results suggest that TL1A inhibition can be used in the treatment of various autoimmune diseases, particularly IBD [3-5].
The Cryopyrin protein, encoded by the NOD-like receptor family pyrin domain-containing 3 (NLRP3) gene, is a core component of the inflammasome in the innate immune system. As a member of the NOD-like receptor (NLR) family, NLRP3 is predominantly expressed in leukocytes and chondrocytes. It participates in the host defense against damage and infection by recognizing pathogen-associated molecular patterns (PAMPs) or damage-associated molecular patterns (DAMPs) to activate immune responses [6]. In its inactive monomeric state, NLRP3 senses intracellular damage signals, such as abnormal protein aggregates and lipid accumulation. Upon activation, NLRP3 oligomerizes, adopting an active conformation and assembling into inflammasome complexes, subsequently activating Caspase-1 to drive the maturation and secretion of pro-inflammatory cytokines, including IL-1β and IL-18 [6-7]. Activated NLRP3 not only induces the release of inflammatory cytokines but also triggers lytic cell pyroptosis. The intracellular components released during pyroptosis can further amplify inflammatory signals, forming a positive feedback loop of autoinflammation. Moreover, IL-1β can exacerbate the inflammatory cascade by stimulating the production of inflammatory markers such as IL-6 and high-sensitivity C-reactive protein (hsCRP) [8-9]. Given NLRP3's upstream position relative to IL-1β/IL-18 and other inflammatory factors, targeting its activity can effectively block the self-reinforcing mechanism of chronic inflammation, providing a significant therapeutic strategy for inflammation-related diseases [10]. The potential therapeutic areas include Alzheimer’s disease, Parkinson’s disease (via neuroinflammation modulation), inflammatory bowel disease, metabolic dysfunction-associated steatohepatitis (MASH), gout, and obesity-related metabolic inflammation [11-12].
B6-hTL1A/hNLRP3 mice are TL1A and NLRP3 double humanized mouse models obtained by mating TL1A humanized mouse models (Catalog No. C001603) with NLRP3 humanized mouse models (Catalog No. C001616). B6-hTL1A/hNLRP3 mice express human TL1A and NLRP3 genomic sequences under the control of mouse promoters. This model is capable of reproducing human TL1A and NLRP3 and is a valuable tool for studying autoimmune diseases and inflammation-related diseases. In addition, this model also provides a powerful preclinical research platform for evaluating the efficacy and mechanism of therapeutic drugs targeting TL1A and NLRP3.
TNF-like ligand 1A (TL1A), also known as TNF superfamily member 15 (TNFSF15), is a member of the tumor necrosis factor (TNF) family encoded by the TNFSF15 gene in humans. TL1A acts as a ligand for death receptor 3 (DR3) and decoy receptor 3 (DcR3), providing a stimulatory signal for downstream pathways. It regulates the proliferation, activation, and apoptosis of effector cells, as well as cytokine and chemokine production. TL1A is expressed in various immune cells, including monocytes, macrophages, dendritic cells, and T cells, as well as in non-immune cells such as synovial fibroblasts and endothelial cells. It plays a crucial role in modulating immune responses by promoting the differentiation and survival of T cells, particularly Th17 cells involved in inflammatory processes [1]. TL1A enhances IL-2 responses in anti-CD3/CD28-stimulated T cells and synergizes with IL-12 and IL-18 to augment IFN-γ release in human T and NK cells, biasing T cell differentiation toward a Th1 phenotype [2]. Dysregulation of TL1A expression is implicated in autoimmune diseases, including inflammatory bowel disease (IBD), rheumatoid arthritis (RA), primary biliary cholangitis (PBC), systemic lupus erythematosus (SLE), and ankylosing spondylitis (AS) [1]. TL1A has emerged as a promising therapeutic target, with ongoing research focused on developing monoclonal antibodies and other biologics to neutralize TL1A and reduce inflammation in autoimmune disorders. Clinical trial results suggest that TL1A inhibition can be used in the treatment of various autoimmune diseases, particularly IBD [3-5].
The Cryopyrin protein, encoded by the NOD-like receptor family pyrin domain-containing 3 (NLRP3) gene, is a core component of the inflammasome in the innate immune system. As a member of the NOD-like receptor (NLR) family, NLRP3 is predominantly expressed in leukocytes and chondrocytes. It participates in the host defense against damage and infection by recognizing pathogen-associated molecular patterns (PAMPs) or damage-associated molecular patterns (DAMPs) to activate immune responses [6]. In its inactive monomeric state, NLRP3 senses intracellular damage signals, such as abnormal protein aggregates and lipid accumulation. Upon activation, NLRP3 oligomerizes, adopting an active conformation and assembling into inflammasome complexes, subsequently activating Caspase-1 to drive the maturation and secretion of pro-inflammatory cytokines, including IL-1β and IL-18 [6-7]. Activated NLRP3 not only induces the release of inflammatory cytokines but also triggers lytic cell pyroptosis. The intracellular components released during pyroptosis can further amplify inflammatory signals, forming a positive feedback loop of autoinflammation. Moreover, IL-1β can exacerbate the inflammatory cascade by stimulating the production of inflammatory markers such as IL-6 and high-sensitivity C-reactive protein (hsCRP) [8-9]. Given NLRP3's upstream position relative to IL-1β/IL-18 and other inflammatory factors, targeting its activity can effectively block the self-reinforcing mechanism of chronic inflammation, providing a significant therapeutic strategy for inflammation-related diseases [10]. The potential therapeutic areas include Alzheimer’s disease, Parkinson’s disease (via neuroinflammation modulation), inflammatory bowel disease, metabolic dysfunction-associated steatohepatitis (MASH), gout, and obesity-related metabolic inflammation [11-12].
