필터
에 대한 검색 결과 140 건
정렬 기준:
알파벳순 (A-Z)
베스트셀러
B6-H11-hBDCA2 (hCLEC4C)
제품 ID:
C001693
계통(Strain):
C57BL/6NCya
상태:
설명:
The CLEC4C gene, also known as BDCA-2 or CD303, encodes a type II transmembrane C-type lectin receptor predominantly expressed by plasmacytoid dendritic cells (pDCs) [1]. This receptor plays a critical role in pDC biology and serves as a key marker for this cell type [2]. The CLEC4C protein, featuring a carbohydrate recognition domain, is implicated in the capture and subsequent processing of antigens, potentially through the recognition of specific glycans and immunoglobulin G [1]. Functionally, CLEC4C acts as a signaling receptor within pDCs, and its engagement can negatively regulate the production of type I interferons, thereby modulating immune responses [2]. Notably, dysregulation of CLEC4C expression and pDC function has been associated with the pathogenesis of autoimmune disorders, including systemic lupus erythematosus (SLE), as well as in the context of certain hematological malignancies [3]. Litifilimab is a monoclonal antibody that targets CLEC4C and is under investigation for the treatment of SLE and other interferonopathies [4].
B6-H11-hCLEC4C mice are humanized models generated by gene editing technology, in which the human CLEC4C genomic DNA was inserted at the H11 safe harbor. This modification does not affect the expression of the mouse homologous gene Clec4b1. This model can be used to study the pathological mechanisms and therapeutic methods of autoimmune disorders and hematological malignancies, as well as the screening and development of CLEC4C-targeted drugs, and preclinical efficacy and safety evaluations.
The CLEC4C gene, also known as BDCA-2 or CD303, encodes a type II transmembrane C-type lectin receptor predominantly expressed by plasmacytoid dendritic cells (pDCs) [1]. This receptor plays a critical role in pDC biology and serves as a key marker for this cell type [2]. The CLEC4C protein, featuring a carbohydrate recognition domain, is implicated in the capture and subsequent processing of antigens, potentially through the recognition of specific glycans and immunoglobulin G [1]. Functionally, CLEC4C acts as a signaling receptor within pDCs, and its engagement can negatively regulate the production of type I interferons, thereby modulating immune responses [2]. Notably, dysregulation of CLEC4C expression and pDC function has been associated with the pathogenesis of autoimmune disorders, including systemic lupus erythematosus (SLE), as well as in the context of certain hematological malignancies [3]. Litifilimab is a monoclonal antibody that targets CLEC4C and is under investigation for the treatment of SLE and other interferonopathies [4].
B6-H11-hCLEC4C mice are humanized models generated by gene editing technology, in which the human CLEC4C genomic DNA was inserted at the H11 safe harbor. This modification does not affect the expression of the mouse homologous gene Clec4b1. This model can be used to study the pathological mechanisms and therapeutic methods of autoimmune disorders and hematological malignancies, as well as the screening and development of CLEC4C-targeted drugs, and preclinical efficacy and safety evaluations.
B6-hTL1A/hNLRP3
제품 ID:
C001690
계통(Strain):
C57BL/6N;6JCya
상태:
설명:
TNF-like ligand 1A (TL1A), also known as TNF superfamily member 15 (TNFSF15), is a member of the tumor necrosis factor (TNF) family encoded by the TNFSF15 gene in humans. TL1A acts as a ligand for death receptor 3 (DR3) and decoy receptor 3 (DcR3), providing a stimulatory signal for downstream pathways. It regulates the proliferation, activation, and apoptosis of effector cells, as well as cytokine and chemokine production. TL1A is expressed in various immune cells, including monocytes, macrophages, dendritic cells, and T cells, as well as in non-immune cells such as synovial fibroblasts and endothelial cells. It plays a crucial role in modulating immune responses by promoting the differentiation and survival of T cells, particularly Th17 cells involved in inflammatory processes [1]. TL1A enhances IL-2 responses in anti-CD3/CD28-stimulated T cells and synergizes with IL-12 and IL-18 to augment IFN-γ release in human T and NK cells, biasing T cell differentiation toward a Th1 phenotype [2]. Dysregulation of TL1A expression is implicated in autoimmune diseases, including inflammatory bowel disease (IBD), rheumatoid arthritis (RA), primary biliary cholangitis (PBC), systemic lupus erythematosus (SLE), and ankylosing spondylitis (AS) [1]. TL1A has emerged as a promising therapeutic target, with ongoing research focused on developing monoclonal antibodies and other biologics to neutralize TL1A and reduce inflammation in autoimmune disorders. Clinical trial results suggest that TL1A inhibition can be used in the treatment of various autoimmune diseases, particularly IBD [3-5].
