Duchenne Muscular Dystrophy (DMD) is a severe, progressive, and disabling X-linked recessive genetic disorder characterized primarily by muscle atrophy. This disease leads to motor impairments, eventually requiring assisted ventilation, and often results in premature death. The primary cause of DMD is mutations in the DMD gene, which encodes the dystrophin protein. These mutations lead to a reduction or absence of dystrophin in muscle tissue, resulting in muscle atrophy and related complications ^[1]. The lack of dystrophin leads to the breakdown of the dystrophin-associated protein complex (DAPC) within the muscle membrane, disrupting the interaction between actin and the extracellular matrix, making the muscles more susceptible to damage. This susceptibility results in the gradual loss of muscle tissue and function, potentially leading to cardiomyopathy ^[2]. Researchers have identified thousands of different DMD gene mutations in patients with DMD. Deletion mutations account for approximately 60%–70%, while duplication mutations account for 5%–15%. These mutations are primarily concentrated in hotspot regions of the DMD gene, specifically between exons 45-55 (47%) and exons 3-9 (7%) ^[1]. Currently, gene therapy approaches for Duchenne Muscular Dystrophy (DMD) primarily include exon skipping and AAV supplementation, as well as emerging gene editing techniques like CRISPR. The exon skipping strategy involves using antisense oligonucleotide (ASO) drugs to bind to specific sequences of pre-mRNA, skipping the mutated exon and restoring the open reading frame (ORF) integrity, thus producing a truncated but partially functional dystrophin protein. Several ASO drugs targeting the DMD gene have been approved, such as Eteplirsen (targeting exon 51), Golodirsen (targeting exon 53), and Casimersen (targeting exon 45) developed by Sarepta, and Viltolarsen (targeting exon 53) developed by Nippon Shinyaku. Since most ASO and CRISPR-based gene editing therapies target the human DMD gene, humanizing mouse genes helps accelerate clinical applications for DMD therapies, considering the genetic differences between animals and humans. The B6-hDMD (E49-53) mouse is a humanized model of exons 49-53 of the Dmd gene, used for researching Duchenne Muscular Dystrophy. Homozygotes are viable and fertile. In addition, based on the independently developed TurboKnockout fusion BAC recombination technology, Cyagen provides other humanized models such as [hE49-53, del E50], [hE44-45], [hE44-45, del E44], [hE44-45, c.6438+2 T to A], and [hE8-30], covering most popular research areas and offering customized services based on different mutation needs.

The protein encoded by the triggering receptor expressed on myeloid cells 2 (TREM2) gene can form a receptor signaling complex with TYRO protein tyrosine kinase-binding protein. This protein is mainly expressed in macrophages and dendritic cells, among which microglia in the central nervous system are the core cell types for its expression. The TREM2 protein binds to the adapter protein Dap-12, recruits various signaling molecules such as kinases and phospholipase C-γ, and assembles to form a receptor signaling complex, thereby activating myeloid cells such as microglia and dendritic cells. Functionally, TREM2 participates in innate and adaptive immune responses, regulates the chronic inflammatory process by inducing the production of inflammatory cytokines, and it has been confirmed to be associated with colonic wound healing ^[1]. Genetic studies have shown that mutations in the TREM2 gene are one of the pathogenic factors for polycystic lipomembranous osteodysplasia with sclerosing leukoencephalopathy (PLOSL), and variations in this gene are closely related to an increased risk of neurodegenerative diseases such as Alzheimer's disease (AD) ^[2]. Tumor-associated macrophages (TAMs) are involved in the tumor's resistance to the immune system, and TREM2 plays a role in TAMs and myeloid-derived suppressor cells (MDSCs), with its expression level being positively correlated with tumor progression ^[3]. The B6-huTREM2 mouse is a humanized model constructed by gene-editing technology, in which the sequence from the upstream of exon 1 to the downstream of exon 5 of the mouse Trem2 gene is replaced with the corresponding sequence of the human TREM2 gene. This model can be used for the research of the pathological mechanisms of Alzheimer's disease (AD), polycystic lipomembranous osteodysplasia with sclerosing leukoencephalopathy (PLOSL), and some cancers, as well as the development of relevant treatment methods, and the screening, development, and pre-clinical evaluation of TREM2-targeted drugs.

