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B6-hSCN9A
Product ID:
I001216
Strain:
C57BL/6NCya
Status:
Description:
The SCN9A gene encodes the Nav1.7 sodium channel protein, which is primarily expressed in the sensory and sympathetic nerves of the peripheral nervous system and is highly expressed in the dorsal root ganglia. Nav1.7 sodium channels play a crucial role in transmitting positively charged sodium ions within cells, which are essential for generating and transmitting electrical signals. When a person experiences pain, this protein releases sodium ion currents that amplify and stimulate nerve cells, sending electrical signals to the brain, thereby causing the sensation of pain. The SCN9A gene guides the entry of sodium ions into cells and facilitates communication between neurons. Mutations in the SCN9A gene can alter the function of sodium channels in the brain, disrupting neuronal communication and leading to various pain, olfactory, and neurological disorders such as erythromelalgia, paroxysmal extreme pain disorder, Dravet syndrome, small fiber neuropathy, and congenital insensitivity to pain. The abnormal protein function and symptoms resulting from gene mutations are directly related to the severity of the mutations, and different mutation types may lead to completely different conditions.
SCN9A is an excellent target for analgesic drug development. Downregulation of SCN9A expression can alleviate acute pain as well as certain types of inflammatory and neuropathic pain [1]. OliPass Corporation, a South Korean biotechnology company, has developed an antisense peptide nucleic acid (PNA) analgesic targeting SCN9A (OLP-1002), which has entered Phase 2a clinical trials. Antisense PNA is an artificially synthesized DNA/RNA mimic that inhibits RNA/DNA transcription and translation by complementary pairing with RNA/DNA sequences. The drug has shown strong analgesic effects and prolonged therapeutic duration in Australian patients with moderate to severe chronic osteoarthritis pain. It is estimated that due to its potent efficacy, excellent safety profile, and broad therapeutic scope, OLP-1002 could generate over $50 billion in market potential annually [2-4].
The B6-hSCN9A mouse is a mouse Scn9a humanized model, generated by replacing the mouse Scn9a gene (including the 5' UTR and 3' UTR) with the corresponding human SCN9A gene sequence using gene editing technology. Internal research revealed that during the generation of B6-hSCN9A mice, the murine Scn9a gene was inserted unexpectedly, and its precise genomic insertion site remains undetermined*. This strain is suitable for studying the pathogenic mechanisms of neurological diseases such as erythromelalgia, Dravet syndrome, small fiber neuropathy, and congenital insensitivity to pain, as well as for screening analgesic drug candidates. In addition, based on the independently developed TurboKnockout fusion BAC recombination technology, Cyagen can also provide customized services.
* Special notes on the genotype of B6-hSCN9A mice:
B6-hSCN9A het: 1 copy of hSCN9A + 2 copies of mScn9a;
B6-hSCN9A homo: 2 copies of hSCN9A + 2 copies of mScn9a.
The SCN9A gene encodes the Nav1.7 sodium channel protein, which is primarily expressed in the sensory and sympathetic nerves of the peripheral nervous system and is highly expressed in the dorsal root ganglia. Nav1.7 sodium channels play a crucial role in transmitting positively charged sodium ions within cells, which are essential for generating and transmitting electrical signals. When a person experiences pain, this protein releases sodium ion currents that amplify and stimulate nerve cells, sending electrical signals to the brain, thereby causing the sensation of pain. The SCN9A gene guides the entry of sodium ions into cells and facilitates communication between neurons. Mutations in the SCN9A gene can alter the function of sodium channels in the brain, disrupting neuronal communication and leading to various pain, olfactory, and neurological disorders such as erythromelalgia, paroxysmal extreme pain disorder, Dravet syndrome, small fiber neuropathy, and congenital insensitivity to pain. The abnormal protein function and symptoms resulting from gene mutations are directly related to the severity of the mutations, and different mutation types may lead to completely different conditions.
