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Abca4/Rdh8-DKO
Product ID:
C001968
Strain:
C57BL/6JCya
Status:
Description:
The Abca4/Rdh8-DKO mouse is a dual-gene knockout model obtained by mating Rdh8-KO mice (catalog No.: C001969) with Abca4-KO mice (catalog No.: C002024). This model can be used to investigate the pathogenic mechanisms and therapeutic strategies of diseases, including Stargardt disease (STGD) and age‑related macular degeneration (AMD), and facilitates the evaluation of synergistic effects of polygenic therapies.
The Abca4/Rdh8-DKO mouse is a dual-gene knockout model obtained by mating Rdh8-KO mice (catalog No.: C001969) with Abca4-KO mice (catalog No.: C002024). This model can be used to investigate the pathogenic mechanisms and therapeutic strategies of diseases, including Stargardt disease (STGD) and age‑related macular degeneration (AMD), and facilitates the evaluation of synergistic effects of polygenic therapies.
Abca4-KO
Product ID:
C002024
Strain:
C57BL/6JCya
Status:
Description:
Stargardt disease (STGD), a hereditary macular dystrophy, is characterized by the presence of yellowish flecks within the retinal pigment epithelium (RPE), ultimately culminating in macular atrophy. Typically manifesting in childhood and adolescence, STGD leads to progressive central vision loss and mild dyschromatopsia. Fundoscopic examination may reveal pale yellow lesions exhibiting a characteristic gold foil-like sheen, accompanied by yellow-white spots surrounding the posterior pole. In advanced stages, atrophy of the RPE, photoreceptors, and choriocapillaris is observed. This bilateral and typically synchronous condition affects both eyes with comparable incidence across sexes, estimated between 1/8,000 and 1/13,000. STGD is predominantly an autosomal recessive disorder, with mutations in the ABCA4 gene accounting for approximately 95% of cases. ABCA4 encodes a retina-specific ABC transporter protein crucial for the clearance of retinal derivatives and toxic metabolites generated during rhodopsin photobleaching. Consequently, ABCA4 mutations result in the accumulation of these cytotoxic substances, triggering apoptosis of both RPE and photoreceptor cells and ultimately driving retinal degeneration. Notably, ABCA4 mutations have been implicated in a spectrum of retinal diseases, including STGD, cone-rod dystrophy (CRD), age-related macular degeneration (AMD), and retinitis pigmentosa (RP), with the specific clinical phenotype correlating with the nature and severity of the ABCA4 mutation.
This strain is an Abca4 gene knockout (KO) mouse model. Gene-editing technology was used to delete the protein-coding sequence of the Abca4 gene (the homolog of the human ABCA4 gene) in mice. Previous studies have demonstrated that Abca4 KO mice exhibit delayed dark adaptation following photobleaching and a slow progression of photoreceptor degeneration[1]. Homozygous Abca4-KO mice are viable and fertile.
Stargardt disease (STGD), a hereditary macular dystrophy, is characterized by the presence of yellowish flecks within the retinal pigment epithelium (RPE), ultimately culminating in macular atrophy. Typically manifesting in childhood and adolescence, STGD leads to progressive central vision loss and mild dyschromatopsia. Fundoscopic examination may reveal pale yellow lesions exhibiting a characteristic gold foil-like sheen, accompanied by yellow-white spots surrounding the posterior pole. In advanced stages, atrophy of the RPE, photoreceptors, and choriocapillaris is observed. This bilateral and typically synchronous condition affects both eyes with comparable incidence across sexes, estimated between 1/8,000 and 1/13,000. STGD is predominantly an autosomal recessive disorder, with mutations in the ABCA4 gene accounting for approximately 95% of cases. ABCA4 encodes a retina-specific ABC transporter protein crucial for the clearance of retinal derivatives and toxic metabolites generated during rhodopsin photobleaching. Consequently, ABCA4 mutations result in the accumulation of these cytotoxic substances, triggering apoptosis of both RPE and photoreceptor cells and ultimately driving retinal degeneration. Notably, ABCA4 mutations have been implicated in a spectrum of retinal diseases, including STGD, cone-rod dystrophy (CRD), age-related macular degeneration (AMD), and retinitis pigmentosa (RP), with the specific clinical phenotype correlating with the nature and severity of the ABCA4 mutation.
This strain is an Abca4 gene knockout (KO) mouse model. Gene-editing technology was used to delete the protein-coding sequence of the Abca4 gene (the homolog of the human ABCA4 gene) in mice. Previous studies have demonstrated that Abca4 KO mice exhibit delayed dark adaptation following photobleaching and a slow progression of photoreceptor degeneration[1]. Homozygous Abca4-KO mice are viable and fertile.
