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Animal Models
C57BL/6NCya-Cd38em1(hCD38)/Cya
The CD38 gene, located on human chromosome 4, encodes a multifunctional type II transmembrane glycoprotein (also known as ADP-ribosyl cyclase/cyclic ADP-ribose hydrolase 1) that acts both as an ectoenzyme and a receptor. It is widely expressed on immune cells, including plasma cells, activated T and B lymphocytes, natural killer cells, monocytes, and dendritic cells, with variable expression depending on cell activation and differentiation states; it is also found in various tissues and can exist in soluble forms [1]. The encoded protein primarily functions as a potent NADase, catalyzing the hydrolysis of NAD⁺ to ADP-ribose (ADPR) and nicotinamide while also synthesizing cyclic ADP-ribose (cADPR), a second messenger involved in intracellular calcium mobilization, cell adhesion (via CD31 interaction), signal transduction, and metabolic regulation [2-4]. High CD38 expression labels malignant plasma cells in multiple myeloma and serves as a prognostic marker in chronic lymphocytic leukemia (CLL), while its role in NAD⁺ depletion links it to inflammation, aging, immune modulation, and metabolic diseases [5-6]. In drug development, CD38 has emerged as a major target, with approved monoclonal antibodies like daratumumab (and isatuximab) demonstrating efficacy in multiple myeloma through mechanisms such as antibody-dependent cellular cytotoxicity (ADCC), complement-dependent cytotoxicity (CDC), and direct apoptosis induction, with ongoing studies exploring broader applications in hematologic malignancies and autoimmune conditions [7].
The hCD38 mice were a humanized mouse model generated via gene editing. The mouse Cd38 endogenous splice acceptor (SA) of intron 1 was replaced with the human CD38 SA of intron 1-Human CD38 exon 2~8 CDS-WPRE-BGH pA cassette. This model is primarily indicated for mechanistic studies and therapeutic development in hematologic malignancies such as multiple myeloma (MM) and chronic lymphocytic leukemia (CLL), as well as for the development of CD38-targeted agents. Furthermore, given the pivotal role of CD38 in NAD⁺ metabolism, this model is also suitable for evaluating the efficacy of CD38-targeted therapies in ameliorating age-related metabolic decline, neurodegenerative diseases, and enhancing NAD⁺ levels.
C57BL/6JCya-Vegfatm1(hVEGFA)/Cya
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.
The huVEGFA mice were generated by replacing the mouse Vegfa gene sequence with the human VEGFA gene sequence, including the non-coding 3’ UTR region. This model expresses the human VEGFA protein. huVEGFA mice can be used for mechanistic studies and efficacy evaluations of ophthalmic diseases such as Age-Related Macular Degeneration (AMD), Diabetic Retinopathy (DR), and corneal neovascularization, as well as for tumor development and cancer drug research.
C57BL/6NCya-Gt(ROSA)26Sorem1(CAG-LSL-hLPA)Tg(Alb-Cre)Pcsk9tm1(hPCSK9)/Cya
Lipoprotein A (LPA) is a type of particle similar to low-density lipoprotein (LDL) that is considered one of the risk factors for cardiovascular disease (CVD), such as atherosclerosis, coronary heart disease, stroke, etc [1]. LP(a) is similar in size and lipid content to LDL (low-density lipoprotein) and also contains the lipoprotein ApoB-100. However, unlike LDL, LP(a) additionally contains a variable-length lipoprotein called Apo(a), which covalently binds to ApoB-100 through a single disulfide bond. LP(a) plays an important role in systemic lipid transport, guiding inflammatory cells into blood vessel walls and leading to smooth muscle cell proliferation. Furthermore, it is involved in wound healing and tissue repair, interacting with the components of blood vessel walls and the extracellular matrix [2]. However, LP(a) can also cause arterial narrowing by adhering to the arterial wall, accelerating the formation of blood clots, and thereby triggering a series of pathological changes related to coronary heart disease, cardiovascular disease, atherosclerosis, thrombus formation, and stroke [3].
The plasma concentration of LP(a) is closely related to genetic factors and is primarily regulated by the LPA gene. Therefore, the LPA gene is an important potential target for cardiovascular disease treatment. The LPA gene encodes a serine protease that inhibits the activity of tissue-type plasminogen activator I. Fragments of this protein, generated through protein hydrolysis, can adhere to atherosclerotic lesions in arteries, promoting blood clot formation. The LPA gene is expressed in both humans and non-human primates but is not expressed in mice. Constructing mouse models expressing the human LPA gene is of significant importance for developing lipid-lowering drugs, which can drive the development of novel therapies for cardiovascular diseases. Currently, various novel therapies targeting the transcription rate of the LPA gene are under development, including small interfering RNA (siRNA) and antisense oligonucleotides (ASO) [4].