The Cryopyrin protein, encoded by the NOD-like receptor family pyrin domain-containing 3 (NLRP3) gene, is a core component of the inflammasome in the innate immune system. As a member of the NOD-like receptor (NLR) family, NLRP3 is predominantly expressed in leukocytes and chondrocytes. It participates in the host defense against damage and infection by recognizing pathogen-associated molecular patterns (PAMPs) or damage-associated molecular patterns (DAMPs) to activate immune responses [6]. In its inactive monomeric state, NLRP3 senses intracellular damage signals, such as abnormal protein aggregates and lipid accumulation. Upon activation, NLRP3 oligomerizes, adopting an active conformation and assembling into inflammasome complexes, subsequently activating Caspase-1 to drive the maturation and secretion of pro-inflammatory cytokines, including IL-1β and IL-18 [6-7]. Activated NLRP3 not only induces the release of inflammatory cytokines but also triggers lytic cell pyroptosis. The intracellular components released during pyroptosis can further amplify inflammatory signals, forming a positive feedback loop of autoinflammation. Moreover, IL-1β can exacerbate the inflammatory cascade by stimulating the production of inflammatory markers such as IL-6 and high-sensitivity C-reactive protein (hsCRP) [8-9]. Given NLRP3's upstream position relative to IL-1β/IL-18 and other inflammatory factors, targeting its activity can effectively block the self-reinforcing mechanism of chronic inflammation, providing a significant therapeutic strategy for inflammation-related diseases [10]. The potential therapeutic areas include Alzheimer’s disease, Parkinson’s disease (via neuroinflammation modulation), inflammatory bowel disease, metabolic dysfunction-associated steatohepatitis (MASH), gout, and obesity-related metabolic inflammation [11-12].
B6-hTL1A/hNLRP3 mice are TL1A and NLRP3 double humanized mouse models obtained by mating TL1A humanized mouse models (Catalog No. C001603) with NLRP3 humanized mouse models (Catalog No. C001616). B6-hTL1A/hNLRP3 mice express human TL1A and NLRP3 genomic sequences under the control of mouse promoters. This model is capable of reproducing human TL1A and NLRP3 and is a valuable tool for studying autoimmune diseases and inflammation-related diseases. In addition, this model also provides a powerful preclinical research platform for evaluating the efficacy and mechanism of therapeutic drugs targeting TL1A and NLRP3.
TNF-like ligand 1A (TL1A), also known as TNF superfamily member 15 (TNFSF15), is a member of the tumor necrosis factor (TNF) family encoded by the TNFSF15 gene in humans. TL1A acts as a ligand for death receptor 3 (DR3) and decoy receptor 3 (DcR3), providing a stimulatory signal for downstream pathways. It regulates the proliferation, activation, and apoptosis of effector cells, as well as cytokine and chemokine production. TL1A is expressed in various immune cells, including monocytes, macrophages, dendritic cells, and T cells, as well as in non-immune cells such as synovial fibroblasts and endothelial cells. It plays a crucial role in modulating immune responses by promoting the differentiation and survival of T cells, particularly Th17 cells involved in inflammatory processes [1]. TL1A enhances IL-2 responses in anti-CD3/CD28-stimulated T cells and synergizes with IL-12 and IL-18 to augment IFN-γ release in human T and NK cells, biasing T cell differentiation toward a Th1 phenotype [2]. Dysregulation of TL1A expression is implicated in autoimmune diseases, including inflammatory bowel disease (IBD), rheumatoid arthritis (RA), primary biliary cholangitis (PBC), systemic lupus erythematosus (SLE), and ankylosing spondylitis (AS) [1]. TL1A has emerged as a promising therapeutic target, with ongoing research focused on developing monoclonal antibodies and other biologics to neutralize TL1A and reduce inflammation in autoimmune disorders. Clinical trial results suggest that TL1A inhibition can be used in the treatment of various autoimmune diseases, particularly IBD [3-5].
The Cryopyrin protein, encoded by the NOD-like receptor family pyrin domain-containing 3 (NLRP3) gene, is a core component of the inflammasome in the innate immune system. As a member of the NOD-like receptor (NLR) family, NLRP3 is predominantly expressed in leukocytes and chondrocytes. It participates in the host defense against damage and infection by recognizing pathogen-associated molecular patterns (PAMPs) or damage-associated molecular patterns (DAMPs) to activate immune responses [6]. In its inactive monomeric state, NLRP3 senses intracellular damage signals, such as abnormal protein aggregates and lipid accumulation. Upon activation, NLRP3 oligomerizes, adopting an active conformation and assembling into inflammasome complexes, subsequently activating Caspase-1 to drive the maturation and secretion of pro-inflammatory cytokines, including IL-1β and IL-18 [6-7]. Activated NLRP3 not only induces the release of inflammatory cytokines but also triggers lytic cell pyroptosis. The intracellular components released during pyroptosis can further amplify inflammatory signals, forming a positive feedback loop of autoinflammation. Moreover, IL-1β can exacerbate the inflammatory cascade by stimulating the production of inflammatory markers such as IL-6 and high-sensitivity C-reactive protein (hsCRP) [8-9]. Given NLRP3's upstream position relative to IL-1β/IL-18 and other inflammatory factors, targeting its activity can effectively block the self-reinforcing mechanism of chronic inflammation, providing a significant therapeutic strategy for inflammation-related diseases [10]. The potential therapeutic areas include Alzheimer’s disease, Parkinson’s disease (via neuroinflammation modulation), inflammatory bowel disease, metabolic dysfunction-associated steatohepatitis (MASH), gout, and obesity-related metabolic inflammation [11-12].