B6-huPRPF31
Product ID:
C001863
Strain:
C57BL/6JCya
Status:
Description:
The PRPF31 gene, located on chromosome 19q13.4, encodes the PRP31 protein, a crucial component of the spliceosome, a large molecular machine essential for pre-mRNA splicing. This gene is ubiquitously expressed, meaning it is active in nearly all cell types and tissues throughout the body, as its function is fundamental to general cell metabolism and survival [1]. The encoded protein, also known as Protein 61K, plays a critical role in the assembly of the U4/U6·U5 tri-snRNP complex, a vital step in the splicing process [2]. Mutations in the PRPF31 gene are primarily associated with autosomal dominant retinitis pigmentosa (adRP), a progressive inherited retinal disease. Although the gene is expressed ubiquitously, the disease phenotype is retina-specific, with cellular labeling and studies showing that photoreceptor and retinal pigment epithelial (RPE) cells are the most affected, leading to their dysfunction and death [3]. This is often attributed to haploinsufficiency, where a single mutated copy of the gene is not sufficient to produce the necessary amount of functional protein, particularly in the retina which has a high demand for splicing activity [4].
The B6-huPRPF31 mouse model was generated by replacing sequences from the ATG start codon to the TGA stop codon of the endogenous mouse Prpf31 gene with the sequences from the ATG start codon to the TGA stop codon of the human PRPF31 gene. This model can be used to study the pathological mechanisms and therapeutic approaches for autosomal dominant retinitis pigmentosa (adRP), as well as for the development of PRPF31-targeted drugs.
The PRPF31 gene, located on chromosome 19q13.4, encodes the PRP31 protein, a crucial component of the spliceosome, a large molecular machine essential for pre-mRNA splicing. This gene is ubiquitously expressed, meaning it is active in nearly all cell types and tissues throughout the body, as its function is fundamental to general cell metabolism and survival [1]. The encoded protein, also known as Protein 61K, plays a critical role in the assembly of the U4/U6·U5 tri-snRNP complex, a vital step in the splicing process [2]. Mutations in the PRPF31 gene are primarily associated with autosomal dominant retinitis pigmentosa (adRP), a progressive inherited retinal disease. Although the gene is expressed ubiquitously, the disease phenotype is retina-specific, with cellular labeling and studies showing that photoreceptor and retinal pigment epithelial (RPE) cells are the most affected, leading to their dysfunction and death [3]. This is often attributed to haploinsufficiency, where a single mutated copy of the gene is not sufficient to produce the necessary amount of functional protein, particularly in the retina which has a high demand for splicing activity [4].
The B6-huPRPF31 mouse model was generated by replacing sequences from the ATG start codon to the TGA stop codon of the endogenous mouse Prpf31 gene with the sequences from the ATG start codon to the TGA stop codon of the human PRPF31 gene. This model can be used to study the pathological mechanisms and therapeutic approaches for autosomal dominant retinitis pigmentosa (adRP), as well as for the development of PRPF31-targeted drugs.
B6-hC3/hTFRC (CDS)
Product ID:
C001608
Strain:
C57BL/6JCya;C57BL/6NCya
Status:
Description:
Complement component C3 plays a central role in activating the complement system and is the most abundant complement protein in human plasma, primarily synthesized in the liver. As part of the innate immune system, the complement system is activated during tissue damage and pathogen invasion, playing a crucial role in the inflammatory response, host homeostasis, and pathogen defense. The complement cascade is activated through the classical pathway, alternative pathway, and lectin pathway, all of which generate C3 convertase, which cleaves C3 into C3a and C3b. C3a is a potent anaphylatoxin with pro-inflammatory activity, while C3b is a regulator that induces C5 cleavage, thereby participating in the dissolution and clearance of immune complexes. Mutations in this gene are associated with atypical hemolytic uremic syndrome (aHUS) and age-related macular degeneration (AMD). Deficiencies in C3 and C3-derived peptides can lead to autoimmune diseases (such as rheumatoid arthritis, systemic lupus erythematosus, and vasculitis) and make individuals susceptible to recurrent respiratory infections and infections caused by encapsulated organisms. Conversely, excessive activation of C3 and related complement components is associated with kidney diseases (immune complex glomerulonephritis, hemolytic uremic syndrome, lupus nephritis, membranous nephropathy, and immune-mediated nephropathy) [1-2].
The Transferrin receptor (TFRC) gene encodes Transferrin Receptor 1 (TFR1), a protein that is expressed at low levels in most normal cells but shows increased expression in highly proliferative cells, such as basal epidermal cells, intestinal epithelium, and certain activated immune cells. Brain capillary endothelial cells, which constitute the blood-brain barrier (BBB), also express this receptor at high levels [3]. TFR1 plays a critical role in maintaining iron metabolism and homeostasis by facilitating receptor-mediated endocytosis of iron-bound transferrin (Tf) via Tf cycling, thereby promoting iron uptake [4]. Cellular iron deficiency can lead to apoptosis, while cellular transformation requires substantial iron to sustain proliferation, with iron overload contributing to tumor progression. The high expression of TFR1 in many tumors makes it a potential tumor marker, offering a target for therapies to inhibit tumor growth and metastasis [3]. Moreover, TFR1 is implicated in anemia and iron metabolism disorders. Studies have shown that elevated TFR1 expression in cardiomyocytes is associated with exacerbated inflammation in myocarditis patients [5]. 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 [6-7]. 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 B6-hC3/hTFRC(CDS) mouse model is a humanized model obtained by breeding huC3 mice (Catalog No.: C001955) with B6-hTFRC(CDS) mice (Catalog No.: C001584). This model can be used for research on complement-mediated diseases, iron metabolism disorders, neurodegenerative diseases, and tumor development, aiding in studying C3/TFRC-targeted drugs.
