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Apc KO
Product ID:
C001511
Strain:
C57BL/6JCya
Status:
Description:
The adenomatous polyposis coli (APC) gene is a tumor suppressor gene, the protein it encodes plays a key regulatory role in the Wnt/β-catenin signaling pathway [1]. The APC protein can antagonize the Wnt signaling pathway, assisting in regulating cell migration, adhesion, transcriptional activation, and apoptosis. More than 10% of human tumors have mutations in the APC gene, and most colorectal cancers have mutations in the APC gene [2]. Defects in the APC gene lead to the occurrence of familial adenomatous polyposis (FAP), characterized by hundreds to thousands of adenomatous polyps in the rectum. This is an autosomal dominant precancerous disease, which usually develops into malignant tumors [1-2]. Disease-related mutations in the APC gene are highly prevalent in a small region known as the mutation cluster region (MCR), which usually leads to the production of truncated proteins [3-4]. In mice, either Apc gene deletion or multiple intestinal neoplasia (Min) mutations that result in the production of truncated APC proteins cause phenotypes similar to human familial adenomatous polyposis (FAP) and/or colorectal tumors [5-9].
The Apc KO mouse is a research model constructed by using gene editing technology to knock out the sequence in the mouse Apc gene that contains the mutation cluster region (MCR), and this strain is homozygous lethal. Heterozygous Apc KO mice can spontaneously develop intestinal adenomas and exhibit significant colorectal cancer disease phenotypes in various aspects such as survival, growth, food intake, and intestinal lesions. Therefore, Apc KO mice can be used for familial adenomatous polyposis (FAP) and colorectal cancer and other tumors or tumor-related diseases, as well as the study of the regulatory mechanism of the Wnt/β-catenin signaling pathway.
The adenomatous polyposis coli (APC) gene is a tumor suppressor gene, the protein it encodes plays a key regulatory role in the Wnt/β-catenin signaling pathway [1]. The APC protein can antagonize the Wnt signaling pathway, assisting in regulating cell migration, adhesion, transcriptional activation, and apoptosis. More than 10% of human tumors have mutations in the APC gene, and most colorectal cancers have mutations in the APC gene [2]. Defects in the APC gene lead to the occurrence of familial adenomatous polyposis (FAP), characterized by hundreds to thousands of adenomatous polyps in the rectum. This is an autosomal dominant precancerous disease, which usually develops into malignant tumors [1-2]. Disease-related mutations in the APC gene are highly prevalent in a small region known as the mutation cluster region (MCR), which usually leads to the production of truncated proteins [3-4]. In mice, either Apc gene deletion or multiple intestinal neoplasia (Min) mutations that result in the production of truncated APC proteins cause phenotypes similar to human familial adenomatous polyposis (FAP) and/or colorectal tumors [5-9].
The Apc KO mouse is a research model constructed by using gene editing technology to knock out the sequence in the mouse Apc gene that contains the mutation cluster region (MCR), and this strain is homozygous lethal. Heterozygous Apc KO mice can spontaneously develop intestinal adenomas and exhibit significant colorectal cancer disease phenotypes in various aspects such as survival, growth, food intake, and intestinal lesions. Therefore, Apc KO mice can be used for familial adenomatous polyposis (FAP) and colorectal cancer and other tumors or tumor-related diseases, as well as the study of the regulatory mechanism of the Wnt/β-catenin signaling pathway.
Alb-cre+/MYC+
Product ID:
C001339
Strain:
C57BL/6JCya
Status:
Description:
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+/MYC+ 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.
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+/MYC+ 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.
B6-huTREM2
Product ID:
C001883
Strain:
C57BL/6NCya
Status:
Description:
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 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.
B6-huIL18BP
Product ID:
C001869
Strain:
C57BL/6NCya
Status:
Description:
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 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.
B6-huMMP7
Product ID:
C001914
Strain:
C57BL/6NCya
Status:
Description:
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.