B6-hTL1A/hNLRP3 mice are TL1A and NLRP3 double humanized mouse models obtained by mating TL1A humanized mouse models (Catalog No. C001603) with NLRP3 humanized mouse models (Catalog No. C001616). B6-hTL1A/hNLRP3 mice express human TL1A and NLRP3 genomic sequences under the control of mouse promoters. This model is capable of reproducing human TL1A and NLRP3 and is a valuable tool for studying autoimmune diseases and inflammation-related diseases. In addition, this model also provides a powerful preclinical research platform for evaluating the efficacy and mechanism of therapeutic drugs targeting TL1A and NLRP3.
B6-huTNFR2 (huTNFRSF1B)
제품 ID:
C001913
계통(Strain):
C57BL/6NCya
상태:
설명:
The TNFR2 gene, officially known as TNFRSF1B (Tumor Necrosis Factor Receptor Superfamily Member 1B), encodes the Tumor Necrosis Factor Receptor 2 protein (also called p75 or CD120b), a member of the TNF-receptor superfamily. Unlike its counterpart TNFR1 (which is widely expressed), TNFR2 exhibits more restricted expression, primarily on specific immune cells like regulatory T cells (Tregs), endothelial cells, and certain neuronal cells and microglia in the central nervous system (CNS), as well as on various cancer cells and mesenchymal stem cells [1]. The TNFR2 protein functions as a receptor for the cytokine TNF-α and generally signals for cell survival, proliferation, and anti-apoptosis by recruiting anti-apoptotic proteins and activating the NF-κB pathway (lacking the death domain found in TNFR1, which typically signals apoptosis) [2]. A soluble form of the receptor, sTNFR2, is also produced via proteolytic processing and can act as a TNF-α binding protein [3]. Dysregulation or polymorphisms of the TNFRSF1B gene and its encoded protein are associated with various diseases, including autoimmune disorders (such as rheumatoid arthritis, systemic lupus erythematosus, and inflammatory bowel disease), several cancers (including breast, cervical, and colon cancer, where it promotes tumor growth and immune escape), and neurodegenerative diseases like Alzheimer's and schizophrenia.
The B6-huTNFR2 (huTNFRSF1B) mouse is a humanized model constructed through gene-editing technology, in which the upstream of exon 2 to p.G258 of the mouse Tnfrsf1b gene was replaced with the upstream of exon 2 to p.D257 of the human TNFRSF1B gene. This model can be used for research on diseases such as autoimmune disorders, several cancers, neurodegenerative diseases like Alzheimer's and schizophrenia, as well as for screening, development, and preclinical evaluation of TNFRSF1B-targeted therapeutics.
The TNFR2 gene, officially known as TNFRSF1B (Tumor Necrosis Factor Receptor Superfamily Member 1B), encodes the Tumor Necrosis Factor Receptor 2 protein (also called p75 or CD120b), a member of the TNF-receptor superfamily. Unlike its counterpart TNFR1 (which is widely expressed), TNFR2 exhibits more restricted expression, primarily on specific immune cells like regulatory T cells (Tregs), endothelial cells, and certain neuronal cells and microglia in the central nervous system (CNS), as well as on various cancer cells and mesenchymal stem cells [1]. The TNFR2 protein functions as a receptor for the cytokine TNF-α and generally signals for cell survival, proliferation, and anti-apoptosis by recruiting anti-apoptotic proteins and activating the NF-κB pathway (lacking the death domain found in TNFR1, which typically signals apoptosis) [2]. A soluble form of the receptor, sTNFR2, is also produced via proteolytic processing and can act as a TNF-α binding protein [3]. Dysregulation or polymorphisms of the TNFRSF1B gene and its encoded protein are associated with various diseases, including autoimmune disorders (such as rheumatoid arthritis, systemic lupus erythematosus, and inflammatory bowel disease), several cancers (including breast, cervical, and colon cancer, where it promotes tumor growth and immune escape), and neurodegenerative diseases like Alzheimer's and schizophrenia.
The B6-huTNFR2 (huTNFRSF1B) mouse is a humanized model constructed through gene-editing technology, in which the upstream of exon 2 to p.G258 of the mouse Tnfrsf1b gene was replaced with the upstream of exon 2 to p.D257 of the human TNFRSF1B gene. This model can be used for research on diseases such as autoimmune disorders, several cancers, neurodegenerative diseases like Alzheimer's and schizophrenia, as well as for screening, development, and preclinical evaluation of TNFRSF1B-targeted therapeutics.
Cd11b-hCD89(FCAR)
제품 ID:
C001793
계통(Strain):
C57BL/6NCya
상태:
설명:
CD89, also known as Fcα receptor (FCAR), is a receptor on the surface of various immune cells and belongs to the Fc receptor family. Fc receptors bind antibodies, linking the immune system’s recognition of pathogens with cellular immune responses. CD89 is primarily expressed on monocytes/macrophages, neutrophils, eosinophils, dendritic cells, and Kupffer cells in the liver, unlike other Fc receptors expressed on lymphocytes [1]. The function of CD89 primarily involves binding with IgA antibodies (especially IgA1 and IgA2), initiating various immune responses. CD89 can trigger phagocytosis (engulfing and destroying pathogens), antibody-dependent cellular cytotoxicity (ADCC) (killing infected or cancerous cells), and release inflammatory mediators (promoting inflammatory responses and recruiting immune cells) [2]. IgA nephropathy (IgAN) is a disease closely associated with CD89 and is the most common form of glomerulonephritis, characterized by the deposition of IgA (particularly IgA1) in the glomeruli. As the myeloid cell-specific Fc receptor for IgA, CD89 specifically binds IgA1, a highly glycosylated IgA subtype predominantly found in serum and responsible for neutralizing pathogens at mucosal surfaces [3-4]. In IgA nephropathy, one pathological mechanism is the formation of immune complexes between aberrantly glycosylated IgA1 and CD89. These complexes deposit in the glomerular mesangium, activate mesangial cells, and trigger inflammation, fibrosis, and kidney structural damage. Without treatment, the condition can progress to chronic kidney disease (CKD) and even end-stage renal disease (ESRD) [5-7].