The IL18BP (Interleukin 18 Binding Protein) gene encodes a secreted, high-affinity, naturally occurring antagonist of the proinflammatory cytokine Interleukin-18 (IL-18), functioning by binding IL-18 to prevent it from interacting with its receptor, thereby inhibiting IL-18-induced immune responses, such as interferon-gamma (IFN-γ) production ^[1]. The gene's protein, IL-18BP, is constitutively expressed and secreted primarily by mononuclear cells (such as monocytes/macrophages and T-cells) and is widely expressed at the RNA level in numerous tissues, including the spleen, lung, placenta, and small intestine ^[2]. Its expression can be enhanced by IFN-γ in a negative feedback loop to regulate inflammation ^[3]. Dysregulation or an imbalance in the ratio of IL-18 to IL-18BP is associated with a range of inflammatory and autoimmune conditions, including Crohn's disease, rheumatoid arthritis, systemic lupus erythematosus (SLE), systemic juvenile idiopathic arthritis (SJIA), fulminant viral hepatitis, and adult-onset Still's disease. The B6-huIL18BP mouse is a humanized model constructed through gene-editing technology, in which the sequences from the ATG start codon to the TAA stop codon of the endogenous mouse Il18bp gene are replaced with the sequences from the ATG start codon to the TAA stop codon of the human IL18BP gene. This model can be used for research on tumor mechanisms and tumor immunotherapy, inflammatory and autoimmune conditions, as well as for the development of IL18BP-targeted 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.

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]. Common mutations include P301L, P301S, and Intron10+3 G>A ^[8]. The B6-huTFRC/htau*P301L mouse is a humanized disease model obtained by mating B6-huTFRC mice (catalog number: C001860) with B6-htau*P301L mice (catalog number: C001835). This model can be used for the research of Alzheimer's disease (AD), frontotemporal dementia (FTD), neurodegenerative diseases, and tumorigenesis and development, as well as the development of TFRC/MAPT-targeted 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]. Common mutations include P301L, P301S, and Intron10+3 G>A ^[8]. The B6-huTFRC/htau*P301S mouse is a humanized disease model obtained by mating B6-huTFRC mice (catalog number: C001860) with B6-htau*P301S mice (catalog number: C001836). This model can be used for the research of Alzheimer's disease (AD), frontotemporal dementia (FTD), neurodegenerative diseases, and tumorigenesis and development, as well as the development of TFRC/MAPT-targeted drugs.

The amyloid beta precursor protein (APP) gene encodes a transmembrane precursor protein that acts as a cell surface receptor. This protein is cleaved by secretase to form a polypeptide, part of which forms the protein basis for beta-amyloid plaques (Aβ) found in the brains of Alzheimer’s disease (AD) patients. Mutations in the APP gene are associated with autosomal dominant Alzheimer’s disease and cerebral amyloid angiopathy (CAA) ^[1]. The presenilin 1 (PS1) gene encodes presenilin, which regulates the processing of APP through its action on γ-secretase, a protease responsible for cleaving the APP precursor. Presenilin is also involved in the cleavage of Notch receptors. Mutations in the PS1 or APP genes are found in patients with hereditary Alzheimer’s disease (AD). These disease-associated mutations typically result in an increase in the longer form of β-amyloid protein, the main component of amyloid deposits found in the brains of AD patients ^[2]. 5xFAD mouse rapidly reproduces the main features of AD amyloid pathology and exhibits behavioral defects at different stages, presenting AD-like and progressive cerebral amyloid angiopathy (CAA)-like phenotypes. It is a useful model for studying Aβ42-induced neurodegeneration and amyloid plaque formation within neurons ^[3-4]. 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 ^[5]. 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 ^[6]. 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 ^[5]. 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 ^[7]. 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 ^[8-9]. 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-huTFRC/5xFAD mice are an Alzheimer's disease research model obtained by mating B6-huTFRC mice (catalog number: C001860) with 5xFAD mice (catalog number: C001541). This model can be used for the research of neurodegenerative diseases such as Alzheimer's disease (AD) and the development and efficacy evaluation of AD treatment strategies targeting TFRC.