Complement component C3 plays a central role in activating the complement system and is the most abundant complement protein in human plasma, primarily synthesized in the liver. As part of the innate immune system, the complement system is activated during tissue damage and pathogen invasion, playing a crucial role in the inflammatory response, host homeostasis, and pathogen defense. The complement cascade is activated through the classical pathway, alternative pathway, and lectin pathway, all of which generate C3 convertase, which cleaves C3 into C3a and C3b. C3a is a potent anaphylatoxin with pro-inflammatory activity, while C3b is a regulator that induces C5 cleavage, thereby participating in the dissolution and clearance of immune complexes. Mutations in this gene are associated with atypical hemolytic uremic syndrome (aHUS) and age-related macular degeneration (AMD). Deficiencies in C3 and C3-derived peptides can lead to autoimmune diseases (such as rheumatoid arthritis, systemic lupus erythematosus, and vasculitis) and make individuals susceptible to recurrent respiratory infections and infections caused by encapsulated organisms. Conversely, excessive activation of C3 and related complement components is associated with kidney diseases (immune complex glomerulonephritis, hemolytic uremic syndrome, lupus nephritis, membranous nephropathy, and immune-mediated nephropathy) [1-2].
The Transferrin receptor (TFRC) gene encodes Transferrin Receptor 1 (TFR1), a protein that is expressed at low levels in most normal cells but shows increased expression in highly proliferative cells, such as basal epidermal cells, intestinal epithelium, and certain activated immune cells. Brain capillary endothelial cells, which constitute the blood-brain barrier (BBB), also express this receptor at high levels [3]. TFR1 plays a critical role in maintaining iron metabolism and homeostasis by facilitating receptor-mediated endocytosis of iron-bound transferrin (Tf) via Tf cycling, thereby promoting iron uptake [4]. Cellular iron deficiency can lead to apoptosis, while cellular transformation requires substantial iron to sustain proliferation, with iron overload contributing to tumor progression. The high expression of TFR1 in many tumors makes it a potential tumor marker, offering a target for therapies to inhibit tumor growth and metastasis [3]. Moreover, TFR1 is implicated in anemia and iron metabolism disorders. Studies have shown that elevated TFR1 expression in cardiomyocytes is associated with exacerbated inflammation in myocarditis patients [5]. 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 [6-7]. 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 B6-hC3/hTFRC(CDS) mouse model is a humanized model obtained by breeding huC3 mice (Catalog No.: C001955) with B6-hTFRC(CDS) mice (Catalog No.: C001584). This model can be used for research on complement-mediated diseases, iron metabolism disorders, neurodegenerative diseases, and tumor development, aiding in studying C3/TFRC-targeted drugs.
B6-huGUCY2D
Product ID:
C001798
Strain:
C57BL/6JCya
Status:
Description:
Gucy2e, which is the gene encoding mouse retinal guanylate cyclase 1 (RetGC1), is a key enzyme in the retina responsible for synthesizing the second messenger cyclic guanosine monophosphate (cGMP). cGMP plays an important role in the process of retinal phototransduction. Especially when restoring the dark state, it regulates the opening and closing of cGMP-gated calcium-sodium channels (CNG) and controls the influx of calcium ions (Ca2+). Mutations in Gucy2e can lead to the loss of function of retinal guanylate cyclase 1, thereby affecting the normal function of retinal photoreceptor cells [1]. Studies have shown that mutations in the Gucy2e gene are one of the main causes of Leber congenital amaurosis type 1 (LCA1). In humans, the GUCY2D gene encodes RetGC1, and its mutations lead to the occurrence of LCA1 [2]. Gene therapy offers a new treatment strategy for LCA1 patients. By delivering the GUCY2D gene or its normal copy into retinal photoreceptor cells via adeno-associated virus (AAV) vectors, it is possible to restore the function of rod and cone cells and improve visual behavior. In addition to gene therapy, researchers have explored other therapeutic approaches. For example, using double-stranded RNA interference (RNAi) technology can reduce the expression of the GUCY2D gene, thereby slowing the progression of retinal degeneration [1-2]. Apart from LCA1, the GUCY2D gene is also associated with other retinal diseases; recessive mutations in the GUCY2D gene cause cone-rod dystrophy (CORD). In a mouse model of retinitis pigmentosa (RP), knocking down the expression of the Gucy2e gene can increase the survival rate of photoreceptors and slow down the process of retinal degeneration [3].