Since mice lack a homologous gene to human CD89, introducing the human CD89 gene into mice aids in studying immune mechanisms and IgA nephropathy (IgAN). The Cd11b-hCD89(FCAR) mice are a humanized model constructed by integrating the coding sequence (CDS) of the human CD89 gene downstream of the TAA stop codon of the mouse Cd11b (Itgam) gene. The human CD89 gene is specifically expressed in myeloid cells under the regulation of the mouse Cd11b gene promoter. Cd11b-hCD89(FCAR) mice can be used in studies on immune responses, autoimmune mechanisms, as well as tumor and infectious diseases. They can also be crossed with the IgA1 humanized mouse model (Product No.: C001565) to construct an IgA nephropathy (IgAN) mouse model that better recapitulates human genetic mechanisms and pathological phenotypes [8], for researching IgAN mechanisms and developing therapies.
CD89, also known as Fcα receptor (FCAR), is a receptor on the surface of various immune cells and belongs to the Fc receptor family. Fc receptors bind antibodies, linking the immune system’s recognition of pathogens with cellular immune responses. CD89 is primarily expressed on monocytes/macrophages, neutrophils, eosinophils, dendritic cells, and Kupffer cells in the liver, unlike other Fc receptors expressed on lymphocytes [1]. The function of CD89 primarily involves binding with IgA antibodies (especially IgA1 and IgA2), initiating various immune responses. CD89 can trigger phagocytosis (engulfing and destroying pathogens), antibody-dependent cellular cytotoxicity (ADCC) (killing infected or cancerous cells), and release inflammatory mediators (promoting inflammatory responses and recruiting immune cells) [2]. IgA nephropathy (IgAN) is a disease closely associated with CD89 and is the most common form of glomerulonephritis, characterized by the deposition of IgA (particularly IgA1) in the glomeruli. As the myeloid cell-specific Fc receptor for IgA, CD89 specifically binds IgA1, a highly glycosylated IgA subtype predominantly found in serum and responsible for neutralizing pathogens at mucosal surfaces [3-4]. In IgA nephropathy, one pathological mechanism is the formation of immune complexes between aberrantly glycosylated IgA1 and CD89. These complexes deposit in the glomerular mesangium, activate mesangial cells, and trigger inflammation, fibrosis, and kidney structural damage. Without treatment, the condition can progress to chronic kidney disease (CKD) and even end-stage renal disease (ESRD) [5-7].
Since mice lack a homologous gene to human CD89, introducing the human CD89 gene into mice aids in studying immune mechanisms and IgA nephropathy (IgAN). The Cd11b-hCD89(FCAR) mice are a humanized model constructed by integrating the coding sequence (CDS) of the human CD89 gene downstream of the TAA stop codon of the mouse Cd11b (Itgam) gene. The human CD89 gene is specifically expressed in myeloid cells under the regulation of the mouse Cd11b gene promoter. Cd11b-hCD89(FCAR) mice can be used in studies on immune responses, autoimmune mechanisms, as well as tumor and infectious diseases. They can also be crossed with the IgA1 humanized mouse model (Product No.: C001565) to construct an IgA nephropathy (IgAN) mouse model that better recapitulates human genetic mechanisms and pathological phenotypes [8], for researching IgAN mechanisms and developing therapies.
huIL6/hIL6RA/Apoe-KO
제품 ID:
C002139
계통(Strain):
C57BL/6Cya
상태:
설명:
Interleukin-6 (IL-6) is a cytokine that plays a crucial role in inflammation and B cell maturation. It is primarily produced and secreted into the serum at sites of acute and chronic inflammation, inducing inflammatory responses through the interleukin-6 receptor alpha (IL-6Rα). The IL6RA (IL6R, also known as CD126) gene encodes a subunit of the interleukin-6 (IL-6) receptor complex. The IL-6 receptor is a protein complex composed of the IL6RA protein and the interleukin-6 signal transducer (IL6ST/GP130/IL6-beta). This receptor subunit is shared by many other cytokines. The expression of IL-6R is primarily restricted to hepatocytes, leukocytes, and megakaryocytes. Upon binding to IL-6Rα, IL-6 interacts with two GP130 molecules to form a hexameric complex in a 2:2:2 configuration [1]. Once the IL-6 receptor complex is activated, multiple downstream events allow IL-6 to mediate its diverse effects. These include the pathways of the GTPase Ras and its effector Raf, the mitogen-activated protein kinase cascade that controls cellular proliferation and differentiation, and the pathways involving tyrosine kinases of the Jak family and transcription factors of the STAT family [2].
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 [3]. 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 [4]. 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 [3-6]. In addition, ApoE forms a complex with activated C1q, becoming a checkpoint inhibitor target of the classical complement pathway [7].