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.
B6-huKIT
Product ID:
C001899
Strain:
C57BL/6NCya
Status:
Description:
KIT (also known as c-Kit or CD117) is a type III receptor tyrosine kinase proto-oncogene located on chromosome 4q12, originally identified as the cellular homolog of the feline sarcoma virus v-kit. Upon binding to its ligand stem cell factor (SCF), KIT activates downstream signaling cascades that regulate cellular proliferation, differentiation, migration, and apoptosis [1]. KIT plays essential roles in hematopoiesis, stem cell maintenance, gametogenesis, melanogenesis, and mast cell development and function. KIT is prominently expressed in hematopoietic stem cells, mast cells, melanocytes, germ cells (up to the pachytene stage), and interstitial cells of Cajal in the gastrointestinal tract. Its protein product is readily detectable via immunohistochemistry. CD117 is widely used in diagnostic pathology to label tissues such as bone marrow (hematopoietic progenitors), skin (mast cells and melanocytes), gastrointestinal stroma (Cajal cells), and testis (germ cells). Mutations in KIT are implicated in a spectrum of diseases, including gastrointestinal stromal tumors (GIST), systemic mastocytosis, acute myeloid leukemia, seminoma, and vitiligo. These mutations often contribute to the persistence of cancer stem cells and therapeutic resistance [1-2]. Clinically approved tyrosine kinase inhibitors (TKIs) such as imatinib, sunitinib, regorafenib, ripretinib, and avapritinib selectively target KIT mutations and are used in the treatment of GIST and mast cell disorders. Ongoing research is advancing next-generation inhibitors, combination therapies, antibody-drug conjugates, and ligand-directed delivery strategies to expand the therapeutic scope of KIT-targeted interventions and support precision medicine approaches [3-4].
The B6-huKIT mouse is a humanized model generated by replacing the endogenous murine Kit gene with the human KIT coding sequence via gene editing. This model enables investigation of the molecular pathogenesis of human KIT mutations in relevant disease contexts, preclinical evaluation of TKIs and emerging therapies, and functional studies of KIT in hematopoietic stem cells, melanocytes, and mast cells.
KIT (also known as c-Kit or CD117) is a type III receptor tyrosine kinase proto-oncogene located on chromosome 4q12, originally identified as the cellular homolog of the feline sarcoma virus v-kit. Upon binding to its ligand stem cell factor (SCF), KIT activates downstream signaling cascades that regulate cellular proliferation, differentiation, migration, and apoptosis [1]. KIT plays essential roles in hematopoiesis, stem cell maintenance, gametogenesis, melanogenesis, and mast cell development and function. KIT is prominently expressed in hematopoietic stem cells, mast cells, melanocytes, germ cells (up to the pachytene stage), and interstitial cells of Cajal in the gastrointestinal tract. Its protein product is readily detectable via immunohistochemistry. CD117 is widely used in diagnostic pathology to label tissues such as bone marrow (hematopoietic progenitors), skin (mast cells and melanocytes), gastrointestinal stroma (Cajal cells), and testis (germ cells). Mutations in KIT are implicated in a spectrum of diseases, including gastrointestinal stromal tumors (GIST), systemic mastocytosis, acute myeloid leukemia, seminoma, and vitiligo. These mutations often contribute to the persistence of cancer stem cells and therapeutic resistance [1-2]. Clinically approved tyrosine kinase inhibitors (TKIs) such as imatinib, sunitinib, regorafenib, ripretinib, and avapritinib selectively target KIT mutations and are used in the treatment of GIST and mast cell disorders. Ongoing research is advancing next-generation inhibitors, combination therapies, antibody-drug conjugates, and ligand-directed delivery strategies to expand the therapeutic scope of KIT-targeted interventions and support precision medicine approaches [3-4].