SCN9A is an excellent target for analgesic drug development. Downregulation of SCN9A expression can alleviate acute pain as well as certain types of inflammatory and neuropathic pain [1]. OliPass Corporation, a South Korean biotechnology company, has developed an antisense peptide nucleic acid (PNA) analgesic targeting SCN9A (OLP-1002), which has entered Phase 2a clinical trials. Antisense PNA is an artificially synthesized DNA/RNA mimic that inhibits RNA/DNA transcription and translation by complementary pairing with RNA/DNA sequences. The drug has shown strong analgesic effects and prolonged therapeutic duration in Australian patients with moderate to severe chronic osteoarthritis pain. It is estimated that due to its potent efficacy, excellent safety profile, and broad therapeutic scope, OLP-1002 could generate over $50 billion in market potential annually [2-4].
The B6-hSCN9A mouse is a mouse Scn9a humanized model, generated by replacing the mouse Scn9a gene (including the 5' UTR and 3' UTR) with the corresponding human SCN9A gene sequence using gene editing technology. Internal research revealed that during the generation of B6-hSCN9A mice, the murine Scn9a gene was inserted unexpectedly, and its precise genomic insertion site remains undetermined*. This strain is suitable for studying the pathogenic mechanisms of neurological diseases such as erythromelalgia, Dravet syndrome, small fiber neuropathy, and congenital insensitivity to pain, as well as for screening analgesic drug candidates. In addition, based on the independently developed TurboKnockout fusion BAC recombination technology, Cyagen can also provide customized services.
* Special notes on the genotype of B6-hSCN9A mice:
B6-hSCN9A het: 1 copy of hSCN9A + 2 copies of mScn9a;
B6-hSCN9A homo: 2 copies of hSCN9A + 2 copies of mScn9a.
B6-hIL23A/hIL12B/hTL1A
Product ID:
C001796
Strain:
C57BL/6Cya
Status:
Description:
The IL23A gene encodes the p19 subunit, a component of interleukin-23 (IL-23), which forms a heterodimer with the p40 subunit (encoded by IL12B) to generate the functional IL-23 cytokine [1]. Primarily expressed by activated dendritic cells, macrophages, and monocytes, IL-23 signals through the IL-23 receptor (IL-23R) complex, activating the JAK-STAT pathway to promote Th17 cell differentiation and maintain IL-17 production. This process drives inflammatory responses and mucosal immunity against extracellular pathogens [1-2]. . Genetic polymorphisms within IL23A are strongly associated with autoimmune and inflammatory diseases, including psoriasis, Crohn's disease, and inflammatory bowel disease, due to dysregulated Th17 activity and chronic inflammation [1-2]. Monoclonal antibodies targeting IL-23, such as risankizumab and guselkumab, selectively block the p19 subunit, demonstrating therapeutic efficacy in psoriasis and inflammatory bowel diseases by suppressing pathogenic IL-17/Th17 pathways [3]. Also, monoclonal antibodies targeting IL-12B, such as ustekinumab, are clinically utilized for the treatment of moderate to severe psoriasis and Crohn's disease [4]. While IL-23 plays a role in protective immunity, its overactivation contributes to tissue damage in autoimmune settings, highlighting its dual function in immune regulation and disease pathogenesis [1-5].
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 [6]. 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 [7]. 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) [6]. 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 [8-10].
B6-hIL23A/hIL12B/hTL1A mouse is a triple-gene humanized model for IL23A, IL12B, and TNFSF15, generated by crossing B6-hIL23A&hIL12B mice (Catalog No.: C001620) with B6-hTL1A (TNFSF15) mice (Catalog No.: C001603). This model serves as a valuable tool for researching immune-related diseases, applicable to studies on immune response regulation and autoimmune diseases. It provides a robust preclinical research platform for the screening, development, and safety evaluation of drugs targeting IL23A/IL12B/TL1A.