The B6-huGUCY2D mouse is a humanized model constructed through gene-editing technology, in which the sequences from p.A55 to 3'UTR of the endogenous mouse Gucy2e gene are replaced with the sequences from p.A52 to 3'UTR of the human GUCY2D gene. The murine signal peptide is remained. This model can be used for research on diseases such as Leber congenital amaurosis type 1 (LCA1), cone-rod dystrophy (CORD), and retinitis pigmentosa (RP), as well as for screening, development, and preclinical evaluation of GUCY2D-targeted therapeutics.
Gucy2e, which is the gene encoding mouse retinal guanylate cyclase 1 (RetGC1), is a key enzyme in the retina responsible for synthesizing the second messenger cyclic guanosine monophosphate (cGMP). cGMP plays an important role in the process of retinal phototransduction. Especially when restoring the dark state, it regulates the opening and closing of cGMP-gated calcium-sodium channels (CNG) and controls the influx of calcium ions (Ca2+). Mutations in Gucy2e can lead to the loss of function of retinal guanylate cyclase 1, thereby affecting the normal function of retinal photoreceptor cells [1]. Studies have shown that mutations in the Gucy2e gene are one of the main causes of Leber congenital amaurosis type 1 (LCA1). In humans, the GUCY2D gene encodes RetGC1, and its mutations lead to the occurrence of LCA1 [2]. Gene therapy offers a new treatment strategy for LCA1 patients. By delivering the GUCY2D gene or its normal copy into retinal photoreceptor cells via adeno-associated virus (AAV) vectors, it is possible to restore the function of rod and cone cells and improve visual behavior. In addition to gene therapy, researchers have explored other therapeutic approaches. For example, using double-stranded RNA interference (RNAi) technology can reduce the expression of the GUCY2D gene, thereby slowing the progression of retinal degeneration [1-2]. Apart from LCA1, the GUCY2D gene is also associated with other retinal diseases; recessive mutations in the GUCY2D gene cause cone-rod dystrophy (CORD). In a mouse model of retinitis pigmentosa (RP), knocking down the expression of the Gucy2e gene can increase the survival rate of photoreceptors and slow down the process of retinal degeneration [3].
The B6-huGUCY2D mouse is a humanized model constructed through gene-editing technology, in which the sequences from p.A55 to 3'UTR of the endogenous mouse Gucy2e gene are replaced with the sequences from p.A52 to 3'UTR of the human GUCY2D gene. The murine signal peptide is remained. This model can be used for research on diseases such as Leber congenital amaurosis type 1 (LCA1), cone-rod dystrophy (CORD), and retinitis pigmentosa (RP), as well as for screening, development, and preclinical evaluation of GUCY2D-targeted therapeutics.
B6-huCFB/huC5
Product ID:
C001918
Strain:
C57BL/6JCya
Status:
Description:
B6-huCFB/huC5 mice are a dual-gene humanized model obtained by mating B6-huCFB mice (catalog No.: C001710) with B6-huC5 mice (catalog No.: C001824). This model can be used for research on immune-related diseases such as age-related macular degeneration (AMD), atypical hemolytic uremic syndrome (aHUS), and systemic lupus erythematosus (SLE), as well as for the development of CFB/C5-targeted drugs.
B6-huCFB/huC5 mice are a dual-gene humanized model obtained by mating B6-huCFB mice (catalog No.: C001710) with B6-huC5 mice (catalog No.: C001824). This model can be used for research on immune-related diseases such as age-related macular degeneration (AMD), atypical hemolytic uremic syndrome (aHUS), and systemic lupus erythematosus (SLE), as well as for the development of CFB/C5-targeted drugs.
B6-huC3*R102G
Product ID:
C001896
Strain:
C57BL/6JCya
Status:
Description:
Complement component C3 plays a central role in activating the complement system and is the most abundant complement protein in human plasma, primarily synthesized in the liver. As part of the innate immune system, the complement system is activated during tissue damage and pathogen invasion, playing a crucial role in the inflammatory response, host homeostasis, and pathogen defense. The complement cascade is activated through the classical pathway, alternative pathway, and lectin pathway, all of which generate C3 convertase, which cleaves C3 into C3a and C3b. C3a is a potent anaphylatoxin with pro-inflammatory activity, while C3b is a regulator that induces C5 cleavage, thereby participating in the dissolution and clearance of immune complexes. Mutations in this gene are associated with atypical hemolytic uremic syndrome (aHUS) and age-related macular degeneration (AMD). Deficiencies in C3 and C3-derived peptides can lead to autoimmune diseases (such as rheumatoid arthritis, systemic lupus erythematosus, and vasculitis) and make individuals susceptible to recurrent respiratory infections and infections caused by encapsulated organisms. Conversely, excessive activation of C3 and related complement components is associated with kidney diseases (immune complex glomerulonephritis, hemolytic uremic syndrome, lupus nephritis, membranous nephropathy, and immune-mediated nephropathy) [1-2]. Specifically, the C3*R102G mutation involves a substitution of the amino acid arginine (R) with glycine (G) at position 102 of the mature C3 protein, often leading to a gain-of-function that results in the protein being more susceptible to cleavage and thus causing uncontrolled complement activation [3].