The B6-huKIT mouse is a humanized model generated by replacing the endogenous murine Kit gene with the human KIT coding sequence via gene editing. This model enables investigation of the molecular pathogenesis of human KIT mutations in relevant disease contexts, preclinical evaluation of TKIs and emerging therapies, and functional studies of KIT in hematopoietic stem cells, melanocytes, and mast cells.
B6-huEPCAM
Product ID:
C001930
Strain:
C57BL/6JCya
Status:
Description:
The EPCAM gene encodes a transmembrane glycoprotein, Epithelial Cell Adhesion Molecule (EPCAM), also known as CD326 or Trop-1, which mediates calcium-independent homotypic cell adhesion and participates in fundamental processes including cell adhesion, migration, proliferation, and signal transduction, thereby maintaining epithelial tissue integrity [1]. While normally expressed on the surface of epithelial cells in organs such as the gastrointestinal tract, lungs, and skin, EPCAM is frequently overexpressed in various cancers, including colorectal, breast, and pancreatic carcinomas, but is largely absent or weakly expressed in healthy squamous epithelia [1]. Structurally, EPCAM comprises an extracellular domain (EpEX) mediating intercellular adhesion, a transmembrane domain, and a short intracellular domain (EpICD). Upon proteolytic cleavage by ADAM17 and γ-secretase, EpICD translocates to the nucleus, activating oncogenic pathways such as Wnt/β-catenin, ERK, and FAK-AKT, which promotes epithelial-mesenchymal transition (EMT), tumor progression, and metastasis [2]. Notably, EPCAM serves as a marker for circulating tumor cells (CTCs) and cancer stem cells, and its downregulation during EMT can complicate advanced cancer detection [2-3]. Furthermore, dysregulated EPCAM expression is associated with congenital tufting enteropathy (CTE), a severe intestinal epithelial dysfunction [2]. Given its involvement in tumor metastasis through interaction with HGFR (c-Met), targeting EPCAM with strategies like the neutralizing antibody EpAb2-6 in combination with HGFR inhibitors has shown promising preclinical efficacy [4].
The B6-huEPCAM mouse is a humanized model constructed through gene-editing technology, in which the mouse Epcam extracellular domain is replaced with the human EPCAM extracellular domain. This model can be used for research on tumor mechanisms and tumor immunotherapy, as well as for the development of EPCAM-targeted drugs.
The EPCAM gene encodes a transmembrane glycoprotein, Epithelial Cell Adhesion Molecule (EPCAM), also known as CD326 or Trop-1, which mediates calcium-independent homotypic cell adhesion and participates in fundamental processes including cell adhesion, migration, proliferation, and signal transduction, thereby maintaining epithelial tissue integrity [1]. While normally expressed on the surface of epithelial cells in organs such as the gastrointestinal tract, lungs, and skin, EPCAM is frequently overexpressed in various cancers, including colorectal, breast, and pancreatic carcinomas, but is largely absent or weakly expressed in healthy squamous epithelia [1]. Structurally, EPCAM comprises an extracellular domain (EpEX) mediating intercellular adhesion, a transmembrane domain, and a short intracellular domain (EpICD). Upon proteolytic cleavage by ADAM17 and γ-secretase, EpICD translocates to the nucleus, activating oncogenic pathways such as Wnt/β-catenin, ERK, and FAK-AKT, which promotes epithelial-mesenchymal transition (EMT), tumor progression, and metastasis [2]. Notably, EPCAM serves as a marker for circulating tumor cells (CTCs) and cancer stem cells, and its downregulation during EMT can complicate advanced cancer detection [2-3]. Furthermore, dysregulated EPCAM expression is associated with congenital tufting enteropathy (CTE), a severe intestinal epithelial dysfunction [2]. Given its involvement in tumor metastasis through interaction with HGFR (c-Met), targeting EPCAM with strategies like the neutralizing antibody EpAb2-6 in combination with HGFR inhibitors has shown promising preclinical efficacy [4].