The huIL6/hIL6RA/Apoe-KO mouse is a combined genetically modified model generated by crossing the huIL6 mouse (Catalog No.: C001605), the hIL6RA mouse (Catalog No.: C001606), and the Apoe-KO(6J) mouse (Catalog No.: C001507). The huIL6/hIL6RA/Apoe-KO mouse can be utilized for the screening, pharmacodynamic evaluation, safety assessment, and mechanism of action studies of IL6/IL6RA-targeted therapeutics. With the Apoe knockout background, the model can also be used for research on hypercholesterolemia and atherosclerosis, providing a preclinical research tool for exploring the effects of IL6/IL6RA-targeted interventions in relevant disease settings.
Interleukin-6 (IL-6) is a cytokine that plays a crucial role in inflammation and B cell maturation. It is primarily produced and secreted into the serum at sites of acute and chronic inflammation, inducing inflammatory responses through the interleukin-6 receptor alpha (IL-6Rα). The IL6RA (IL6R, also known as CD126) gene encodes a subunit of the interleukin-6 (IL-6) receptor complex. The IL-6 receptor is a protein complex composed of the IL6RA protein and the interleukin-6 signal transducer (IL6ST/GP130/IL6-beta). This receptor subunit is shared by many other cytokines. The expression of IL-6R is primarily restricted to hepatocytes, leukocytes, and megakaryocytes. Upon binding to IL-6Rα, IL-6 interacts with two GP130 molecules to form a hexameric complex in a 2:2:2 configuration [1]. Once the IL-6 receptor complex is activated, multiple downstream events allow IL-6 to mediate its diverse effects. These include the pathways of the GTPase Ras and its effector Raf, the mitogen-activated protein kinase cascade that controls cellular proliferation and differentiation, and the pathways involving tyrosine kinases of the Jak family and transcription factors of the STAT family [2].
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 [3]. 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 [4]. 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 [3-6]. In addition, ApoE forms a complex with activated C1q, becoming a checkpoint inhibitor target of the classical complement pathway [7].
The huIL6/hIL6RA/Apoe-KO mouse is a combined genetically modified model generated by crossing the huIL6 mouse (Catalog No.: C001605), the hIL6RA mouse (Catalog No.: C001606), and the Apoe-KO(6J) mouse (Catalog No.: C001507). The huIL6/hIL6RA/Apoe-KO mouse can be utilized for the screening, pharmacodynamic evaluation, safety assessment, and mechanism of action studies of IL6/IL6RA-targeted therapeutics. With the Apoe knockout background, the model can also be used for research on hypercholesterolemia and atherosclerosis, providing a preclinical research tool for exploring the effects of IL6/IL6RA-targeted interventions in relevant disease settings.
huIL18R1/huIL18RAP/huIL18BP
제품 ID:
C002137
계통(Strain):
C57BL/6Cya
상태:
설명:
Interleukin-18 (IL-18) is an important pro-inflammatory cytokine that binds to its receptor complex (IL-18Rα encoded by IL18R1 and IL-18Rβ encoded by IL18RAP), activating downstream MyD88/NF-κB and MAPK signaling pathways and playing key regulatory roles in innate and adaptive immunity [1]. The IL18BP (Interleukin 18 Binding Protein) gene encodes a secreted, high-affinity, naturally occurring antagonist of the proinflammatory cytokine 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 [2]. 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 [3].
The huIL18R1/huIL18RAP/huIL18BP mouse is a triple-gene humanized model obtained by crossing the huIL18R1/huIL18RAP mouse (Catalog No.: C002016) with the huIL18BP mouse (Catalog No.: C001869). The huIL18R1/huIL18RAP/huIL18BP mouse can be utilized for screening, pharmacodynamic evaluation, safety assessment, and mechanism of action studies of multi-target therapeutics targeting the IL-18 receptor complex (IL18R1/IL18RAP) and the natural antagonist of IL-18, IL18BP. It provides an ideal preclinical research platform for developing innovative therapies for inflammatory bowel disease (IBD), rheumatoid arthritis (RA), psoriasis, and systemic lupus erythematosus (SLE), as well as for tumor immunology-related research.
Interleukin-18 (IL-18) is an important pro-inflammatory cytokine that binds to its receptor complex (IL-18Rα encoded by IL18R1 and IL-18Rβ encoded by IL18RAP), activating downstream MyD88/NF-κB and MAPK signaling pathways and playing key regulatory roles in innate and adaptive immunity [1]. The IL18BP (Interleukin 18 Binding Protein) gene encodes a secreted, high-affinity, naturally occurring antagonist of the proinflammatory cytokine 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 [2]. 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 [3].