Proprotein convertase subtilisin/kexin 9 (PCSK9) is a serine protease primarily produced in the liver but expressed in other tissues, including the intestine, heart, and neurons. The N-terminal domain of the PCSK9 protein is responsible for protein localization and stability, while the C-terminal domain is responsible for protein enzymatic activity [5]. The Low-density lipoprotein receptor (LDLR) is a receptor that is responsible for clearing low-density lipoprotein cholesterol (LDL-C) from the blood. PCSK9 cleaves the intracellular domain of LDLR on the cell surface, causing it to detach from the cell membrane and be transported to the lysosome for degradation, promoting LDLR degradation, and increasing plasma LDL-C. Overexpression or gain-of-function mutations of the PCSK9 gene can lead to LDL-C accumulation by reducing LDLR levels. This can cause hypercholesterolemia, which increases the risk of cardiovascular diseases, such as atherosclerosis and coronary heart disease, and neurodegenerative diseases, such as Alzheimer's disease [6]. PCSK9 has emerged as a key target for the development of lipid-lowering drugs. Several PCSK9-targeted antibodies or small nucleic acid drugs have been approved for marketing worldwide, including evolocumab from Amgen, alirocumab from Sanofi and Regeneron, and inclisiran from Novartis. These drugs primarily work by inhibiting PCSK9 activity or preventing PCSK9 protein from binding to LDLR, lowering LDL-C levels in the blood to treat hypercholesterolemia [7-8]. In addition, PCSK9 can promote tumor growth and development by regulating cell proliferation, migration, and invasion. It can also regulate the expression of inflammatory factors that contribute to inflammation. Therefore, targeting the expression of PCSK9 has been investigated in tumor immunotherapy and autoimmune disease therapy [9-10].
The B6-hLPA (CKI)/Alb-cre/hPCSK9 mouse model is generated by crossing B6-hLPA (CKI) mice (Catalog No.: C001521, a mouse strain with conditional expression of the human LPA gene), Alb-Cre mice (liver-specific Cre-expressing mice), and B6-hPCSK9 mice (Catalog No.: C001617). This model harbors two cardiovascular disease risk factors, namely Lp (a) (lipoprotein (a)) and PCSK9, making it suitable for research on hyperlipidemia, stroke, coronary heart disease, and other atherosclerotic cardiovascular diseases (ASCVD).
C57BL/6Cya-Pcsk9tm1(hPCSK9)Apoeem1/Cya
Proprotein convertase subtilisin/kexin 9 (PCSK9) is a serine protease primarily produced in the liver but expressed in other tissues, including the intestine, heart, and neurons. The N-terminal domain of the PCSK9 protein is responsible for protein localization and stability, while the C-terminal domain is responsible for protein enzymatic activity [1]. The Low-density lipoprotein receptor (LDLR) is a receptor that is responsible for clearing low-density lipoprotein cholesterol (LDL-C) from the blood. PCSK9 cleaves the intracellular domain of LDLR on the cell surface, causing it to detach from the cell membrane and be transported to the lysosome for degradation, promoting LDLR degradation, and increasing plasma LDL-C. Overexpression or gain-of-function mutations of the PCSK9 gene can lead to LDL-C accumulation by reducing LDLR levels. This can cause hypercholesterolemia, which increases the risk of cardiovascular diseases, such as atherosclerosis and coronary heart disease, and neurodegenerative diseases, such as Alzheimer's disease [2]. PCSK9 has become an important target for the development of lipid-lowering drugs. Several PCSK9-targeted antibodies or small nucleic acid drugs have been approved for marketing worldwide, including evolocumab from Amgen, alirocumab from Sanofi and Regeneron, and inclisiran from Novartis. These drugs primarily work by inhibiting PCSK9 activity or preventing PCSK9 protein from binding to LDLR, lowering LDL-C levels in the blood to treat hypercholesterolemia [3-4]. In addition, PCSK9 can promote tumor growth and development by regulating cell proliferation, migration, and invasion. It can also regulate the expression of inflammatory factors that contribute to inflammation. Therefore, targeting the expression of PCSK9 has been investigated in tumor immunotherapy and autoimmune disease therapy [5-6].