The B6-huEPCAM mouse is a humanized model constructed through gene-editing technology, in which the mouse Epcam extracellular domain is replaced with the human EPCAM extracellular domain. This model can be used for research on tumor mechanisms and tumor immunotherapy, as well as for the development of EPCAM-targeted drugs.
B6-hCD3/hEPCAM
Product ID:
C001694
Strain:
C57BL/6N;6JCya
Status:
Description:
Cluster of Differentiation 3 (CD3) is a protein complex that acts as a co-receptor for T cells and is involved in the activation of cytotoxic T cells (CTLs) and helper T cells (THs). CD3 consists of five polypeptide chains: γ, δ, ε, ζ, and η, all of which are transmembrane proteins. The transmembrane regions of CD3 molecules connect with the transmembrane regions of TCR's two polypeptide chains through salt bridges, forming the TCR-CD3 complex, which is essential for T cell antigen recognition [1-2]. After TCR recognizes an antigen, the activation signal is transduced by CD3 into the T cell. CD3 is highly specific at all developmental stages of T cells, thus it is considered a T cell-specific immunohistochemical marker. Additionally, CD3 is present in almost all T cell lymphomas and leukemias and can be used to distinguish between morphologically similar B cell and bone marrow tumors. Due to its significant role in T cell activation and antigen recognition, CD3 is an important drug target in immunosuppressive therapy for type 1 diabetes and other autoimmune diseases [3].
The EPCAM gene encodes a transmembrane glycoprotein, Epithelial Cell Adhesion Molecule (EPCAM), also known as CD326 or Trop-1, which mediates calcium-independent homotypic cell adhesion and participates in fundamental processes including cell adhesion, migration, proliferation, and signal transduction, thereby maintaining epithelial tissue integrity [4]. While normally expressed on the surface of epithelial cells in organs such as the gastrointestinal tract, lungs, and skin, EPCAM is frequently overexpressed in various cancers, including colorectal, breast, and pancreatic carcinomas, but is largely absent or weakly expressed in healthy squamous epithelia [4]. Structurally, EPCAM comprises an extracellular domain (EpEX) mediating intercellular adhesion, a transmembrane domain, and a short intracellular domain (EpICD). Upon proteolytic cleavage by ADAM17 and γ-secretase, EpICD translocates to the nucleus, activating oncogenic pathways such as Wnt/β-catenin, ERK, and FAK-AKT, which promotes epithelial-mesenchymal transition (EMT), tumor progression, and metastasis [5]. Notably, EPCAM serves as a marker for circulating tumor cells (CTCs) and cancer stem cells, and its downregulation during EMT can complicate advanced cancer detection [5-6]. Furthermore, dysregulated EPCAM expression is associated with congenital tufting enteropathy (CTE), a severe intestinal epithelial dysfunction [5]. Given its involvement in tumor metastasis through interaction with HGFR (c-Met), targeting EPCAM with strategies like the neutralizing antibody EpAb2-6 in combination with HGFR inhibitors has shown promising preclinical efficacy [7].
The B6-hCD3/hEPCAM mouse is obtained by crossbreeding B6-hCD3 mice (Catalog No.: C001325) with B6-hEPCAM mice. It can be used for the development of CD3/EPCAM-targeted drugs, as well as for research in tumor immunotherapy and autoimmune disease-related drugs.
Cluster of Differentiation 3 (CD3) is a protein complex that acts as a co-receptor for T cells and is involved in the activation of cytotoxic T cells (CTLs) and helper T cells (THs). CD3 consists of five polypeptide chains: γ, δ, ε, ζ, and η, all of which are transmembrane proteins. The transmembrane regions of CD3 molecules connect with the transmembrane regions of TCR's two polypeptide chains through salt bridges, forming the TCR-CD3 complex, which is essential for T cell antigen recognition [1-2]. After TCR recognizes an antigen, the activation signal is transduced by CD3 into the T cell. CD3 is highly specific at all developmental stages of T cells, thus it is considered a T cell-specific immunohistochemical marker. Additionally, CD3 is present in almost all T cell lymphomas and leukemias and can be used to distinguish between morphologically similar B cell and bone marrow tumors. Due to its significant role in T cell activation and antigen recognition, CD3 is an important drug target in immunosuppressive therapy for type 1 diabetes and other autoimmune diseases [3].