The huIL18R1/huIL18RAP/huIL18BP mouse is a triple-gene humanized model obtained by crossing the huIL18R1/huIL18RAP mouse (Catalog No.: C002016) with the huIL18BP mouse (Catalog No.: C001869). The huIL18R1/huIL18RAP/huIL18BP mouse can be utilized for screening, pharmacodynamic evaluation, safety assessment, and mechanism of action studies of multi-target therapeutics targeting the IL-18 receptor complex (IL18R1/IL18RAP) and the natural antagonist of IL-18, IL18BP. It provides an ideal preclinical research platform for developing innovative therapies for inflammatory bowel disease (IBD), rheumatoid arthritis (RA), psoriasis, and systemic lupus erythematosus (SLE), as well as for tumor immunology-related research.
huIL5RA
제품 ID:
C002007
계통(Strain):
C57BL/6NCya
상태:
설명:
The IL5RA gene encodes the interleukin-5 receptor subunit alpha (IL5RA), the receptor subunit that specifically binds IL5. It is primarily expressed on eosinophils, basophils, and their progenitor cells, with low expression levels in most normal tissues [1]. IL5RA plays a critical role in the proliferation, differentiation, survival, recruitment, and activation of eosinophils. Upon binding to IL5, it activates downstream signaling pathways such as JAK2-STAT5, thereby promoting type 2 inflammatory responses. Excessive activation of the IL5/IL5RA axis in cells or tissues can lead to eosinophil expansion and tissue infiltration, exacerbating inflammation and tissue damage [2]. IL5RA exerts a central regulatory role in the pathogenesis of eosinophil-related inflammatory diseases, including severe eosinophilic asthma (SEA), chronic rhinosinusitis with nasal polyps (CRSwNP), and eosinophilic granulomatosis with polyangiitis (EGPA) [3-5]. Studies have shown that abnormal IL5RA expression is causally associated with the genetic risk of multiple myeloma (MM), positioning it as a potential tumor biomarker and therapeutic target [6]. Humanized anti-IL5RA CAR-T cell therapy can effectively deplete eosinophils and their precursors at various developmental stages in the bone marrow and peripheral blood [1]. Currently, multiple clinical drugs targeting the IL-5/IL5RA pathway have been approved or are under development, including mepolizumab, reslizumab, and benralizumab [7-8].
The huIL5RA mouse was generated by replacing the mouse Il5ra endogenous extracellular domain with the human IL5RA extracellular domain. The murine transmembrane-cytoplasmic region was preserved. huIL5RA mice can be used for research and development as well as preclinical pharmacological and efficacy evaluation of IL5RA-targeted drugs for multiple eosinophil-related inflammatory diseases, including severe eosinophilic asthma (SEA), chronic rhinosinusitis with nasal polyps (CRSwNP), and eosinophilic granulomatosis with polyangiitis (EGPA), as well as multiple myeloma (MM).
The IL5RA gene encodes the interleukin-5 receptor subunit alpha (IL5RA), the receptor subunit that specifically binds IL5. It is primarily expressed on eosinophils, basophils, and their progenitor cells, with low expression levels in most normal tissues [1]. IL5RA plays a critical role in the proliferation, differentiation, survival, recruitment, and activation of eosinophils. Upon binding to IL5, it activates downstream signaling pathways such as JAK2-STAT5, thereby promoting type 2 inflammatory responses. Excessive activation of the IL5/IL5RA axis in cells or tissues can lead to eosinophil expansion and tissue infiltration, exacerbating inflammation and tissue damage [2]. IL5RA exerts a central regulatory role in the pathogenesis of eosinophil-related inflammatory diseases, including severe eosinophilic asthma (SEA), chronic rhinosinusitis with nasal polyps (CRSwNP), and eosinophilic granulomatosis with polyangiitis (EGPA) [3-5]. Studies have shown that abnormal IL5RA expression is causally associated with the genetic risk of multiple myeloma (MM), positioning it as a potential tumor biomarker and therapeutic target [6]. Humanized anti-IL5RA CAR-T cell therapy can effectively deplete eosinophils and their precursors at various developmental stages in the bone marrow and peripheral blood [1]. Currently, multiple clinical drugs targeting the IL-5/IL5RA pathway have been approved or are under development, including mepolizumab, reslizumab, and benralizumab [7-8].
The huIL5RA mouse was generated by replacing the mouse Il5ra endogenous extracellular domain with the human IL5RA extracellular domain. The murine transmembrane-cytoplasmic region was preserved. huIL5RA mice can be used for research and development as well as preclinical pharmacological and efficacy evaluation of IL5RA-targeted drugs for multiple eosinophil-related inflammatory diseases, including severe eosinophilic asthma (SEA), chronic rhinosinusitis with nasal polyps (CRSwNP), and eosinophilic granulomatosis with polyangiitis (EGPA), as well as multiple myeloma (MM).
huCD40LG
제품 ID:
C001720
계통(Strain):
C57BL/6NCya
상태:
설명:
The CD40LG gene is located on the X chromosome (Xq26.3) and encodes CD40 ligand (CD40L, also known as CD154), a type II transmembrane protein mainly expressed on activated T cells, platelets, and some B cells. Under inflammatory conditions, monocytes, natural killer cells, mast cells, and basophils can also be induced to express CD40L [1-3]. This protein binds to CD40 on the surface of antigen-presenting cells (such as B cells and dendritic cells), mediating key immune functions including T cell-dependent B cell activation, immunoglobulin class switching, and germinal center formation [3]. The CD40/CD40L interaction also regulates thrombosis, inflammatory responses, hematopoiesis, and the tumor immune microenvironment. Abnormal regulation of CD40LG is associated with X-linked hyper-IgM syndrome (XHIGM), a primary immunodeficiency disease characterized by recurrent infections due to defective antibody production [4]. In addition, abnormal expression of CD40L is involved in diseases such as systemic lupus erythematosus and atherosclerosis through its pro-inflammatory effects [5-6]. Due to the important role of the CD40/CD40L interaction in immune activation, CD40/CD40L has been an important target for immunotherapy. In recent years, significant progress has been made in CD40/CD40L-targeted therapy. Various drugs have been developed, including agonistic/antagonistic monoclonal antibodies, cellular vaccines, adenoviral vectors, and protein antagonists, and have shown therapeutic potential in malignant tumors, autoimmune diseases, and allograft rejection [7].