The IL23A gene encodes the p19 subunit, a component of interleukin-23 (IL-23), which forms a heterodimer with the p40 subunit (encoded by IL12B) to generate the functional IL-23 cytokine [1]. Primarily expressed by activated dendritic cells, macrophages, and monocytes, IL-23 signals through the IL-23 receptor (IL-23R) complex, activating the JAK-STAT pathway to promote Th17 cell differentiation and maintain IL-17 production. This process drives inflammatory responses and mucosal immunity against extracellular pathogens [1-2]. . Genetic polymorphisms within IL23A are strongly associated with autoimmune and inflammatory diseases, including psoriasis, Crohn's disease, and inflammatory bowel disease, due to dysregulated Th17 activity and chronic inflammation [1-2]. Monoclonal antibodies targeting IL-23, such as risankizumab and guselkumab, selectively block the p19 subunit, demonstrating therapeutic efficacy in psoriasis and inflammatory bowel diseases by suppressing pathogenic IL-17/Th17 pathways [3]. Also, monoclonal antibodies targeting IL-12B, such as ustekinumab, are clinically utilized for the treatment of moderate to severe psoriasis and Crohn's disease [4]. While IL-23 plays a role in protective immunity, its overactivation contributes to tissue damage in autoimmune settings, highlighting its dual function in immune regulation and disease pathogenesis [1-5].
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 [6]. 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 [7]. 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) [6]. 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 [8-10].
B6-hIL23A/hIL12B/hTL1A mouse is a triple-gene humanized model for IL23A, IL12B, and TNFSF15, generated by crossing B6-hIL23A&hIL12B mice (Catalog No.: C001620) with B6-hTL1A (TNFSF15) mice (Catalog No.: C001603). This model serves as a valuable tool for researching immune-related diseases, applicable to studies on immune response regulation and autoimmune diseases. It provides a robust preclinical research platform for the screening, development, and safety evaluation of drugs targeting IL23A/IL12B/TL1A.
B6-hIL31RA
Product ID:
C001917
Strain:
C57BL/6NCya
Status:
Description:
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.
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.
B6-huSLC16A1
Product ID:
C001915
Strain:
C57BL/6NCya
Status:
Description:
The SLC16A1 gene encodes the Monocarboxylate Transporter 1 (MCT1) protein, a vital proton-coupled symporter that facilitates the rapid transmembrane movement of metabolic substrates, including lactate, pyruvate, and ketone bodies (acetoacetate and β-hydroxybutyrate). This gene is ubiquitously expressed across nearly all human tissues to maintain energy balance and pH homeostasis, with notably high levels labeled in the heart, oxidative skeletal muscle fibers, erythrocytes (red blood cells), and the brain (specifically in oligodendrocytes and the blood-brain barrier), while being uniquely "disallowed" or suppressed in normal pancreatic beta-cells to prevent inappropriate insulin release [1]. Functionally, MCT1 is central to the "lactate shuttle" mechanism, allowing tissues to coordinate metabolic fuel exchange by facilitating either the influx or efflux of substrates depending on the concentration gradient and proton motive force [2]. Mutations in SLC16A1 are clinically linked to Erythrocyte Lactate Transporter Defect, which causes exercise-induced muscle cramping and fatigue, and Monocarboxylate Transporter 1 Deficiency, a rare disorder characterized by recurrent episodes of severe ketoacidosis and vomiting triggered by fasting or infection [3]. Conversely, gain-of-function mutations in the gene's promoter lead to familial hyperinsulinemia type 7 (HHF7), where exercise triggers excessive insulin secretion, while its widespread overexpression in various cancers (such as melanoma and lung cancer) supports the Warburg effect by managing lactate efflux to prevent intracellular acidification and fueling tumor progression [4].
The B6-huSLC16A1 mouse is a humanized model constructed through gene-editing technology, in which the sequences from the ATG start codon to the TGA stop codon of the endogenous mouse Slc16a1 gene are replaced with the sequences from the ATG start codon to the TGA stop codon of the human SLC16A1 gene. This model can be used for research on diseases such as Erythrocyte Lactate Transporter Defect, Monocarboxylate Transporter 1 Deficiency, familial hyperinsulinemia type 7 (HHF7), and various cancers, as well as for screening, development, and preclinical evaluation of SLC16A1-targeted therapeutics.