The B6-huC3*R102G mouse is a humanized disease model constructed by gene-editing technology. The sequences from upstream of exon 1 to the TGA stop codon of mouse C3 were replaced with the sequences from upstream of exon 1 to downstream of exon 41 of human C3. The p.R102G (CGC to GGC) mutation was introduced into human C3 exon 3. This model is suitable for the mechanistic study of immune-related diseases caused by uncontrolled activation of the complement system (such as age-related macular degeneration (AMD), etc.) and the development of therapies targeting C3 R102G.
Complement component C3 plays a central role in activating the complement system and is the most abundant complement protein in human plasma, primarily synthesized in the liver. As part of the innate immune system, the complement system is activated during tissue damage and pathogen invasion, playing a crucial role in the inflammatory response, host homeostasis, and pathogen defense. The complement cascade is activated through the classical pathway, alternative pathway, and lectin pathway, all of which generate C3 convertase, which cleaves C3 into C3a and C3b. C3a is a potent anaphylatoxin with pro-inflammatory activity, while C3b is a regulator that induces C5 cleavage, thereby participating in the dissolution and clearance of immune complexes. Mutations in this gene are associated with atypical hemolytic uremic syndrome (aHUS) and age-related macular degeneration (AMD). Deficiencies in C3 and C3-derived peptides can lead to autoimmune diseases (such as rheumatoid arthritis, systemic lupus erythematosus, and vasculitis) and make individuals susceptible to recurrent respiratory infections and infections caused by encapsulated organisms. Conversely, excessive activation of C3 and related complement components is associated with kidney diseases (immune complex glomerulonephritis, hemolytic uremic syndrome, lupus nephritis, membranous nephropathy, and immune-mediated nephropathy) [1-2]. Specifically, the C3*R102G mutation involves a substitution of the amino acid arginine (R) with glycine (G) at position 102 of the mature C3 protein, often leading to a gain-of-function that results in the protein being more susceptible to cleavage and thus causing uncontrolled complement activation [3].
The B6-huC3*R102G mouse is a humanized disease model constructed by gene-editing technology. The sequences from upstream of exon 1 to the TGA stop codon of mouse C3 were replaced with the sequences from upstream of exon 1 to downstream of exon 41 of human C3. The p.R102G (CGC to GGC) mutation was introduced into human C3 exon 3. This model is suitable for the mechanistic study of immune-related diseases caused by uncontrolled activation of the complement system (such as age-related macular degeneration (AMD), etc.) and the development of therapies targeting C3 R102G.
B6-huCFB/hMASP2
Product ID:
C001919
Strain:
C57BL/6Cya
Status:
Description:
Complement factor B (CFB) is a circulating serine protease that plays a central role in the alternative pathway of the complement system, a critical component of innate immunity. Encoded by the CFB gene, this protein is primarily synthesized by hepatocytes, adipocytes, and monocytes, reflecting its systemic and local involvement in immune surveillance and inflammation [1]. Upon activation by factor D, CFB forms the active enzyme factor Bb, which, in complex with complement component C3b, constitutes the alternative pathway C3 convertase (C3bBb). This convertase catalyzes the cleavage of C3 into the anaphylatoxin C3a and the opsonin C3b, leading to the amplification of the complement cascade and the subsequent elimination of pathogens and damaged cells [2]. Dysregulation of CFB activity, often stemming from genetic polymorphisms within the CFB locus, has been implicated in the pathogenesis of several human diseases, including age-related macular degeneration (AMD), atypical hemolytic uremic syndrome (aHUS), and systemic lupus erythematosus (SLE), underscoring the delicate balance required for proper complement regulation and immune homeostasis [3-4]. These associations highlight CFB as a key mediator of both protective and pathological immune responses.
The MASP2 gene encodes MASP-2, a serum serine protease that serves as a key mediator in complement system activation. MASP-2 initiates the lectin pathway by forming complexes with pattern recognition molecules such as mannose-binding lectin (MBL) and ficolins. Upon pathogen recognition by MBL, MASP-2 is activated and subsequently cleaves complement components C4 and C2, leading to the generation of C3 convertase and triggering downstream complement activation. Beyond its role in the complement cascade, MASP-2 also contributes to the coagulation pathway by cleaving prothrombin to generate thrombin, thereby linking innate immunity and hemostasis [5]. Emerging evidence highlights the clinical significance of MASP2 gene polymorphisms, which are associated with altered susceptibility to infectious diseases and immune-related disorders. Reduced plasma levels of MASP-2 have been linked to increased vulnerability to HIV infection, while elevated MASP-2 activity may exacerbate inflammatory responses [6]. Given its pivotal role in immune regulation, MASP-2 has emerged as a promising therapeutic target. Inhibition of MASP-2 is currently under investigation as a potential strategy for treating a range of conditions, including IgA nephropathy (IgAN) [7], atypical hemolytic uremic syndrome (aHUS), and transplant-associated thrombotic microangiopathy (TA-TMA) [8].