The huCD40LG mice are a humanized model constructed by using gene editing technology to replace the endogenous extracellular domain of the mouse Cd40lg gene with the extracellular domain of the human CD40LG gene. This model can be used for research on the disease mechanisms and treatment methods of autoimmune diseases, cardiovascular diseases, cancers, etc., as well as for CD40LG-targeted drug development.
The huCD40LG mice are a humanized model constructed by using gene editing technology to replace the endogenous extracellular domain of the mouse Cd40lg gene with the extracellular domain of the human CD40LG gene. This model can be used for research on the disease mechanisms and treatment methods of autoimmune diseases, cardiovascular diseases, cancers, etc., as well as for CD40LG-targeted drug development.
The CD40LG gene is located on the X chromosome (Xq26.3) and encodes CD40 ligand (CD40L, also known as CD154), a type II transmembrane protein mainly expressed on activated T cells, platelets, and some B cells. Under inflammatory conditions, monocytes, natural killer cells, mast cells, and basophils can also be induced to express CD40L [1-3]. This protein binds to CD40 on the surface of antigen-presenting cells (such as B cells and dendritic cells), mediating key immune functions including T cell-dependent B cell activation, immunoglobulin class switching, and germinal center formation [3]. The CD40/CD40L interaction also regulates thrombosis, inflammatory responses, hematopoiesis, and the tumor immune microenvironment. Abnormal regulation of CD40LG is associated with X-linked hyper-IgM syndrome (XHIGM), a primary immunodeficiency disease characterized by recurrent infections due to defective antibody production [4]. In addition, abnormal expression of CD40L is involved in diseases such as systemic lupus erythematosus and atherosclerosis through its pro-inflammatory effects [5-6]. Due to the important role of the CD40/CD40L interaction in immune activation, CD40/CD40L has been an important target for immunotherapy. In recent years, significant progress has been made in CD40/CD40L-targeted therapy. Various drugs have been developed, including agonistic/antagonistic monoclonal antibodies, cellular vaccines, adenoviral vectors, and protein antagonists, and have shown therapeutic potential in malignant tumors, autoimmune diseases, and allograft rejection [7].
The huCD40LG mice are a humanized model constructed by using gene editing technology to replace the endogenous extracellular domain of the mouse Cd40lg gene with the extracellular domain of the human CD40LG gene. This model can be used for research on the disease mechanisms and treatment methods of autoimmune diseases, cardiovascular diseases, cancers, etc., as well as for CD40LG-targeted drug development.
The huCD40LG mice are a humanized model constructed by using gene editing technology to replace the endogenous extracellular domain of the mouse Cd40lg gene with the extracellular domain of the human CD40LG gene. This model can be used for research on the disease mechanisms and treatment methods of autoimmune diseases, cardiovascular diseases, cancers, etc., as well as for CD40LG-targeted drug development.
huIL4/huIL4RA
제품 ID:
C001834
계통(Strain):
C57BL/6NCya
상태:
설명:
Interleukin-4 (IL-4) and its receptor, IL-4R, are pivotal regulators of immune responses and inflammation. The IL4 gene encodes the IL-4 cytokine, a multifunctional protein predominantly secreted by Th2 cells, mast cells, and eosinophils, while the IL4R gene encodes the IL-4 receptor, which is expressed on a variety of immune cells, including B cells, T cells, macrophages, and endothelial cells. IL-4 binds to IL-4R, which exists in two distinct forms: Type I (comprising IL-4Rα and the common γ-chain) and Type II (comprising IL-4Rα and IL-13Rα1) [1]. This interaction activates the JAK-STAT signaling pathway, driving Th2 cell differentiation, B cell class switching to IgE, and anti-inflammatory responses. The IL-4/IL-4R signaling axis is critically implicated in allergic diseases such as asthma, atopic dermatitis, and allergic rhinitis, as well as in parasitic infections and certain cancers [2-5]. Dysregulation of this pathway underlies various pathological conditions, positioning IL-4Rα as a promising therapeutic target. For instance, dupilumab, a monoclonal antibody targeting IL-4Rα, has been approved for the treatment of atopic dermatitis, asthma, and chronic rhinosinusitis with nasal polyps, underscoring the therapeutic potential of modulating this pathway [6-7].
The huIL4/huIL4RA mouse model is generated by crossing IL4 humanized mice (Catalog Number: C001628) with IL4R humanized mice (Catalog Number: C001629), resulting in a dual-humanized model. This model faithfully recapitulates the human IL-4/IL-4R signaling pathway, making it an invaluable tool for studying allergic diseases (e.g., asthma and atopic dermatitis), Th2 immune responses, parasitic infections, tumor immunology, and chronic inflammation. Furthermore, it serves as a robust preclinical platform for evaluating the efficacy and mechanisms of therapeutic agents targeting the IL-4/IL-4Rα pathway.
