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Abca4/Rdh8-DKO
製品ID :
C001968
系統:
C57BL/6JCya
状況:
説明:
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
製品ID :
C002024
系統:
C57BL/6JCya
状況:
説明:
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-Rpe65 R44X
製品ID :
C001360
系統:
C57BL/6JCya
状況:
説明:
Leber congenital amaurosis (LCA) is a group of inherited retinal diseases accompanied by severe visual impairment. The main symptoms of this disease are vision loss at birth or within a few months after birth, nystagmus, and weakened or absent light reflexes of rods and cones. Approximately 16% of LCA cases are caused by mutations in the RPE65 gene. In visual cells, vitamin A aldehyde (retinal) combines with opsin to form visual pigments. After vitamin A aldehyde absorbs light, it is isomerized to all - trans - retinal, which causes a conformational change in rhodopsin and initiates nerve impulses to the brain, thus forming vision. During the decomposition and resynthesis of rhodopsin, a portion of vitamin A aldehyde is consumed and is mainly replenished by vitamin A (retinol) in the blood.The retinoid isomerase encoded by the RPE65 gene is present in the retinal pigment epithelial cells (RPE) of the retina. The RPE65 protein plays a crucial role in the visual process. It participates in the conversion of vitamin A to vitamin A aldehyde and the regeneration of retinal photoreceptor pigments, so it is a key molecule for the conversion and transmission of light signals in the retina[1].
Mutations in the RPE65 gene can lead to further degeneration of the neural retina and RPE cells, resulting in irreversible blindness. Multiple allelic mutations of RPE65 have been found to damage optic nerve cells and cause type II Leber congenital amaurosis (LCA2) and early - onset severe retinal atrophy (EOSRD), ultimately leading to complete blindness[1-3].
This model is a mouse Rpe65 gene point - mutation model. Using gene - editing technology, a p.R44*(CGA to TGA) point mutation was introduced into the mouse Rpe65 gene, which led to abnormal expression of the mouse Rpe65 protein. This caused phenotypes such as damage to RPE cell function, apoptosis of photoreceptor cells, disordered arrangement of rod outer segment membrane discs, and extinction of rod waveforms, resulting in severe retinal degeneration.
This model is a mouse Rpe65 gene point - mutation model. Using gene - editing technology, a p.R44*(CGA to TGA) point mutation was introduced into the mouse Rpe65 gene, which led to abnormal expression of the mouse Rpe65 protein. This caused phenotypes such as damage to RPE cell function, apoptosis of photoreceptor cells, disordered arrangement of rod outer segment membrane discs, and extinction of rod waveforms, resulting in severe retinal degeneration.
Leber congenital amaurosis (LCA) is a group of inherited retinal diseases accompanied by severe visual impairment. The main symptoms of this disease are vision loss at birth or within a few months after birth, nystagmus, and weakened or absent light reflexes of rods and cones. Approximately 16% of LCA cases are caused by mutations in the RPE65 gene. In visual cells, vitamin A aldehyde (retinal) combines with opsin to form visual pigments. After vitamin A aldehyde absorbs light, it is isomerized to all - trans - retinal, which causes a conformational change in rhodopsin and initiates nerve impulses to the brain, thus forming vision. During the decomposition and resynthesis of rhodopsin, a portion of vitamin A aldehyde is consumed and is mainly replenished by vitamin A (retinol) in the blood.The retinoid isomerase encoded by the RPE65 gene is present in the retinal pigment epithelial cells (RPE) of the retina. The RPE65 protein plays a crucial role in the visual process. It participates in the conversion of vitamin A to vitamin A aldehyde and the regeneration of retinal photoreceptor pigments, so it is a key molecule for the conversion and transmission of light signals in the retina[1].
Mutations in the RPE65 gene can lead to further degeneration of the neural retina and RPE cells, resulting in irreversible blindness. Multiple allelic mutations of RPE65 have been found to damage optic nerve cells and cause type II Leber congenital amaurosis (LCA2) and early - onset severe retinal atrophy (EOSRD), ultimately leading to complete blindness[1-3].
This model is a mouse Rpe65 gene point - mutation model. Using gene - editing technology, a p.R44*(CGA to TGA) point mutation was introduced into the mouse Rpe65 gene, which led to abnormal expression of the mouse Rpe65 protein. This caused phenotypes such as damage to RPE cell function, apoptosis of photoreceptor cells, disordered arrangement of rod outer segment membrane discs, and extinction of rod waveforms, resulting in severe retinal degeneration.
This model is a mouse Rpe65 gene point - mutation model. Using gene - editing technology, a p.R44*(CGA to TGA) point mutation was introduced into the mouse Rpe65 gene, which led to abnormal expression of the mouse Rpe65 protein. This caused phenotypes such as damage to RPE cell function, apoptosis of photoreceptor cells, disordered arrangement of rod outer segment membrane discs, and extinction of rod waveforms, resulting in severe retinal degeneration.