The EPCAM gene encodes a transmembrane glycoprotein, Epithelial Cell Adhesion Molecule (EPCAM), also known as CD326 or Trop-1, which mediates calcium-independent homotypic cell adhesion and participates in fundamental processes including cell adhesion, migration, proliferation, and signal transduction, thereby maintaining epithelial tissue integrity [4]. While normally expressed on the surface of epithelial cells in organs such as the gastrointestinal tract, lungs, and skin, EPCAM is frequently overexpressed in various cancers, including colorectal, breast, and pancreatic carcinomas, but is largely absent or weakly expressed in healthy squamous epithelia [4]. Structurally, EPCAM comprises an extracellular domain (EpEX) mediating intercellular adhesion, a transmembrane domain, and a short intracellular domain (EpICD). Upon proteolytic cleavage by ADAM17 and γ-secretase, EpICD translocates to the nucleus, activating oncogenic pathways such as Wnt/β-catenin, ERK, and FAK-AKT, which promotes epithelial-mesenchymal transition (EMT), tumor progression, and metastasis [5]. Notably, EPCAM serves as a marker for circulating tumor cells (CTCs) and cancer stem cells, and its downregulation during EMT can complicate advanced cancer detection [5-6]. Furthermore, dysregulated EPCAM expression is associated with congenital tufting enteropathy (CTE), a severe intestinal epithelial dysfunction [5]. Given its involvement in tumor metastasis through interaction with HGFR (c-Met), targeting EPCAM with strategies like the neutralizing antibody EpAb2-6 in combination with HGFR inhibitors has shown promising preclinical efficacy [7].
The B6-hCD3/hEPCAM mouse is obtained by crossbreeding B6-hCD3 mice (Catalog No.: C001325) with B6-hEPCAM mice. It can be used for the development of CD3/EPCAM-targeted drugs, as well as for research in tumor immunotherapy and autoimmune disease-related drugs.
B6-huCD3/huDLL3
Product ID:
C001902
Strain:
C57BL/6NCya
Status:
Description:
Cluster of differentiation 3 (CD3) is a multimeric protein complex that is essential for T cell activation and antigen recognition. It consists of five different polypeptide chains (γ, δ, ε, ζ, and η) that are noncovalently associated with the T cell receptor (TCR). The TCR is responsible for recognizing antigens presented by antigen-presenting cells (APCs), while CD3 transduces the activation signal into the T cell and activates helper T-cells and cytotoxic T-cells [1-2]. The CD3-TCR complex is expressed on the surface of all mature T cells, and its assembly is required for T cell development and function. CD3 plays a crucial role in stabilizing the TCR and facilitating its interaction with antigens. It also recruits signaling molecules to the TCR, which initiates a cascade of events that leads to T cell activation. CD3 is a highly specific T cell marker, and its expression is increased upon T cell activation. This makes it a valuable tool for identifying and characterizing T cells in tissues and blood samples. CD3 staining is also used to diagnose T-cell lymphomas and leukemias. Due to its essential role in T cell activation, CD3 is a promising target for immunosuppressive therapy. Several anti-CD3 monoclonal antibodies have been developed and are being tested in clinical trials for the treatment of autoimmune diseases, such as type 1 diabetes and rheumatoid arthritis [3].
