The MYC oncogene family comprises regulatory genes and proto-oncogenes that encode transcription factors, involved in various cellular processes such as the cell cycle, apoptosis, DNA repair, and metabolism. Members include c-Myc (MYC), l-Myc (MYCL), and n-Myc (MYCN). c-Myc (MYC) is a basic helix-loop-helix leucine zipper (bHLHZip) transcription factor, which forms heterodimers with Max protein to bind DNA and regulate the expression of approximately 15% of genes, thereby participating in key cellular processes such as cell proliferation, apoptosis, DNA repair, and metabolism. In many cancers, c-Myc is overexpressed, leading to uncontrolled cell proliferation and tumor growth, such as in Burkitt's lymphoma where c-Myc gene rearrangement is common. Dysregulation of the MYC oncogene plays a crucial role in tumorigenesis, predominantly through transcriptional dysregulation resulting in overexpression of c-Myc protein. Alb-Cre+/hMYC-IRES-EGFP+ mice are generated by crossing H11-CAG-LSL-hMYC-IRES-EGFP mice (Catalog Number: C001338), which conditionally express the human c-Myc oncogene, with Alb-Cre mice that express Cre recombinase specifically in hepatocytes under the control of the Alb promoter. The Cre-mediated recombination results in the deletion of the transcriptional stop sequence (Loxp-Stop-Loxp, LSL) in H11-CAG-LSL-hMYC-IRES-EGFP mice, leading to overexpression of the MYC oncogene in the liver and subsequent carcinogenesis. This model, therefore, spontaneously develops liver cancer with an early onset.

TNF-like ligand 1A (TL1A), also known as TNF superfamily member 15 (TNFSF15), is a member of the tumor necrosis factor (TNF) family encoded by the TNFSF15 gene in humans. TL1A acts as a ligand for death receptor 3 (DR3) and decoy receptor 3 (DcR3), providing a stimulatory signal for downstream pathways. It regulates the proliferation, activation, and apoptosis of effector cells, as well as cytokine and chemokine production. TL1A is expressed in various immune cells, including monocytes, macrophages, dendritic cells, and T cells, as well as in non-immune cells such as synovial fibroblasts and endothelial cells. It plays a crucial role in modulating immune responses by promoting the differentiation and survival of T cells, particularly Th17 cells involved in inflammatory processes ^[1]. TL1A enhances IL-2 responses in anti-CD3/CD28-stimulated T cells and synergizes with IL-12 and IL-18 to augment IFN-γ release in human T and NK cells, biasing T cell differentiation toward a Th1 phenotype ^[2]. Dysregulation of TL1A expression is implicated in autoimmune diseases, including inflammatory bowel disease (IBD), rheumatoid arthritis (RA), primary biliary cholangitis (PBC), systemic lupus erythematosus (SLE), and ankylosing spondylitis (AS) ^[1]. TL1A has emerged as a promising therapeutic target, with ongoing research focused on developing monoclonal antibodies and other biologics to neutralize TL1A and reduce inflammation in autoimmune disorders. Clinical trial results suggest that TL1A inhibition can be used in the treatment of various autoimmune diseases, particularly IBD ^[3-5]. The Cryopyrin protein, encoded by the NOD-like receptor family pyrin domain-containing 3 (NLRP3) gene, is a core component of the inflammasome in the innate immune system. As a member of the NOD-like receptor (NLR) family, NLRP3 is predominantly expressed in leukocytes and chondrocytes. It participates in the host defense against damage and infection by recognizing pathogen-associated molecular patterns (PAMPs) or damage-associated molecular patterns (DAMPs) to activate immune responses ^[6]. In its inactive monomeric state, NLRP3 senses intracellular damage signals, such as abnormal protein aggregates and lipid accumulation. Upon activation, NLRP3 oligomerizes, adopting an active conformation and assembling into inflammasome complexes, subsequently activating Caspase-1 to drive the maturation and secretion of pro-inflammatory cytokines, including IL-1β