The B6-huCFB/hMASP2 mouse is a dual-gene humanized model obtained by mating B6-huCFB mice (catalog number: C001710) with B6-hMASP2 mice (catalog number: C001592). This model can be used for research on the pathological mechanisms and treatment methods of autoimmune diseases and infectious diseases, as well as the development of CFB/MASP2-targeted drugs.
Complement factor B (CFB) is a circulating serine protease that plays a central role in the alternative pathway of the complement system, a critical component of innate immunity. Encoded by the CFB gene, this protein is primarily synthesized by hepatocytes, adipocytes, and monocytes, reflecting its systemic and local involvement in immune surveillance and inflammation [1]. Upon activation by factor D, CFB forms the active enzyme factor Bb, which, in complex with complement component C3b, constitutes the alternative pathway C3 convertase (C3bBb). This convertase catalyzes the cleavage of C3 into the anaphylatoxin C3a and the opsonin C3b, leading to the amplification of the complement cascade and the subsequent elimination of pathogens and damaged cells [2]. Dysregulation of CFB activity, often stemming from genetic polymorphisms within the CFB locus, has been implicated in the pathogenesis of several human diseases, including age-related macular degeneration (AMD), atypical hemolytic uremic syndrome (aHUS), and systemic lupus erythematosus (SLE), underscoring the delicate balance required for proper complement regulation and immune homeostasis [3-4]. These associations highlight CFB as a key mediator of both protective and pathological immune responses.
The MASP2 gene encodes MASP-2, a serum serine protease that serves as a key mediator in complement system activation. MASP-2 initiates the lectin pathway by forming complexes with pattern recognition molecules such as mannose-binding lectin (MBL) and ficolins. Upon pathogen recognition by MBL, MASP-2 is activated and subsequently cleaves complement components C4 and C2, leading to the generation of C3 convertase and triggering downstream complement activation. Beyond its role in the complement cascade, MASP-2 also contributes to the coagulation pathway by cleaving prothrombin to generate thrombin, thereby linking innate immunity and hemostasis [5]. Emerging evidence highlights the clinical significance of MASP2 gene polymorphisms, which are associated with altered susceptibility to infectious diseases and immune-related disorders. Reduced plasma levels of MASP-2 have been linked to increased vulnerability to HIV infection, while elevated MASP-2 activity may exacerbate inflammatory responses [6]. Given its pivotal role in immune regulation, MASP-2 has emerged as a promising therapeutic target. Inhibition of MASP-2 is currently under investigation as a potential strategy for treating a range of conditions, including IgA nephropathy (IgAN) [7], atypical hemolytic uremic syndrome (aHUS), and transplant-associated thrombotic microangiopathy (TA-TMA) [8].
The B6-huCFB/hMASP2 mouse is a dual-gene humanized model obtained by mating B6-huCFB mice (catalog number: C001710) with B6-hMASP2 mice (catalog number: C001592). This model can be used for research on the pathological mechanisms and treatment methods of autoimmune diseases and infectious diseases, as well as the development of CFB/MASP2-targeted drugs.
B6-hNRL
Product ID:
C001799
Strain:
C57BL/6JCya
Status:
Description:
The NRL (neural retina leucine zipper) gene encodes a basic motif-leucine zipper (bZIP) transcription factor of the Maf subfamily, which plays a critical role in the development and function of photoreceptor cells, particularly rods, in the mammalian retina. Gene expression of NRL is highly specific to the retina, appearing in postmitotic neuronal cells during embryonic development and maintaining high levels in mature neural retina. It functions as a master regulator of rod photoreceptor cell fate, working in conjunction with other transcription factors like CRX and NR2E3 to activate rod-specific genes (e.g., rhodopsin) and repress cone-specific genes. Cellular tissues predominantly labeled by NRL include rod photoreceptor nuclei, with some labeling also observed in rod and cone inner segments, somata, and synapses, and weak labeling in the cytoplasm of scattered cells in the inner nuclear and ganglion cell layers. Mutations in the NRL gene are associated with various inherited retinal degenerative diseases, most notably Retinitis Pigmentosa (RP), which can manifest as autosomal dominant (Retinitis Pigmentosa 27) or autosomal recessive forms (clumped pigmentary retinal degeneration, resembling Enhanced S-cone Syndrome), leading to progressive loss of vision [1-3].