Apolipoprotein E (ApoE) is a lipid particle-associated polymorphic carrier protein encoded by the APOE gene. It is a core component of plasma lipoproteins, participating in the production, transport, and clearance of lipoproteins. ApoE is associated with chylomicrons, chylomicron remnants, high-density lipoprotein (HDL), very low-density lipoprotein (VLDL), and intermediate-density lipoprotein (IDL), especially showing preferential binding to HDL [7]. ApoE is the most important lipid transport protein in the body, having a profound impact on lipid metabolism. The interaction of ApoE with the low-density lipoprotein receptor (LDLR) is essential for the normal processing (catabolism) of triglyceride-rich lipoproteins [8]. In peripheral tissues, ApoE is primarily produced by the liver and macrophages and mediates cholesterol metabolism. In the central nervous system, ApoE is produced mainly by astrocytes and is the major cholesterol carrier in the brain. ApoE is essential for transporting cholesterol from astrocytes to neurons [7-10]. In addition, ApoE forms a complex with activated C1q, becoming a checkpoint inhibitor target of the classical complement pathway [11]. Polymorphisms of the APOE are associated with Alzheimer's disease and lipid accumulation, hyperlipidemia, atherosclerosis, high cholesterolemia, etc., and are related to the risk of various cardiovascular diseases.
The B6-hPCSK9/Apoe KO mice are obtained by crossing B6-hPCSK9 mice (Catalog No.: I001179) with B6J-Apoe KO mice (Catalog No.: C001507). B6J-Apoe KO mice exhibit elevated cholesterol levels and spontaneous atherosclerosis phenotypes due to the disruption of ApoE protein synthesis, further exacerbated under a high-fat diet (HFD). On the other hand, B6-hPCSK9 mice have the mouse Pcsk9 gene sequence replaced with the human PCSK9 gene sequence through gene editing technology, expressing the human PCSK9 protein. They can be used for the development of PCSK9-targeted drugs in hyperlipidemia, stroke, coronary heart disease, and other atherosclerotic cardiovascular diseases (ASCVD). The B6-hPCSK9/Apoe KO mice, while expressing the human PCSK9 protein, exhibit significantly elevated cholesterol levels and spontaneous atherosclerosis characteristics. These mice provide an ideal platform for the PCSK9-targeted drug development in hyperlipidemia and cardiovascular diseases, demonstrating good clinical and pathological relevance.
C57BL/6NCya-Cd3tm2(hCD3)Igs2em1(B2M/HLA-A2.1/H2-D1)/Cya
Cluster of Differentiation 3 (CD3) is a protein complex that functions as a co-receptor on T cells, playing a critical role in the activation of cytotoxic T lymphocytes (CTLs) and helper T cells (THs). CD3 comprises five transmembrane polypeptide chains—γ, δ, ε, ζ, and η—each contributing to the structural integrity and signaling capacity of the complex. The transmembrane domains of CD3 form salt bridges with the transmembrane regions of the T cell receptor (TCR) α and β chains, assembling into the TCR-CD3 complex that mediates antigen recognition by T cells [1-2]. Upon antigen engagement by the TCR, activation signals are transduced intracellularly via CD3. CD3 is expressed with high specificity throughout all stages of T cell development and is therefore widely utilized as an immunohistochemical marker for T cell identification. Moreover, CD3 is present in nearly all T cell lymphomas and leukemias, enabling differential diagnosis from morphologically similar B cell and myeloid malignancies. Given its pivotal role in T cell activation and antigen recognition, CD3 has emerged as a key therapeutic target in immunosuppressive strategies for type 1 diabetes and other autoimmune disorders [3].
The B2M gene encodes β2-microglobulin, a serum protein that associates with the heavy chain of major histocompatibility complex (MHC) class I molecules and is essential for their surface expression on virtually all nucleated cells. Human leukocyte antigens (HLAs), also referred to as MHC molecules, are cell-surface proteins responsible for antigen presentation. The HLA system comprises class I, class II, and class III molecules. HLA class I molecules—including HLA-A, HLA-B, and HLA-C—primarily present antigens to CD8⁺ T cells and are central to immune surveillance. Through HLA class I–mediated antigen presentation, the immune system can detect aberrant peptides and initiate targeted cytotoxic responses for immune clearance. HLA-A2.1 is a subtype of HLA class I and represents one of the most prevalent HLA alleles worldwide.