MMP7 encodes matrix metalloproteinase-7 (MMP-7), also known as matrilysin, a member of the matrix metalloproteinase family that plays a crucial role in the degradation and remodeling of extracellular matrix (ECM) components ^[1]. MMP7 is primarily expressed in epithelial tissues of the gastrointestinal tract, lungs, and reproductive system. Cytokines, growth factors, hypoxia, and inflammatory signals regulate its expression. MMP7 is secreted as a zymogen and activated by other proteases or autolytic cleavage. Activated MMP7 can degrade ECM components such as collagen, proteoglycans, elastin, and fibronectin, and can also activate antimicrobial peptides (e.g., defensins) and process cytokines ^[2]. Functionally, MMP7 involves various physiological and pathological processes, including ECM remodeling, immune regulation, wound healing, and tumor progression. It is notably significant in tumor invasion and metastasis, where it promotes cancer cell migration by degrading matrix barriers and accelerates tumor growth by regulating angiogenesis and immune evasion ^[2-3]. MMP7 is associated with several diseases, including cancers (e.g., colorectal, gastric, pancreatic, and lung cancers, with high expression often correlated with poor prognosis), inflammatory diseases (e.g., inflammatory bowel disease, chronic obstructive pulmonary disease, and asthma), fibrotic diseases (e.g., idiopathic pulmonary fibrosis), and cardiovascular diseases (e.g., atherosclerosis and aneurysms) ^[3-5]. Hence, MMP7 is an important therapeutic target for various diseases. However, clinical trials targeting MMP7 face challenges in efficacy and safety. Broad-spectrum MMP inhibitors (e.g., Marimastat and Batimastat) have limited efficacy due to low specificity and adverse effects like musculoskeletal pain. Recent research focuses on selective MMP7-targeted inhibitory therapies, including small molecule inhibitors, monoclonal antibodies, peptide inhibitors, small interfering RNA (siRNA), and antisense oligonucleotides (ASO) ^[5-8]. MMP7 plays dual roles in maintaining physiological homeostasis and mediating pathological processes (particularly in cancer and fibrosis), making it a promising yet challenging therapeutic target. The B6-huMMP7 mouse is a humanized model constructed by gene-editing technology. The sequences from upstream of exon 1 to downstream of exon 6 of the mouse Mmp7 gene were replaced with the sequences from upstream of exon 1 to downstream of exon 6 of the human MMP7. This model can be used for the research of various cancers, inflammatory diseases, fibrotic diseases, and cardiovascular diseases, as well as for the development of MMP7-targeted drugs.