The SLC16A1 gene encodes the Monocarboxylate Transporter 1 (MCT1) protein, a vital proton-coupled symporter that facilitates the rapid transmembrane movement of metabolic substrates, including lactate, pyruvate, and ketone bodies (acetoacetate and β-hydroxybutyrate). This gene is ubiquitously expressed across nearly all human tissues to maintain energy balance and pH homeostasis, with notably high levels labeled in the heart, oxidative skeletal muscle fibers, erythrocytes (red blood cells), and the brain (specifically in oligodendrocytes and the blood-brain barrier), while being uniquely "disallowed" or suppressed in normal pancreatic beta-cells to prevent inappropriate insulin release [1]. Functionally, MCT1 is central to the "lactate shuttle" mechanism, allowing tissues to coordinate metabolic fuel exchange by facilitating either the influx or efflux of substrates depending on the concentration gradient and proton motive force [2]. Mutations in SLC16A1 are clinically linked to Erythrocyte Lactate Transporter Defect, which causes exercise-induced muscle cramping and fatigue, and Monocarboxylate Transporter 1 Deficiency, a rare disorder characterized by recurrent episodes of severe ketoacidosis and vomiting triggered by fasting or infection [3]. Conversely, gain-of-function mutations in the gene's promoter lead to familial hyperinsulinemia type 7 (HHF7), where exercise triggers excessive insulin secretion, while its widespread overexpression in various cancers (such as melanoma and lung cancer) supports the Warburg effect by managing lactate efflux to prevent intracellular acidification and fueling tumor progression [4].
The B6-huSLC16A1 mouse is a humanized model constructed through gene-editing technology, in which the sequences from the ATG start codon to the TGA stop codon of the endogenous mouse Slc16a1 gene are replaced with the sequences from the ATG start codon to the TGA stop codon of the human SLC16A1 gene. This model can be used for research on diseases such as Erythrocyte Lactate Transporter Defect, Monocarboxylate Transporter 1 Deficiency, familial hyperinsulinemia type 7 (HHF7), and various cancers, as well as for screening, development, and preclinical evaluation of SLC16A1-targeted therapeutics.
B6-huIL4/huIL13/huTSLP
Product ID:
C001812
Strain:
C57BL/6NCya
Status:
Description:
The B6-huIL4/huIL13/huTSLP mouse is a triple-gene humanized model obtained by mating B6-huIL4 mice (catalog number: C001628), B6-huIL13 mice (catalog number: C001634), and B6-huTSLP mice (catalog number: C001809). This model can be used for the mechanism research and development of treatment methods in allergic diseases, inflammation and autoimmune diseases, Th2 immune response, parasitic infections, tumor immunology, as well as the development of IL-4/IL13/TSLP-targeted drugs, and the pre-clinical evaluation of drug efficacy and safety.
The B6-huIL4/huIL13/huTSLP mouse is a triple-gene humanized model obtained by mating B6-huIL4 mice (catalog number: C001628), B6-huIL13 mice (catalog number: C001634), and B6-huTSLP mice (catalog number: C001809). This model can be used for the mechanism research and development of treatment methods in allergic diseases, inflammation and autoimmune diseases, Th2 immune response, parasitic infections, tumor immunology, as well as the development of IL-4/IL13/TSLP-targeted drugs, and the pre-clinical evaluation of drug efficacy and safety.
B6-huOSM/hOSMR
Product ID:
C001901
Strain:
C57BL/6NCya
Status:
Description:
The B6-huOSM/hOSMR mouse is a dual-gene humanized model obtained by crossing B6-huOSM mice (catalog No.: C001815) with B6-hOSMR mice (catalog No.: C001841). This model can be used for studying the pathogenesis of inflammatory diseases (such as rheumatoid arthritis, osteoarthritis, and inflammatory bowel disease), cancers (cervical squamous cell carcinoma, lung adenocarcinoma, and pancreatic cancer), pulmonary and skin diseases (such as asthma and psoriasis), cardiovascular diseases (such as atherosclerosis), liver diseases (such as fibrosis), and hematopoietic system and bone marrow-related diseases, as well as for the development of OSM/OSMR-targeted drugs.