and IL-18 ^[6-7]. Activated NLRP3 not only induces the release of inflammatory cytokines but also triggers lytic cell pyroptosis. The intracellular components released during pyroptosis can further amplify inflammatory signals, forming a positive feedback loop of autoinflammation. Moreover, IL-1β can exacerbate the inflammatory cascade by stimulating the production of inflammatory markers such as IL-6 and high-sensitivity C-reactive protein (hsCRP) ^[8-9]. Given NLRP3's upstream position relative to IL-1β/IL-18 and other inflammatory factors, targeting its activity can effectively block the self-reinforcing mechanism of chronic inflammation, providing a significant therapeutic strategy for inflammation-related diseases ^[10]. The potential therapeutic areas include Alzheimer’s disease, Parkinson’s disease (via neuroinflammation modulation), inflammatory bowel disease, metabolic dysfunction-associated steatohepatitis (MASH), gout, and obesity-related metabolic inflammation ^[11-12]. B6-hTL1A/hNLRP3 mice are TL1A and NLRP3 double humanized mouse models obtained by mating TL1A humanized mouse models (Catalog No. C001603) with NLRP3 humanized mouse models (Catalog No. C001616). B6-hTL1A/hNLRP3 mice express human TL1A and NLRP3 genomic sequences under the control of mouse promoters. This model is capable of reproducing human TL1A and NLRP3 and is a valuable tool for studying autoimmune diseases and inflammation-related diseases. In addition, this model also provides a powerful preclinical research platform for evaluating the efficacy and mechanism of therapeutic drugs targeting TL1A and NLRP3.

CD7 is mainly expressed in T cells and natural killer (NK) cells. It is expressed throughout thymocyte development from early stages to mature T cells, and also in some hematopoietic progenitor cells, but its expression level is low in most normal non-T-cell and non-NK-cell tissues. Abnormal expression or signaling dysregulation of CD7 is closely associated with various diseases. As an important target for immunotherapy, CD7 has become a key molecule for targeting T-cell malignancies due to its high expression in T-cell acute lymphoblastic leukemia (T-ALL), T-cell lymphoma, and other T-cell malignant tumors ^[1]. The CD19 gene encodes a member of the immunoglobulin gene superfamily. As a key co-receptor in the B-cell receptor (BCR) signaling pathway, it is essential for B-cell development, activation, and differentiation. CD19 is a pan-B-cell marker, expressed only in the B-cell lineage, and is stably expressed throughout B-cell development (from pre-B cells to mature B cells and memory B cells). CD19 is a positive regulatory factor for BCR signal transduction. This protein forms a B-cell-specific signaling complex with CD21 (complement receptor 2), CD81 (tetraspanin), and CD225 (Leu13), which lowers the threshold for antigen-induced B-cell activation ^[2]. Dysregulation of CD19 is closely related to autoimmune diseases such as systemic lupus erythematosus (SLE) and B-cell malignancies including acute lymphoblastic leukemia (ALL) and non-Hodgkin lymphoma. Mutations in this gene are associated with common variable immunodeficiency 3 (CVID3), manifesting as impaired B-cell differentiation and hypogammaglobulinemia. Due to its B-cell-specific expression, CD19 has become an important target for immunotherapy. For example, anti-CD19 CAR-T cell therapy (e.g., tisagenlecleucel) has shown significant efficacy in refractory or relapsed acute lymphoblastic leukemia ^[3]. Recent studies have also explored bispecific antibodies targeting CD19 (e.g., blinatumomab) to enhance the clearance of tumor cells ^[4]. The huCD7/huCD19 mouse is a dual-gene humanized model obtained by crossing the huCD7 mouse (Catalog No.: C002067) with the huCD19 mouse (Catalog No.: C001731). This model can be used for studying the immune mechanisms of CD7/CD19-related malignancies, as well as for screening, efficacy evaluation, and safety assessment of drugs targeting CD7/CD19.