B6-hTL1A/hNLRP3 mice are TL1A and NLRP3 double humanized mouse models obtained by mating TL1A humanized mouse models (Catalog No. C001603) with NLRP3 humanized mouse models (Catalog No. C001616). B6-hTL1A/hNLRP3 mice express human TL1A and NLRP3 genomic sequences under the control of mouse promoters. This model is capable of reproducing human TL1A and NLRP3 and is a valuable tool for studying autoimmune diseases and inflammation-related diseases. In addition, this model also provides a powerful preclinical research platform for evaluating the efficacy and mechanism of therapeutic drugs targeting TL1A and NLRP3.
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.
huLAG3
Product ID:
C001787
Strain:
C57BL/6JCya
Status:
Description:
The Lymphocyte Activation Gene 3 (LAG3), also known as CD223, is a gene encoding a transmembrane protein that acts as an immune checkpoint receptor. It is primarily expressed on activated T cells (CD4+, CD8+, and regulatory T cells), natural killer (NK) cells, and plasmacytoid dendritic cells (pDCs) [1]. LAG3 plays a crucial role in immune regulation and homeostasis by delivering inhibitory signals to immune cells, particularly upon binding to its primary ligand, MHC class II molecules, and other ligands like FGL1. This binding leads to reduced T cell activation, proliferation, cytokine production, and cytolytic activity, ultimately contributing to T cell exhaustion in chronic infections and cancer [2]. Conversely, in autoimmune diseases, dysregulation of LAG3 can lead to rapid, immune-mediated tissue damage [3]. Therefore, LAG3 is implicated in a range of associated diseases, including various cancers (e.g., melanoma, colorectal cancer, non-small cell lung carcinoma, Hodgkin lymphoma, multiple myeloma), chronic infections (e.g., HIV, hepatitis B virus, tuberculosis), and autoimmune disorders (e.g., rheumatoid arthritis, Hashimoto's thyroiditis). Due to its significant role in immune suppression, LAG3 is a major target for cancer immunotherapy, with many anti-LAG3 monoclonal antibodies currently under clinical investigation [4].
The huLAG3 mouse is a humanized model constructed by replacing the endogenous extracellular domain of the mouse Lag3 gene with the human LAG3 extracellular domain. The murine signal peptide and aa.443~521 are preserved. huLAG3 mice can be used for research into the pathogenesis of various diseases, including malignant tumors, chronic infections, and autoimmune diseases, as well as for the screening, development, and safety evaluation of LAG3-targeted drugs.
The Lymphocyte Activation Gene 3 (LAG3), also known as CD223, is a gene encoding a transmembrane protein that acts as an immune checkpoint receptor. It is primarily expressed on activated T cells (CD4+, CD8+, and regulatory T cells), natural killer (NK) cells, and plasmacytoid dendritic cells (pDCs) [1]. LAG3 plays a crucial role in immune regulation and homeostasis by delivering inhibitory signals to immune cells, particularly upon binding to its primary ligand, MHC class II molecules, and other ligands like FGL1. This binding leads to reduced T cell activation, proliferation, cytokine production, and cytolytic activity, ultimately contributing to T cell exhaustion in chronic infections and cancer [2]. Conversely, in autoimmune diseases, dysregulation of LAG3 can lead to rapid, immune-mediated tissue damage [3]. Therefore, LAG3 is implicated in a range of associated diseases, including various cancers (e.g., melanoma, colorectal cancer, non-small cell lung carcinoma, Hodgkin lymphoma, multiple myeloma), chronic infections (e.g., HIV, hepatitis B virus, tuberculosis), and autoimmune disorders (e.g., rheumatoid arthritis, Hashimoto's thyroiditis). Due to its significant role in immune suppression, LAG3 is a major target for cancer immunotherapy, with many anti-LAG3 monoclonal antibodies currently under clinical investigation [4].
The huLAG3 mouse is a humanized model constructed by replacing the endogenous extracellular domain of the mouse Lag3 gene with the human LAG3 extracellular domain. The murine signal peptide and aa.443~521 are preserved. huLAG3 mice can be used for research into the pathogenesis of various diseases, including malignant tumors, chronic infections, and autoimmune diseases, as well as for the screening, development, and safety evaluation of LAG3-targeted drugs.
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.
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