The B6-hNRL mouse is a humanized model, constructed by replacing the sequences from 5'UTR to 3'UTR of the endogenous mouse Nrl gene with the corresponding human NRL gene sequence. B6-hNRL mice can be used for research into the pathogenesis of various inherited retinal degenerative diseases such as Retinitis Pigmentosa (RP). They are also useful for the screening, development, and safety evaluation of NRL-targeted drugs.
The NRL (neural retina leucine zipper) gene encodes a basic motif-leucine zipper (bZIP) transcription factor of the Maf subfamily, which plays a critical role in the development and function of photoreceptor cells, particularly rods, in the mammalian retina. Gene expression of NRL is highly specific to the retina, appearing in postmitotic neuronal cells during embryonic development and maintaining high levels in mature neural retina. It functions as a master regulator of rod photoreceptor cell fate, working in conjunction with other transcription factors like CRX and NR2E3 to activate rod-specific genes (e.g., rhodopsin) and repress cone-specific genes. Cellular tissues predominantly labeled by NRL include rod photoreceptor nuclei, with some labeling also observed in rod and cone inner segments, somata, and synapses, and weak labeling in the cytoplasm of scattered cells in the inner nuclear and ganglion cell layers. Mutations in the NRL gene are associated with various inherited retinal degenerative diseases, most notably Retinitis Pigmentosa (RP), which can manifest as autosomal dominant (Retinitis Pigmentosa 27) or autosomal recessive forms (clumped pigmentary retinal degeneration, resembling Enhanced S-cone Syndrome), leading to progressive loss of vision [1-3].
The B6-hNRL mouse is a humanized model, constructed by replacing the sequences from 5'UTR to 3'UTR of the endogenous mouse Nrl gene with the corresponding human NRL gene sequence. B6-hNRL mice can be used for research into the pathogenesis of various inherited retinal degenerative diseases such as Retinitis Pigmentosa (RP). They are also useful for the screening, development, and safety evaluation of NRL-targeted drugs.
B6-hVEGFA/hANGPT2
Product ID:
C001691
Strain:
C57BL/6JCya
Status:
Description:
The Vascular Endothelial Growth Factor (VEGF) family is a group of particular endothelial growth factors intimately associated with angiogenesis. These factors promote increased vascular permeability, extracellular matrix degeneration, vascular endothelial cell migration and proliferation, and are capable of stimulating angiogenesis and increasing the permeability of existing vessels. As such, they play a pivotal role in normal vascular development and wound healing. The VEGF family comprises VEGFA, VEGFB, VEGFC, VEGFD, VEGFE, and PLGF [1]. Of these, VEGFA is the most commonly targeted in research related to neovascular ophthalmic diseases due to its crucial role in the proliferation, migration, and formation of endothelial cell microvessels [2]. Overexpression of VEGFA in the eye can result in abnormal vascular growth and leakage, leading to various ophthalmic diseases such as Age-Related Macular Degeneration (AMD), Diabetic Retinopathy (DR), and corneal neovascularization [2-3]. The progression of solid tumors depends on vascularization and angiogenesis within malignant tissues, with VEGFA playing a crucial role among various pro-angiogenic factors. The VEGFA gene is upregulated in many known tumors, correlating with tumor staging and progression. Blocking VEGFA may lead to vascular network regression, thereby inhibiting tumor growth [4]. Thus, VEGFA is an important target for anti-angiogenic cancer therapies.
Angiopoietin-2 (ANG2/ANGPT2), encoded by the ANGPT2 gene, is a secreted glycoprotein of the angiopoietin family predominantly expressed in vascular endothelial cells and stored in Weibel-Palade bodies for rapid release. ANGPT2 regulates vascular biology in a context-dependent manner by binding to the Tie2 tyrosine kinase receptor, playing pivotal roles in angiogenesis and vascular remodeling [5]. Its molecular structure includes a coiled-coil domain facilitating oligomerization and a fibrinogen-like domain critical for receptor binding. Functionally, ANGPT2 acts as a partial Tie2 receptor antagonist to Angiopoietin-1 (ANG1). Through competitive inhibition of Tie2 signaling, ANGPT2 disrupts vascular endothelial homeostasis, inducing increased vascular permeability and structural plasticity. In synergy with vascular endothelial growth factor (VEGF), ANGPT2 drives angiogenic sprouting and pathological neovascularization. Conversely, under conditions of low or absent VEGF, it mediates vascular regression [6-7]. ANGPT2 plays a central pathological role in vascular proliferative diseases such as tumor angiogenesis, diabetic retinopathy, and age-related macular degeneration. Endothelial cell activation and inflammatory responses mediated by ANGPT2 also contribute to the pathogenesis of inflammatory conditions including sepsis and rheumatoid arthritis [8]. Therapeutic strategies targeting ANGPT2 include monoclonal antibodies (e.g., Nesvacumab) and peptide-Fc fusion proteins (e.g., Trebananib), often combined with VEGF inhibitors to enhance anti-angiogenic efficacy [9-10]. Current research efforts are focused on optimizing ANGPT2/VEGF dual-target inhibition strategies and developing biomarkers, aiming to improve clinical outcomes in tumors and ocular vascular diseases and validate its translational value as a therapeutic target in vascular and inflammatory diseases [11-12].