The CD7 gene encodes a transmembrane glycoprotein in the immunoglobulin superfamily (IgSF). As an important co-receptor on the T cell surface, it plays a key regulatory role in T cell activation, proliferation, and signal transduction. CD7 is mainly expressed in T cells and natural killer (NK) cells, from early thymocyte development to the mature T cell stage, and also in some hematopoietic progenitor cells; however, its expression level is low in most normal non-T cell and NK cell tissues ^[1]. Abnormal expression or dysregulated signaling of CD7 is closely related to multiple diseases. As an important target for immunotherapy, CD7 has become a key molecule for targeting T-cell malignancies due to its high expression in T-cell acute lymphoblastic leukemia (T-ALL), T-cell lymphoma, and other T-cell malignant tumors ^[1]. In addition, CD7 is also associated with systemic sclerosis (SSc) and graft-versus-host disease (GvHD) ^[2-3]. Cluster of differentiation 20 (CD20), also known as MS4A1, is a functional receptor molecule on the surface of B lymphocytes, closely related to B cell activation, signal transduction, and growth regulation. CD20 is expressed at the late stage of B-cell lymphopoiesis and disappears after differentiation into plasma cells. Therefore, CD20 is expressed from pre-B cells to mature B cells, but not in plasma cells ^[4]. The huCD7/huCD20 mouse is a dual-gene humanized model obtained by crossing the huCD7 mouse (Catalog No.: C002067) with the huCD20 mouse (Catalog No.: C001625). This model can be used for studying the immune mechanisms of CD7/CD20-related malignant tumors, as well as for screening, efficacy evaluation, and safety assessment of CD7/CD20-targeted drugs.

The APP gene encodes the Amyloid Precursor Protein, a type I transmembrane glycoprotein that is ubiquitously expressed but reaches its highest levels in the central nervous system, particularly in the cerebral cortex and hippocampus. Following translation, the APP protein is proteolytically processed via two primary pathways: the non-amyloidogenic pathway, which prevents Aβ formation, and the amyloidogenic pathway, where sequential cleavage by β-secretase (BACE1) and γ-secretase releases amyloid-beta (Aβ) peptides ^[1]. While its precise physiological role remains an area of active research, APP is known to function in synaptic formation and repair, anterograde neuronal transport, and cell-to-cell adhesion ^[2]. Pathological mutations or duplications of the APP gene are primary drivers of Alzheimer’s Disease (AD) and Cerebral Amyloid Angiopathy (CAA), characterized by the extracellular accumulation of Aβ plaques and vascular deposits that lead to neurodegeneration and cognitive decline ^[3]. Pathogenic point mutations in the APP gene typically disrupt these proteolytic pathways, favoring the production or aggregation of neurotoxic peptides. The p.K670N/p.M671L (Swedish) double mutation (AAGATG to AATCTG) occurs at the β-secretase cleavage site, significantly increasing the production of total Aβ by enhancing BACE1 affinity ^[4]. In contrast, the p.E693G (Arctic) mutation (GAA to GGA) is located within the Aβ sequence itself; it does not increase peptide quantity but dramatically accelerates the formation of protofibrils ^[5]. Mutations near the γ-secretase cleavage site, such as p.I716F (Iberian) (ATC to TTC) and p.V717I (London) (GTC to ATC), shift the cleavage precision to increase the ratio of the highly aggregate-prone Aβ42 isoform over Aβ40, thereby facilitating early-onset amyloid plaque deposition ^[6]. The huAPP-Aβ-NL-G-F-I mouse is an Alzheimer's disease research model generated by replacing the sequence from upstream of exon 16 to downstream of exon 17 in the murine App gene with the corresponding sequence from the human APP gene. Simultaneously, the p.K670N/p.M671L (AAGATG to AATCTG), p.I716F (ATC to TTC), p.E693G (GAA to GGA) and p.V717I (GTC to ATC) point mutations were introduced into exon 16 and exon 17 of human APP gene. This model is suitable for studying neurodegenerative diseases such as Alzheimer's disease (AD), as well as for the research, development, and efficacy evaluation of AD therapeutic strategies targeting APP. Cyagen Biosciences offers a variety of APP gene-edited mouse models: hAPP-NL-F mice (Catalog No.: C002124): Generated using a different APP humanization strategy and lacking the p.E693G and p.V717I mutations. hAPP-NL-G-F mice (Catalog No.: C002125): Generated using a different APP humanization strategy and lacking the p.V717I mutation.