The B6-huOSM/hOSMR mouse is a dual-gene humanized model obtained by crossing B6-huOSM mice (catalog No.: C001815) with B6-hOSMR mice (catalog No.: C001841). This model can be used for studying the pathogenesis of inflammatory diseases (such as rheumatoid arthritis, osteoarthritis, and inflammatory bowel disease), cancers (cervical squamous cell carcinoma, lung adenocarcinoma, and pancreatic cancer), pulmonary and skin diseases (such as asthma and psoriasis), cardiovascular diseases (such as atherosclerosis), liver diseases (such as fibrosis), and hematopoietic system and bone marrow-related diseases, as well as for the development of OSM/OSMR-targeted drugs.
B6-huIL4R/huTSLP
Product ID:
C001810
Strain:
C57BL/6NCya
Status:
Description:
The B6-huIL4R/huTSLP mouse is a dual-gene humanized model obtained by mating B6-huIL4RA mice (catalog No.: C001629) with B6-huTSLP mice (catalog No.: C001809). This model can be used in the research of allergic diseases (such as asthma and atopic dermatitis), Th2 immune responses, parasitic infections, tumor immunology, chronic inflammation, and autoimmune diseases, as well as in the development of IL-4Rα/TSLP-targeted drugs.
The B6-huIL4R/huTSLP mouse is a dual-gene humanized model obtained by mating B6-huIL4RA mice (catalog No.: C001629) with B6-huTSLP mice (catalog No.: C001809). This model can be used in the research of allergic diseases (such as asthma and atopic dermatitis), Th2 immune responses, parasitic infections, tumor immunology, chronic inflammation, and autoimmune diseases, as well as in the development of IL-4Rα/TSLP-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-huIL13/huTSLP
Product ID:
C001811
Strain:
C57BL/6NCya
Status:
Description:
Interleukin-13, encoded by the IL13 gene, is a key type 2 immune response cytokine, predominantly expressed by activated Th2 helper T cells, type 2 innate lymphoid cells (ILC2s), and mast cells, and central to type 2 immune responses elicited by allergens or other stimuli [1]. The IL-13 protein, a ~13 kDa molecule with a four-helix bundle structure, mediates its biological effects by binding to the cell surface receptor IL-13Rα1 and recruiting the IL-4Rα chain to form a functional receptor complex, thereby activating the downstream JAK/STAT6 signaling pathway [2]. Key functions of IL-13 include promoting B cell maturation and plasma cell differentiation, inducing IgE isotype switching, and suppressing the pro-inflammatory activity of macrophages, leading to reduced production of pro-inflammatory cytokines and chemokines [3]. Furthermore, IL-13 induces goblet cell hyperplasia, promotes mucus secretion, and contributes to airway remodeling and fibrosis [4]. Numerous studies have established the critical role of IL-13 in the pathogenesis of various diseases, including asthma, allergic rhinitis, atopic dermatitis, and eosinophilic esophagitis [1-4]. Consequently, targeting IL-13 and its signaling pathways has become a significant therapeutic strategy for these conditions; for example, the monoclonal antibody Dupilumab, which simultaneously blocks IL-4 and IL-13 signaling, has demonstrated substantial efficacy in treating diverse type 2 inflammation-related diseases [5]. Thus, IL-13 represents a promising therapeutic target for allergic and inflammatory disorders.
Thymic stromal lymphopoietin (TSLP), an interleukin-7 (IL-7) family cytokine, is encoded by the TSLP gene and is predominantly produced by epithelial cells. Its expression is notably upregulated by environmental cues, including allergens and proteases, positioning it as a sentinel at the interface of environmental exposure and immune activation [6-7]. Secreted by a range of cell types, such as epithelial cells, keratinocytes, mast cells, and dendritic cells, TSLP is critical in the initiation of immune responses, primarily through the activation of dendritic cells and subsequent polarization of T helper type 2 (Th2) cell differentiation. This process has broad implications for diverse immune cell populations and B cell functions relevant to allergic inflammation [7]. Transcriptional regulation of TSLP gene expression is tightly controlled by factors including NF-κB and AP-1, with genetic polymorphisms within the TSLP locus being strongly implicated in asthma susceptibility [6-8]. Dysregulated TSLP signaling is now recognized as a pivotal factor in the pathogenesis of atopic disorders, encompassing conditions such as atopic dermatitis, asthma, allergic rhinitis, and eosinophilic esophagitis [6-9]. For example, tezepelumab, a monoclonal antibody that blocks the TSLP signaling pathway, has demonstrated significant efficacy in clinical trials for patients with severe asthma, reducing acute exacerbations and improving lung function [9]. Consequently, TSLP is under intense investigation as a therapeutic target, with current strategies focusing on disrupting its signaling pathways to modulate allergic and inflammatory diseases.