The B6-hCD3/H11-hB2M&HLA-A2.1 mouse model is generated by crossing B6-hCD3 mice (catalog no. C001325) with H11-hB2M&HLA-A2.1 mice (catalog no. I001138). These mice co-express human CD3, human β2-microglobulin, and HLA-A0201 proteins in vivo. This model enables mechanistic investigation of T cell activation, antigen recognition, and antigen presentation, and serves as a versatile platform for evaluating immunosuppressive therapies in autoimmune diseases, studying human viral infections, and developing and testing novel viral vaccines.
C57BL/6Cya-Pdcd1em1(hPDCD1)Cd274em1(hCD274)/Cya
Programmed cell death protein 1 (PDCD1/PD-1) is a member of the B7-CD28 costimulatory receptor family. It is an inhibitory receptor expressed on activated T cells and plays a role in regulating the function of effector T cells, including CD8+ T cells, and promoting the differentiation of CD4+ T cells into regulatory T cells. PD-1 is expressed in a variety of tumors and plays an important role in antitumor immunity. In addition, PD-1 is involved in the defense against autoimmune diseases and has inhibitory effects on antitumor and antimicrobial immunity [1].
Programmed cell death 1 ligand 1 (PD-L1), also known as cluster of differentiation 274 (CD274) or B7 homolog 1 (B7H1), is an immune inhibitory receptor ligand. PD-L1 is a type I transmembrane protein with immunoglobulin V-like (IgV) and C-like (IgC) structural domains and is expressed by hematopoietic and non-hematopoietic cells, including T cells, B cells, and various types of tumor cells [2]. PD-L1 can bind to the PD-1 on the surface of CD8+ T cells, inhibiting the activity of CD8+ T cells. This interaction can prevent the immune system from damaging normal tissues, but it can also be used by tumor cells to escape immune surveillance. Monoclonal antibodies that competitively bind to PD-L1 can relieve the immune function inhibition mediated by the binding of PD-1 and PD-L1. This can reactivate CD8+ T cells, triggering the human body's anti-tumor immune response [3]. Therefore, developing of antibody drugs targeting PD-1 and PD-L1 is a hot area in tumor immunotherapy [3-5].
B6-hPD-1/hPDL1 mice are PD-1 and CD274 double humanized mouse models obtained by mating PD-1 humanized mouse models with CD274 humanized mouse models. They express human PD-1 and CD274 genomic sequences under the control of mouse promoters. This model is a valuable tool for studying cancer immunotherapy. In addition, this model also provides a powerful preclinical research platform for evaluating the efficacy and mechanism of therapeutic drugs targeting PD-1 and PD-L1.
C57BL/6NCya-Pdcd1em1(hPDCD1)Ctla4em1(hCTLA4)/Cya
PD-1 and CTLA-4 are checkpoint receptors that critically modulate T cell immunity. The genes PDCD1 and CTLA4 encode PD-1 and CTLA-4 respectively, with CTLA4 expression largely restricted to T cells, while PDCD1 is evident in activated T cells, B cells, and myeloid populations [1]. These transmembrane proteins function as key negative regulators of T cell activation [2]. CTLA-4 primarily operates in lymphoid tissues during early immune responses to restrain T cell proliferation, whereas PD-1 predominantly acts in peripheral tissues during the effector phase to dampen T cell activity and limit immunopathology, particularly in chronically stimulated or ‘exhausted’ T cells [2-3]. Aberrant regulation of PD-1 and CTLA-4 is implicated in the pathogenesis of cancers, including melanoma, non-small cell lung cancer, and renal cell carcinoma, as well as chronic viral infections such as hepatitis B and C [1][4]. Clinically, monoclonal antibodies targeting CTLA-4 (e.g., ipilimumab) and PD-1 (e.g., nivolumab, pembrolizumab) are established immunotherapeutic agents that enhance anti-tumor responses. By blocking these negative signaling pathways, these monoclonal antibodies restore the anti-tumor activity of T cells, significantly enhancing anti-tumor responses [1-2]. These drug applications have not only improved the treatment outcomes for various cancers but also offer new strategies for the treatment of chronic viral infections.