The DLL3 (Delta-like canonical Notch ligand 3) gene encodes a transmembrane protein belonging to the Delta/Serrate/Lag-2 (DSL) family of ligands. Functioning within the highly conserved Notch signaling pathway, DLL3 exhibits a unique, inhibitory role, contrasting with the canonical activating function of other Notch ligands. It is believed to antagonize Notch signaling by preventing ligand-receptor interactions or by promoting receptor degradation, a mechanism critical for establishing proper cell fate decisions during development [4]. This is particularly evident in the formation of somites, where DLL3's function is essential for the rhythmic segmentation of the presomitic mesoderm [5]. While its expression is largely restricted to fetal tissues and progenitor cells in healthy adults, DLL3 is ectopically and highly expressed in a number of neuroendocrine tumors, including small cell lung cancer (SCLC), making it a promising therapeutic target. Pathogenic variants in the DLL3 gene are directly linked to Spondylocostal dysostosis type 1, a congenital disorder of vertebral segmentation [6].
The B6-huCD3/huDLL3 mouse is a dual-gene humanized model obtained by mating B6-huCD3 mice (catalog number: C001325) with B6-huDLL3 mice (catalog number: C001854). This model can be used for studying the pathological mechanisms and treatment methods of tumors and autoimmune diseases, as well as for the development of CD3/DLL3-targeted drugs.
Cluster of differentiation 3 (CD3) is a multimeric protein complex that is essential for T cell activation and antigen recognition. It consists of five different polypeptide chains (γ, δ, ε, ζ, and η) that are noncovalently associated with the T cell receptor (TCR). The TCR is responsible for recognizing antigens presented by antigen-presenting cells (APCs), while CD3 transduces the activation signal into the T cell and activates helper T-cells and cytotoxic T-cells [1-2]. The CD3-TCR complex is expressed on the surface of all mature T cells, and its assembly is required for T cell development and function. CD3 plays a crucial role in stabilizing the TCR and facilitating its interaction with antigens. It also recruits signaling molecules to the TCR, which initiates a cascade of events that leads to T cell activation. CD3 is a highly specific T cell marker, and its expression is increased upon T cell activation. This makes it a valuable tool for identifying and characterizing T cells in tissues and blood samples. CD3 staining is also used to diagnose T-cell lymphomas and leukemias. Due to its essential role in T cell activation, CD3 is a promising target for immunosuppressive therapy. Several anti-CD3 monoclonal antibodies have been developed and are being tested in clinical trials for the treatment of autoimmune diseases, such as type 1 diabetes and rheumatoid arthritis [3].
The DLL3 (Delta-like canonical Notch ligand 3) gene encodes a transmembrane protein belonging to the Delta/Serrate/Lag-2 (DSL) family of ligands. Functioning within the highly conserved Notch signaling pathway, DLL3 exhibits a unique, inhibitory role, contrasting with the canonical activating function of other Notch ligands. It is believed to antagonize Notch signaling by preventing ligand-receptor interactions or by promoting receptor degradation, a mechanism critical for establishing proper cell fate decisions during development [4]. This is particularly evident in the formation of somites, where DLL3's function is essential for the rhythmic segmentation of the presomitic mesoderm [5]. While its expression is largely restricted to fetal tissues and progenitor cells in healthy adults, DLL3 is ectopically and highly expressed in a number of neuroendocrine tumors, including small cell lung cancer (SCLC), making it a promising therapeutic target. Pathogenic variants in the DLL3 gene are directly linked to Spondylocostal dysostosis type 1, a congenital disorder of vertebral segmentation [6].
The B6-huCD3/huDLL3 mouse is a dual-gene humanized model obtained by mating B6-huCD3 mice (catalog number: C001325) with B6-huDLL3 mice (catalog number: C001854). This model can be used for studying the pathological mechanisms and treatment methods of tumors and autoimmune diseases, as well as for the development of CD3/DLL3-targeted drugs.