The OSM gene (Oncostatin M) encodes a secreted cytokine, Oncostatin M, which is a pleiotropic protein belonging to the leukemia inhibitory factor/oncostatin-M (LIF/OSM) family. This protein is expressed in various immune cells, including activated T lymphocytes, macrophages, and neutrophils, as well as in other tissues like endothelial cells, osteoblasts, and smooth muscle cells ^[1]. OSM plays diverse functions, acting as a growth regulator that can inhibit the proliferation of certain tumor cell lines, stimulate proliferation of others (e.g., AIDS-KS cells), and regulate the production of other cytokines like IL-6, G-CSF, and GM-CSF. Its activities are mediated through two receptor complexes: Type I (gp130 and LIFRβ) and Type II (gp130 and OSMRβ), primarily activating the JAK/STAT, MAPK, JNK, and PI3K/AKT signaling pathways ^[2]. OSM is implicated in a wide array of diseases, contributing to inflammatory conditions such as arthritis (rheumatoid and osteoarthritis), inflammatory bowel disease, lung and skin diseases (e.g., psoriasis, asthma), cardiovascular diseases (e.g., atherosclerosis), and liver diseases (e.g., fibrosis) ^[3]. It also exhibits a complex role in various cancers, sometimes inhibiting tumor growth in early stages or in specific cell lines, while promoting tumorigenesis, epithelial-mesenchymal transition (EMT), invasion, and metastasis in more advanced cancers like breast, cervical, ovarian, pancreatic, and lung cancers. Deficiency in OSM has also been linked to severe bone marrow failure syndromes ^[4]. BALB/c-huOSM mice are humanized models constructed by gene-editing technology, in which the sequences from the ATG start codon to the TAG stop codon of the endogenous mouse Osm gene were replaced with the sequences from the ATG start codon to the TAG stop codon of the human OSM gene. This model can be used to study the pathogenesis of inflammatory diseases (such as rheumatoid arthritis, osteoarthritis, and inflammatory bowel disease), lung and skin diseases (such as asthma and psoriasis), cardiovascular diseases (such as atherosclerosis), liver diseases (such as fibrosis), and bone marrow failure syndrome, as well as the development of OSM-targeted drugs.

Retinitis pigmentosa (RP) is a hereditary retinal disease with a global prevalence of approximately 1:5000-1:3000. RP is highly clinically and genetically heterogeneous, with mutations in the rhodopsin (RHO) gene causing approximately 25% of dominant RP ^[1]. The rhodopsin encoded by the RHO gene is closely associated with visual light transduction and GPCR downstream signals. Rhodopsin is essential for the transmission of light signals in the process of vision formation. Most RHO mutations lead to high levels of rhodopsin expression in photoreceptor cells, causing many mutant proteins to be abnormally located and aggregated in cells. This results in the apoptosis of photoreceptor cells, which cannot perform normal light signal transduction functions. Additionally, mutations in the RHO gene are associated with congenital stationary night blindness (CSNB) ^[2-6]. Mutations in the RHO gene can lead to rhodopsin-mediated autosomal dominant retinitis pigmentosa (RHO-adRP). In 25% of autosomal dominant inherited RP (adRP) cases, there are over 150 different RHO gene mutations. Notably, the P23H mutation is one of the most prevalent, accounting for 10% of adRP cases ^[2]. Previous studies have shown that mice carrying the heterozygous human RHO P23H mutation exhibit retinopathy and progressive retinal degeneration similar to the patient's disease process, which could be used for visual signaling and retinitis pigmentosa (RP) studies ^[3]. Current gene therapy targeting the RHO gene to treat retinitis pigmentosa includes ASO, CRISPR, and others. Applying fully humanized animal models will promote the further development of RHO-related potential therapies in clinical trials ^[7-11]. B6-hRHO (Promoter) /hRHO*P23H (Promoter) mouse is an F1 humanized model generated by crossing homozygous B6-hRHO (Promoter) mice (Catalog No.: C001646) with homozygous B6-hRHO*P23H (Promoter) mice (Catalog No.: C001727). This model carries two human RHO gene alleles, both with humanized promoter regions. One allele is the wild-type human RHO (without mutation), while the other is the human RHO carrying a pathogenic point mutation (P23H) (hRHO*P23H). The abnormal proteins encoded by the human genes are expressed in mice, resulting in abnormal retinal morphology, functional impairments, and visual defects in this model. Additionally, leveraging the technological innovation of independently developed TurboKnockout-fused BAC recombination, Cyagen Biosciences can provide customized services for different point mutations based on B6-hRHO humanized mice to meet the experimental needs of researchers, such as pharmacodynamic studies related to retinitis pigmentosa (RP).