The B6-huIL13/huTSLP mouse is a double-gene humanized model obtained by mating B6-huIL13 mice (catalog number: C001634) with B6-huTSLP mice (catalog number: C001809). This model can be used for mechanism research and development of treatment methods for allergic diseases, inflammation, and autoimmune diseases, as well as for the development of IL13/TSLP-targeted drugs.
Interleukin-13, encoded by the IL13 gene, is a key type 2 immune response cytokine, predominantly expressed by activated Th2 helper T cells, type 2 innate lymphoid cells (ILC2s), and mast cells, and central to type 2 immune responses elicited by allergens or other stimuli [1]. The IL-13 protein, a ~13 kDa molecule with a four-helix bundle structure, mediates its biological effects by binding to the cell surface receptor IL-13Rα1 and recruiting the IL-4Rα chain to form a functional receptor complex, thereby activating the downstream JAK/STAT6 signaling pathway [2]. Key functions of IL-13 include promoting B cell maturation and plasma cell differentiation, inducing IgE isotype switching, and suppressing the pro-inflammatory activity of macrophages, leading to reduced production of pro-inflammatory cytokines and chemokines [3]. Furthermore, IL-13 induces goblet cell hyperplasia, promotes mucus secretion, and contributes to airway remodeling and fibrosis [4]. Numerous studies have established the critical role of IL-13 in the pathogenesis of various diseases, including asthma, allergic rhinitis, atopic dermatitis, and eosinophilic esophagitis [1-4]. Consequently, targeting IL-13 and its signaling pathways has become a significant therapeutic strategy for these conditions; for example, the monoclonal antibody Dupilumab, which simultaneously blocks IL-4 and IL-13 signaling, has demonstrated substantial efficacy in treating diverse type 2 inflammation-related diseases [5]. Thus, IL-13 represents a promising therapeutic target for allergic and inflammatory disorders.
Thymic stromal lymphopoietin (TSLP), an interleukin-7 (IL-7) family cytokine, is encoded by the TSLP gene and is predominantly produced by epithelial cells. Its expression is notably upregulated by environmental cues, including allergens and proteases, positioning it as a sentinel at the interface of environmental exposure and immune activation [6-7]. Secreted by a range of cell types, such as epithelial cells, keratinocytes, mast cells, and dendritic cells, TSLP is critical in the initiation of immune responses, primarily through the activation of dendritic cells and subsequent polarization of T helper type 2 (Th2) cell differentiation. This process has broad implications for diverse immune cell populations and B cell functions relevant to allergic inflammation [7]. Transcriptional regulation of TSLP gene expression is tightly controlled by factors including NF-κB and AP-1, with genetic polymorphisms within the TSLP locus being strongly implicated in asthma susceptibility [6-8]. Dysregulated TSLP signaling is now recognized as a pivotal factor in the pathogenesis of atopic disorders, encompassing conditions such as atopic dermatitis, asthma, allergic rhinitis, and eosinophilic esophagitis [6-9]. For example, tezepelumab, a monoclonal antibody that blocks the TSLP signaling pathway, has demonstrated significant efficacy in clinical trials for patients with severe asthma, reducing acute exacerbations and improving lung function [9]. Consequently, TSLP is under intense investigation as a therapeutic target, with current strategies focusing on disrupting its signaling pathways to modulate allergic and inflammatory diseases.