B6-hCD3/hCD19/hBCMA
Product ID:
C001897
Strain:
C57BL/6NCya
Status:
Description:
Cluster of differentiation 3 (CD3) is a multimeric protein complex that is essential for T cell activation and antigen recognition. It consists of five different polypeptide chains (γ, δ, ε, ζ, and η) that are noncovalently associated with the T cell receptor (TCR). The TCR is responsible for recognizing antigens presented by antigen-presenting cells (APCs), while CD3 transduces the activation signal into the T cell and activates helper T-cells and cytotoxic T-cells [1-2]. The CD3-TCR complex is expressed on the surface of all mature T cells, and its assembly is required for T cell development and function. CD3 plays a crucial role in stabilizing the TCR and facilitating its interaction with antigens. It also recruits signaling molecules to the TCR, which initiates a cascade of events that leads to T cell activation. CD3 is a highly specific T cell marker, and its expression is increased upon T cell activation. This makes it a valuable tool for identifying and characterizing T cells in tissues and blood samples. CD3 staining is also used to diagnose T-cell lymphomas and leukemias. Due to its essential role in T cell activation, CD3 is a promising target for immunosuppressive therapy. Several anti-CD3 monoclonal antibodies have been developed and are being tested in clinical trials for the treatment of autoimmune diseases, such as type 1 diabetes and rheumatoid arthritis [3].
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 crucial for B cell development, activation, and differentiation. CD19, a pan-B-cell marker exclusively expressed in the B cell lineage, remains stable throughout B cell development, from pro-B cells to mature and memory B cells. It acts as a positive regulator of BCR signal transduction by forming 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 [4]. Dysregulation of CD19 is strongly linked to autoimmune diseases such as systemic lupus erythematosus (SLE) and B cell malignancies like acute lymphoblastic leukemia (ALL) and non-Hodgkin lymphoma. Mutations in this gene are associated with common variable immunodeficiency 3 (CVID3), characterized by impaired B cell differentiation and hypogammaglobulinemia. Owing to its B cell-specific expression, CD19 has become a pivotal target for immunotherapy. For example, anti-CD19 CAR-T cell therapy (e.g., Tisagenlecleucel) has shown remarkable efficacy in refractory or relapsed ALL [5]. Recent studies have also explored CD19-targeted bispecific antibodies (e.g., blinatumomab) to enhance tumor cell clearance [6].
The TNFRSF17 gene, also known as BCMA, encodes a protein belonging to the tumor necrosis factor receptor superfamily. This protein is predominantly expressed in mature B lymphocytes, particularly plasma cells, with lower expression in early B cells and non-B cells [7-8]. As a type III transmembrane glycoprotein, TNFRSF17 plays a critical role in B cell survival and differentiation, acting as a key regulator of B cell maturation [8]. Functionally, TNFRSF17 primarily acts as a receptor for the B cell-activating factor (BAFF). Upon BAFF binding, it activates both the classical NF-κB pathway and the non-classical MAPK8/JNK pathway, subsequently regulating downstream gene expression to promote B cell survival, proliferation, and antibody secretion. Furthermore, TNFRSF17 can interact with TNFR-associated factors (TRAFs) 1, 2, and 3, further mediating physiological processes related to cell differentiation and growth [7-8]. Multiple studies have demonstrated that the TNFRSF17 gene and its protein are associated with various B cell-related diseases. Notably, this gene exhibits abnormally high expression in diseases such as multiple myeloma and systemic lupus erythematosus, rendering it a potential therapeutic target for these conditions [9-10].
The B6-hCD3/hCD19/hBCMA mouse is a tri-gene humanized model generated by crossing B6-hCD3 mice (Catalog No.: C001325), B6-hCD19 mice (Catalog No.: C001731), and B6-hBCMA (hTNFRSF17) mice (Catalog No.: C001630). This model can be used for the research of autoimmune diseases such as systemic lupus erythematosus (SLE) and rheumatoid arthritis (RA), as well as B-cell malignancies, and for the development, screening, and preclinical evaluation of related targeted therapeutics.