The APP gene encodes the Amyloid Precursor Protein, a type I transmembrane glycoprotein that is ubiquitously expressed but reaches its highest levels in the central nervous system, particularly in the cerebral cortex and hippocampus. Following translation, APP is proteolytically processed via two primary pathways: the non-amyloidogenic pathway, which precludes Aβ formation, and the amyloidogenic pathway, in which sequential cleavage by β-secretase (BACE1) and γ-secretase releases amyloid-β (Aβ) peptides ^[1]. Although the precise physiological functions of APP remain under active investigation, it is known to participate in synaptic formation and repair, anterograde neuronal transport, and cell-cell adhesion ^[2]. Pathological mutations or duplications of the APP gene are primary drivers of Alzheimer’s Disease (AD) and Cerebral Amyloid Angiopathy (CAA), characterized by the extracellular accumulation of Aβ plaques and vascular deposits that lead to neurodegeneration and cognitive decline ^[3]. Pathogenic point mutations in the APP gene typically disrupt these proteolytic pathways, favoring the production or aggregation of neurotoxic peptides. The p.K670N/p.M671L (Swedish) double mutation (AAGATG to AATCTG) occurs at the β-secretase cleavage site, significantly increasing total Aβ production by enhancing BACE1 binding affinity ^[4]. In contrast, the p.I716F (Iberian) mutation (ATC to TTC), located near the γ-secretase cleavage site, alters cleavage specificity to increase the ratio of the highly aggregation-prone Aβ42 isoform relative to Aβ40, thereby facilitating early-onset amyloid plaque deposition ^[5]. The hAPP-NL-F mouse is an Alzheimer's disease research model generated by replacing the region from downstream of the mouse App signal peptide-coding sequence through part of intron 1 with the "Mutant Human APP CDS-3'UTR of Human APP-WPRE-BGH pA" cassette, while retaining the mouse App signal peptide-coding sequence. The following mutations were introduced into the mutant human APP CDS: p.K670N/p.M671L (AAGATG→AATCTG) and p.I716F (ATC→TTC). This model can be used for research on Alzheimer's disease and other neurodegenerative diseases, as well as for the development and efficacy evaluation of AD therapeutic strategies targeting APP. Cyagen Biosciences offers a variety of APP gene-edited mouse models: hAPP-NL-G-F mice (Catalog No.: C002125): Generated using a construction strategy similar to that of the present model but additionally carrying the p.E693G (Arctic) mutation. huAPP-Aβ-NL-G-F-I mice (Catalog No.: C002033): Generated using a different APP humanization strategy and additionally carrying the p.E693G and p.V717I mutations.