B6-hPD-1/hCTLA4 mouse is a dual humanized model of PD1 and CTLA4 constructed by humanizing the mouse Pdcd1 gene based on the CTLA4 humanized mouse model (Catalog No. C001413), due to the fact that the mouse Pdcd1 gene and Ctla4 gene are on the same chromosome. These mice express human CTLA4 and PDCD1 genomic sequences under the control of mouse promoters. This model is capable of reproducing the human PD-1/CTLA4 signaling pathway and is a valuable tool for studying cancers and chronic viral infections. Furthermore, this model provides a powerful preclinical research platform for evaluating the efficacy and mechanism of therapeutic drugs targeting the PD-1/CTLA4 signaling pathway.
C57BL/6JCya-Tg(hSERPINA1*E366K)/Cya
The SERPINA1 gene encodes alpha-1 antitrypsin (AAT), a serine protease inhibitor primarily synthesized and secreted by hepatocytes in the liver, with additional expression in immune cells such as macrophages. AAT's main function is to inhibit neutrophil-derived proteases (e.g., elastase) to protect lung tissue from enzymatic degradation. This glycoprotein is crucial for maintaining lung tissue elasticity and regulating inflammatory responses. Mutations in the Serpina1 gene, particularly the Z variant (such as the most common mutation p.E366K), can cause alpha-1 antitrypsin deficiency (AATD), which in turn leads to emphysema and chronic obstructive pulmonary disease (COPD). The pathological mechanism of these diseases stems from dysregulated protease activity. Additionally, the intracellular accumulation of misfolded AAT in hepatocytes may also induce cirrhosis or hepatocellular carcinoma [1-3]. Individuals carrying the ZZ genotype face the highest risk of developing pulmonary and hepatic disease manifestations: in the liver, protein aggregation causes cellular damage; in the lungs, tissue destruction triggers disease [4]. This highlights AAT's systemic role in protease regulation and disease pathology.
The TG-hSERPINA1*E366K mouse is generated by integrating the Human SERPINA1 Genomic DNA (the region from ~5kb upstream of exon 1 to ~3kb downstream of exon 5) into the mouse genome via transgenesis (TG) technology. A p.E366K (GAG to AAG) point mutation is introduced into exon 5 of this integrated human SERPINA1 sequence. This model can be used to study diseases such as alpha-1 antitrypsin deficiency (AATD), emphysema, chronic obstructive pulmonary disease (COPD), cirrhosis, and hepatocellular carcinoma, as well as to develop relevant therapeutic strategies.
C57BL/6NCya-lgf1rem2(hIGF1R)Tfrctm2(hTFRC)/Cya
hIGF1R/huTFRC mouse model is a humanized model obtained by breeding hIGF1R mice (Catalog No.: C001623) with huTFRC mice (Catalog No.: C001860). This model can be utilized in research for thyroid eye disease (TED), growth retardation, diabetes, and oncological diseases, supporting the development of TFRC/IGF1R-targeted drugs.
C57BL/6NCya-Il31raem1(hIL31RA)/Cya
The IL31RA gene encodes the interleukin-31 receptor subunit alpha, a type I cytokine receptor that serves as a critical mediator in neuroimmune communication. The protein typically functions as a heterodimer by associating with the oncostatin M receptor (OSMRβ) to form the functional IL-31 receptor complex, which triggers intracellular signaling through the JAK/STAT (primarily STAT3), PI3K/AKT, and MAPK pathways [1]. While the gene is expressed at low levels across various tissues, including the testis, thymus, and bone marrow, it is highly localized and functionally significant in CD14+ monocytes, macrophages, keratinocytes, and a specific subset of dorsal root ganglia (DRG) neurons. In these tissues, IL31RA plays a pivotal role in mediating pruritus (itching) and regulating skin immunity and inflammation [2]. Genetically, dysregulation of the IL31RA pathway is heavily implicated in the pathogenesis of inflammatory and pruritic diseases such as atopic dermatitis, prurigo nodularis, allergic asthma, and certain cutaneous T-cell lymphomas, making it a major therapeutic target for monoclonal antibodies like nemolizumab [3].
The B6-hIL31RA mouse is a humanized model constructed through gene-editing technology, in which the sequences from aa.19 to partial intron 4 of mouse Il31ra were deleted, and the human IL31RA extracellular domain-mouse Il31ra transmembrane-cytoplasmic domain-3’UTR of mouse Il31ra WPRE-BGH pA cassette was inserted downstream of mouse Il31ra signal peptide. This model can be used for research on inflammatory and pruritic diseases such as atopic dermatitis, prurigo nodularis, allergic asthma, and certain cutaneous T-cell lymphomas, as well as for screening, development, and preclinical evaluation of IL31RA-targeted therapeutics.
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