Cluster of differentiation 3 (CD3) is a multimeric protein complex that is essential for T cell activation and antigen recognition. It consists of five different polypeptide chains (γ, δ, ε, ζ, and η) that are noncovalently associated with the T cell receptor (TCR). The TCR is responsible for recognizing antigens presented by antigen-presenting cells (APCs), while CD3 transduces the activation signal into the T cell and activates helper T-cells and cytotoxic T-cells [1-2]. The CD3-TCR complex is expressed on the surface of all mature T cells, and its assembly is required for T cell development and function. CD3 plays a crucial role in stabilizing the TCR and facilitating its interaction with antigens. It also recruits signaling molecules to the TCR, which initiates a cascade of events that leads to T cell activation. CD3 is a highly specific T cell marker, and its expression is increased upon T cell activation. This makes it a valuable tool for identifying and characterizing T cells in tissues and blood samples. CD3 staining is also used to diagnose T-cell lymphomas and leukemias. Due to its essential role in T cell activation, CD3 is a promising target for immunosuppressive therapy. Several anti-CD3 monoclonal antibodies have been developed and are being tested in clinical trials for the treatment of autoimmune diseases, such as type 1 diabetes and rheumatoid arthritis [3].
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 crucial for B cell development, activation, and differentiation. CD19, a pan-B-cell marker exclusively expressed in the B cell lineage, remains stable throughout B cell development, from pro-B cells to mature and memory B cells. It acts as a positive regulator of BCR signal transduction by forming 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 [4]. Dysregulation of CD19 is strongly linked to autoimmune diseases such as systemic lupus erythematosus (SLE) and B cell malignancies like acute lymphoblastic leukemia (ALL) and non-Hodgkin lymphoma. Mutations in this gene are associated with common variable immunodeficiency 3 (CVID3), characterized by impaired B cell differentiation and hypogammaglobulinemia. Owing to its B cell-specific expression, CD19 has become a pivotal target for immunotherapy. For example, anti-CD19 CAR-T cell therapy (e.g., Tisagenlecleucel) has shown remarkable efficacy in refractory or relapsed ALL [5]. Recent studies have also explored CD19-targeted bispecific antibodies (e.g., blinatumomab) to enhance tumor cell clearance [6].
The TNFRSF17 gene, also known as BCMA, encodes a protein belonging to the tumor necrosis factor receptor superfamily. This protein is predominantly expressed in mature B lymphocytes, particularly plasma cells, with lower expression in early B cells and non-B cells [7-8]. As a type III transmembrane glycoprotein, TNFRSF17 plays a critical role in B cell survival and differentiation, acting as a key regulator of B cell maturation [8]. Functionally, TNFRSF17 primarily acts as a receptor for the B cell-activating factor (BAFF). Upon BAFF binding, it activates both the classical NF-κB pathway and the non-classical MAPK8/JNK pathway, subsequently regulating downstream gene expression to promote B cell survival, proliferation, and antibody secretion. Furthermore, TNFRSF17 can interact with TNFR-associated factors (TRAFs) 1, 2, and 3, further mediating physiological processes related to cell differentiation and growth [7-8]. Multiple studies have demonstrated that the TNFRSF17 gene and its protein are associated with various B cell-related diseases. Notably, this gene exhibits abnormally high expression in diseases such as multiple myeloma and systemic lupus erythematosus, rendering it a potential therapeutic target for these conditions [9-10].
The B6-hCD3/hCD19/hBCMA mouse is a tri-gene humanized model generated by crossing B6-hCD3 mice (Catalog No.: C001325), B6-hCD19 mice (Catalog No.: C001731), and B6-hBCMA (hTNFRSF17) mice (Catalog No.: C001630). This model can be used for the research of autoimmune diseases such as systemic lupus erythematosus (SLE) and rheumatoid arthritis (RA), as well as B-cell malignancies, and for the development, screening, and preclinical evaluation of related targeted therapeutics.
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