Interleukin-4 (IL-4) and its receptor, IL-4R, are pivotal regulators of immune responses and inflammation. The IL4 gene encodes the IL-4 cytokine, a multifunctional protein predominantly secreted by Th2 cells, mast cells, and eosinophils, while the IL4R gene encodes the IL-4 receptor, which is expressed on a variety of immune cells, including B cells, T cells, macrophages, and endothelial cells. IL-4 binds to IL-4R, which exists in two distinct forms: Type I (comprising IL-4Rα and the common γ-chain) and Type II (comprising IL-4Rα and IL-13Rα1) [1]. This interaction activates the JAK-STAT signaling pathway, driving Th2 cell differentiation, B cell class switching to IgE, and anti-inflammatory responses. The IL-4/IL-4R signaling axis is critically implicated in allergic diseases such as asthma, atopic dermatitis, and allergic rhinitis, as well as in parasitic infections and certain cancers [2-5]. Dysregulation of this pathway underlies various pathological conditions, positioning IL-4Rα as a promising therapeutic target. For instance, dupilumab, a monoclonal antibody targeting IL-4Rα, has been approved for the treatment of atopic dermatitis, asthma, and chronic rhinosinusitis with nasal polyps, underscoring the therapeutic potential of modulating this pathway [6-7].
The huIL4/huIL4RA mouse model is generated by crossing IL4 humanized mice (Catalog Number: C001628) with IL4R humanized mice (Catalog Number: C001629), resulting in a dual-humanized model. This model faithfully recapitulates the human IL-4/IL-4R signaling pathway, making it an invaluable tool for studying allergic diseases (e.g., asthma and atopic dermatitis), Th2 immune responses, parasitic infections, tumor immunology, and chronic inflammation. Furthermore, it serves as a robust preclinical platform for evaluating the efficacy and mechanisms of therapeutic agents targeting the IL-4/IL-4Rα pathway.
hCRBN(BALB/c)
제품 ID:
C001724
계통(Strain):
BALB/cAnCya
상태:
설명:
The CRBN gene, located on human chromosome 3, exhibits broad expression across diverse tissues, including the brain, kidney, muscle, and immune cell populations such as monocytes, macrophages, dendritic cells, and B lymphocytes [1]. This gene encodes cereblon, a protein that functions as a key substrate receptor within the CRL4-CRBN E3 ubiquitin ligase complex. This complex mediates the ubiquitination and subsequent proteasomal degradation of specific target proteins, thereby regulating crucial cellular processes encompassing protein homeostasis, ion transport, and AMPK signaling [1-2]. Notably, mutations in CRBN are implicated in autosomal recessive nonsyndromic intellectual disability [2]. Furthermore, Cereblon protein serves as a primary molecular target for targeted protein degradation (TPD/TBD) therapy by specifically modulating the enzymatic activity of the CRL4-CRBN complex and altering its substrate recognition properties, thereby enabling the selective degradation of specific transcription factors. This molecular mechanism has emerged as a critical theoretical foundation for the clinical treatment of malignant hematological diseases, such as multiple myeloma, leading to the development of diverse therapeutic modalities including molecular glues and proteolysis targeting chimeras (PROTACs) [3-5].
hCRBN(BALB/c) mice are humanized models generated by gene editing technology, in which the exon 2 to partial intron 2 of the mouse Crbn gene was replaced in situ with the Exon 2~11 of the coding sequence (CDS) of the human CRBN gene. This model can be used to study the pathological mechanisms and therapeutic methods of autosomal recessive nonsyndromic intellectual disability and multiple myeloma, and other hematological cancers, as well as the screening, development, and preclinical efficacy and safety evaluation of CRBN-based targeted protein degradation (TPD) therapies.
The CRBN gene, located on human chromosome 3, exhibits broad expression across diverse tissues, including the brain, kidney, muscle, and immune cell populations such as monocytes, macrophages, dendritic cells, and B lymphocytes [1]. This gene encodes cereblon, a protein that functions as a key substrate receptor within the CRL4-CRBN E3 ubiquitin ligase complex. This complex mediates the ubiquitination and subsequent proteasomal degradation of specific target proteins, thereby regulating crucial cellular processes encompassing protein homeostasis, ion transport, and AMPK signaling [1-2]. Notably, mutations in CRBN are implicated in autosomal recessive nonsyndromic intellectual disability [2]. Furthermore, Cereblon protein serves as a primary molecular target for targeted protein degradation (TPD/TBD) therapy by specifically modulating the enzymatic activity of the CRL4-CRBN complex and altering its substrate recognition properties, thereby enabling the selective degradation of specific transcription factors. This molecular mechanism has emerged as a critical theoretical foundation for the clinical treatment of malignant hematological diseases, such as multiple myeloma, leading to the development of diverse therapeutic modalities including molecular glues and proteolysis targeting chimeras (PROTACs) [3-5].
hCRBN(BALB/c) mice are humanized models generated by gene editing technology, in which the exon 2 to partial intron 2 of the mouse Crbn gene was replaced in situ with the Exon 2~11 of the coding sequence (CDS) of the human CRBN gene. This model can be used to study the pathological mechanisms and therapeutic methods of autosomal recessive nonsyndromic intellectual disability and multiple myeloma, and other hematological cancers, as well as the screening, development, and preclinical efficacy and safety evaluation of CRBN-based targeted protein degradation (TPD) therapies.
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