B6-hVEGFA/hANGPT2 mice are VEGFA and ANGPT2 double humanized mouse models obtained by mating VEGFA humanized mouse models (Catalog No. C001555) with ANGPT2 humanized mouse models (Catalog No. C001615). B6-hVEGFA/hANGPT2 mice express human VEGFA and ANGPT2 genomic sequences under the control of mouse promoters. This model is capable of reproducing human VEGFA and ANGPT2 and is a valuable tool for studying cancer, vascular diseases and autoimmune disorders. In addition, this model also provides a powerful preclinical research platform for evaluating the efficacy and mechanism of therapeutic drugs targeting VEGFA and ANGPT2.
The Vascular Endothelial Growth Factor (VEGF) family is a group of particular endothelial growth factors intimately associated with angiogenesis. These factors promote increased vascular permeability, extracellular matrix degeneration, vascular endothelial cell migration and proliferation, and are capable of stimulating angiogenesis and increasing the permeability of existing vessels. As such, they play a pivotal role in normal vascular development and wound healing. The VEGF family comprises VEGFA, VEGFB, VEGFC, VEGFD, VEGFE, and PLGF [1]. Of these, VEGFA is the most commonly targeted in research related to neovascular ophthalmic diseases due to its crucial role in the proliferation, migration, and formation of endothelial cell microvessels [2]. Overexpression of VEGFA in the eye can result in abnormal vascular growth and leakage, leading to various ophthalmic diseases such as Age-Related Macular Degeneration (AMD), Diabetic Retinopathy (DR), and corneal neovascularization [2-3]. The progression of solid tumors depends on vascularization and angiogenesis within malignant tissues, with VEGFA playing a crucial role among various pro-angiogenic factors. The VEGFA gene is upregulated in many known tumors, correlating with tumor staging and progression. Blocking VEGFA may lead to vascular network regression, thereby inhibiting tumor growth [4]. Thus, VEGFA is an important target for anti-angiogenic cancer therapies.
Angiopoietin-2 (ANG2/ANGPT2), encoded by the ANGPT2 gene, is a secreted glycoprotein of the angiopoietin family predominantly expressed in vascular endothelial cells and stored in Weibel-Palade bodies for rapid release. ANGPT2 regulates vascular biology in a context-dependent manner by binding to the Tie2 tyrosine kinase receptor, playing pivotal roles in angiogenesis and vascular remodeling [5]. Its molecular structure includes a coiled-coil domain facilitating oligomerization and a fibrinogen-like domain critical for receptor binding. Functionally, ANGPT2 acts as a partial Tie2 receptor antagonist to Angiopoietin-1 (ANG1). Through competitive inhibition of Tie2 signaling, ANGPT2 disrupts vascular endothelial homeostasis, inducing increased vascular permeability and structural plasticity. In synergy with vascular endothelial growth factor (VEGF), ANGPT2 drives angiogenic sprouting and pathological neovascularization. Conversely, under conditions of low or absent VEGF, it mediates vascular regression [6-7]. ANGPT2 plays a central pathological role in vascular proliferative diseases such as tumor angiogenesis, diabetic retinopathy, and age-related macular degeneration. Endothelial cell activation and inflammatory responses mediated by ANGPT2 also contribute to the pathogenesis of inflammatory conditions including sepsis and rheumatoid arthritis [8]. Therapeutic strategies targeting ANGPT2 include monoclonal antibodies (e.g., Nesvacumab) and peptide-Fc fusion proteins (e.g., Trebananib), often combined with VEGF inhibitors to enhance anti-angiogenic efficacy [9-10]. Current research efforts are focused on optimizing ANGPT2/VEGF dual-target inhibition strategies and developing biomarkers, aiming to improve clinical outcomes in tumors and ocular vascular diseases and validate its translational value as a therapeutic target in vascular and inflammatory diseases [11-12].
B6-hVEGFA/hANGPT2 mice are VEGFA and ANGPT2 double humanized mouse models obtained by mating VEGFA humanized mouse models (Catalog No. C001555) with ANGPT2 humanized mouse models (Catalog No. C001615). B6-hVEGFA/hANGPT2 mice express human VEGFA and ANGPT2 genomic sequences under the control of mouse promoters. This model is capable of reproducing human VEGFA and ANGPT2 and is a valuable tool for studying cancer, vascular diseases and autoimmune disorders. In addition, this model also provides a powerful preclinical research platform for evaluating the efficacy and mechanism of therapeutic drugs targeting VEGFA and ANGPT2.
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