The B6-huIL13/huTSLP mouse is a double-gene humanized model obtained by mating B6-huIL13 mice (catalog number: C001634) with B6-huTSLP mice (catalog number: C001809). This model can be used for mechanism research and development of treatment methods for allergic diseases, inflammation, and autoimmune diseases, as well as for the development of IL13/TSLP-targeted drugs.
BALB/c-hIL13
Product ID:
C001797
Strain:
BALB/cAnCya
Status:
Description:
Interleukin-13, encoded by the IL13 gene, is a key type 2 immune response cytokine, predominantly expressed by activated Th2 helper T cells, type 2 innate lymphoid cells (ILC2s), and mast cells, and central to type 2 immune responses elicited by allergens or other stimuli [1]. The IL-13 protein, a ~13 kDa molecule with a four-helix bundle structure, mediates its biological effects by binding to the cell surface receptor IL-13Rα1 and recruiting the IL-4Rα chain to form a functional receptor complex, thereby activating the downstream JAK/STAT6 signaling pathway [2]. Key functions of IL-13 include promoting B cell maturation and plasma cell differentiation, inducing IgE isotype switching, and suppressing the pro-inflammatory activity of macrophages, leading to reduced production of pro-inflammatory cytokines and chemokines [3]. Furthermore, IL-13 induces goblet cell hyperplasia, promotes mucus secretion, and contributes to airway remodeling and fibrosis [4]. Numerous studies have established the critical role of IL-13 in the pathogenesis of various diseases, including asthma, allergic rhinitis, atopic dermatitis, and eosinophilic esophagitis [1-4]. Consequently, targeting IL-13 and its signaling pathways has become a significant therapeutic strategy for these conditions; for example, the monoclonal antibody Dupilumab, which simultaneously blocks IL-4 and IL-13 signaling, has demonstrated substantial efficacy in treating diverse type 2 inflammation-related diseases [5]. Thus, IL-13 represents a promising therapeutic target for allergic and inflammatory disorders.
The BALB/c-hIL13 mouse is a humanized model constructed using gene editing technology to replace the sequence of the mouse Il13 gene in situ with the corresponding sequence from the human IL13 gene. This model can be used for studying the pathological mechanisms and therapeutic approaches of allergic and inflammatory diseases, and for the development of IL13-targeted drugs.
Interleukin-13, encoded by the IL13 gene, is a key type 2 immune response cytokine, predominantly expressed by activated Th2 helper T cells, type 2 innate lymphoid cells (ILC2s), and mast cells, and central to type 2 immune responses elicited by allergens or other stimuli [1]. The IL-13 protein, a ~13 kDa molecule with a four-helix bundle structure, mediates its biological effects by binding to the cell surface receptor IL-13Rα1 and recruiting the IL-4Rα chain to form a functional receptor complex, thereby activating the downstream JAK/STAT6 signaling pathway [2]. Key functions of IL-13 include promoting B cell maturation and plasma cell differentiation, inducing IgE isotype switching, and suppressing the pro-inflammatory activity of macrophages, leading to reduced production of pro-inflammatory cytokines and chemokines [3]. Furthermore, IL-13 induces goblet cell hyperplasia, promotes mucus secretion, and contributes to airway remodeling and fibrosis [4]. Numerous studies have established the critical role of IL-13 in the pathogenesis of various diseases, including asthma, allergic rhinitis, atopic dermatitis, and eosinophilic esophagitis [1-4]. Consequently, targeting IL-13 and its signaling pathways has become a significant therapeutic strategy for these conditions; for example, the monoclonal antibody Dupilumab, which simultaneously blocks IL-4 and IL-13 signaling, has demonstrated substantial efficacy in treating diverse type 2 inflammation-related diseases [5]. Thus, IL-13 represents a promising therapeutic target for allergic and inflammatory disorders.
The BALB/c-hIL13 mouse is a humanized model constructed using gene editing technology to replace the sequence of the mouse Il13 gene in situ with the corresponding sequence from the human IL13 gene. This model can be used for studying the pathological mechanisms and therapeutic approaches of allergic and inflammatory diseases, and for the development of IL13-targeted drugs.
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