B6-hTGFBI
製品ID :
C001546
系統:
C57BL/6JCya
状況:
説明:
Corneal dystrophy (CD) refers to a group of primary hereditary progressive corneal diseases. The typical clinical presentation involves gradual loss of corneal transparency in both eyes, often leading to recurrent corneal erosions and visual impairment. The TGFBI gene (also known as BIGH3) encodes an extracellular matrix protein called keratoepithelin (KE protein), which plays a role in cell growth, differentiation, wound healing, cell adhesion, migration, apoptosis, proliferation, and tumorigenesis [1]. Mutations in the TGFBI gene are associated with various types of corneal dystrophy. Abnormal accumulation of mutated TGFBI deposits in the corneal epithelium and stroma progressively affects corneal transparency, leading to visual impairment.
Currently, therapeutic pipelines targeting the TGFBI gene have entered preclinical research stages. For instance, SiSaf Ltd. is developing a siRNA drug pipeline called SIS-201-CD, which aims to treat the disease by specifically inhibiting abnormal TGFBI expression. Most gene therapies target human genes, but considering the genetic differences between animals and humans, humanizing mouse genes can accelerate the development of TGFBI-targeted gene therapies for clinical use. This strain is a mouse Tgfbi gene humanized model and can be used for research on CD. The homozygous B6-hTGFBI mice are viable and fertile. In addition, based on the independently developed TurboKnockout fusion BAC recombination technology, Cyagen can also generate hot mutation models based on this strain and provide customized services for specific mutations to meet the experimental needs in pharmacology and other fields related to CD.
Corneal dystrophy (CD) refers to a group of primary hereditary progressive corneal diseases. The typical clinical presentation involves gradual loss of corneal transparency in both eyes, often leading to recurrent corneal erosions and visual impairment. The TGFBI gene (also known as BIGH3) encodes an extracellular matrix protein called keratoepithelin (KE protein), which plays a role in cell growth, differentiation, wound healing, cell adhesion, migration, apoptosis, proliferation, and tumorigenesis [1]. Mutations in the TGFBI gene are associated with various types of corneal dystrophy. Abnormal accumulation of mutated TGFBI deposits in the corneal epithelium and stroma progressively affects corneal transparency, leading to visual impairment.
Currently, therapeutic pipelines targeting the TGFBI gene have entered preclinical research stages. For instance, SiSaf Ltd. is developing a siRNA drug pipeline called SIS-201-CD, which aims to treat the disease by specifically inhibiting abnormal TGFBI expression. Most gene therapies target human genes, but considering the genetic differences between animals and humans, humanizing mouse genes can accelerate the development of TGFBI-targeted gene therapies for clinical use. This strain is a mouse Tgfbi gene humanized model and can be used for research on CD. The homozygous B6-hTGFBI mice are viable and fertile. In addition, based on the independently developed TurboKnockout fusion BAC recombination technology, Cyagen can also generate hot mutation models based on this strain and provide customized services for specific mutations to meet the experimental needs in pharmacology and other fields related to CD.
B6-hVEGFA/hANGPT2
製品ID :
C001691
系統:
C57BL/6JCya
状況:
説明:
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.
B6-hCFB
製品ID :
C001710
系統:
C57BL/6JCya
状況:
説明:
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 B6-hCFB mouse is a humanized model constructed by replacing the sequence of the mouse Cfb gene in situ with the corresponding sequence from the human CFB gene. The homozygous B6-hCFB mice are viable and fertile and can be used for studies on age-related macular degeneration (AMD), atypical hemolytic uremic syndrome (aHUS), and systemic lupus erythematosus (SLE), and pathogenesis of immune-related diseases, as well as for CFB-targeted drug development.
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 B6-hCFB mouse is a humanized model constructed by replacing the sequence of the mouse Cfb gene in situ with the corresponding sequence from the human CFB gene. The homozygous B6-hCFB mice are viable and fertile and can be used for studies on age-related macular degeneration (AMD), atypical hemolytic uremic syndrome (aHUS), and systemic lupus erythematosus (SLE), and pathogenesis of immune-related diseases, as well as for CFB-targeted drug development.
B6-huPRPF31
製品ID :
C001863
系統:
C57BL/6JCya
状況:
説明:
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-hNRL
製品ID :
C001799
系統:
C57BL/6JCya
状況:
説明:
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-huCFB/huC5
製品ID :
C001918
系統:
C57BL/6JCya
状況:
説明:
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-huCFB/hMASP2
製品ID :
C001919
系統:
C57BL/6Cya
状況:
説明:
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.
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