The APP gene encodes the Amyloid Precursor Protein, a type I transmembrane glycoprotein that is ubiquitously expressed but reaches its highest levels in the central nervous system, particularly in the cerebral cortex and hippocampus. Following translation, the APP protein is proteolytically processed via two primary pathways: the non-amyloidogenic pathway, which prevents Aβ formation, and the amyloidogenic pathway, where sequential cleavage by β-secretase (BACE1) and γ-secretase releases amyloid-beta (Aβ) peptides ^[1]. While its precise physiological role remains an area of active research, APP is known to function in synaptic formation and repair, anterograde neuronal transport, and cell-to-cell adhesion ^[2]. Pathological mutations or duplications of the APP gene are primary drivers of Alzheimer’s Disease (AD) and Cerebral Amyloid Angiopathy (CAA), characterized by the extracellular accumulation of Aβ plaques and vascular deposits that lead to neurodegeneration and cognitive decline ^[3]. Pathogenic point mutations in the APP gene typically disrupt these proteolytic pathways, favoring the production or aggregation of neurotoxic peptides. The p.K670N/p.M671L (Swedish) double mutation (AAGATG to AATCTG) occurs at the β-secretase cleavage site, significantly increasing the production of total Aβ by enhancing BACE1 affinity ^[4]. In contrast, the p.E693G (Arctic) mutation (GAA to GGA) is located within the Aβ sequence itself; it does not increase peptide quantity but dramatically accelerates the formation of protofibrils ^[5]. The p.I716F (Iberian) mutation (ATC to TTC), located near the γ-secretase cleavage site, shifts the cleavage precision to increase the ratio of the highly aggregate-prone Aβ42 isoform over Aβ40, thereby facilitating early-onset amyloid plaque deposition ^[6]. The hAPP-NL-G-F mouse is an Alzheimer's disease research model generated by replacing the region from downstream of the mouse App signal peptide-coding sequence through part of intron 1 with the "Mutant Human APP CDS-3'UTR of Human APP-WPRE-BGH pA" cassette, while retaining the mouse App signal peptide-coding sequence. In addition, the following point mutations were introduced into the mutant human APP CDS: p.K670N/p.M671L (AAGATG→AATCTG), p.E693G (GAA to GGA) and p.I716F (ATC→TTC). This model can be used for research on Alzheimer's disease and other neurodegenerative diseases, as well as for the development and efficacy evaluation of AD therapeutic strategies targeting APP. Cyagen Biosciences offers a variety of APP gene-edited mouse models: hAPP-NL-F mice (Catalog No.: C002124): Generated using a construction strategy similar to that of the present model but without the p.E693G (Arctic) mutation. huAPP-Aβ-NL-G-F-I mice (Catalog No.: C002033): Generated using a different APP humanization strategy and additionally carrying the p.V717I mutation.

The APP gene encodes the Amyloid Precursor Protein, a type I transmembrane glycoprotein that is ubiquitously expressed but reaches its highest levels in the central nervous system, particularly in the cerebral cortex and hippocampus. Following translation, APP is proteolytically processed via two primary pathways: the non-amyloidogenic pathway, which precludes Aβ formation, and the amyloidogenic pathway, in which sequential cleavage by β-secretase (BACE1) and γ-secretase releases amyloid-β (Aβ) peptides ^[1]. Although the precise physiological functions of APP remain under active investigation, it is known to participate in synaptic formation and repair, anterograde neuronal transport, and cell-cell adhesion ^[2]. Pathological mutations or duplications of the APP gene are primary drivers of Alzheimer’s Disease (AD) and Cerebral Amyloid Angiopathy (CAA), characterized by the extracellular accumulation of Aβ plaques and vascular deposits that lead to neurodegeneration and cognitive decline ^[3]. The hAPP mouse is a humanized model generated using gene-editing technology. The region downstream of the mouse App signal peptide-coding sequence to a portion of intron 1 was replaced with the “Human APP CDS-3'UTR of Human APP-WPRE-BGH pA” cassette, while the mouse App signal peptide-coding sequence was retained. This model is suitable for studying neurodegenerative diseases such as Alzheimer's disease (AD), as well as for the research, development, and efficacy evaluation of AD therapeutic strategies targeting APP. Cyagen also offers huAPP-Aβ mice (Catalog No.: C002031), providing an alternative model for APP/Aβ-related research. The two models feature distinct humanization designs: the hAPP mouse incorporates a human APP CDS expression cassette, whereas the huAPP-Aβ mouse carries a genomic replacement in which the corresponding mouse App genomic region was replaced with its human APP genomic counterpart. The appropriate model can be selected based on the humanized region and construct design, according to the specific drug target and research objectives.