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B6-hCTLA4
製品ID :
C001413
系統:
C57BL/6NCya
状況:
説明:
Cytotoxic T-lymphocyte-associated protein 4 (CTLA4), also known as cluster of differentiation 152 (CD152), is an immunoglobulin superfamily protein encoded by the CTLA4 gene. CTLA4 is expressed by activated T cells and delivers inhibitory signals to T cells [1]. The structure of the CTLA4 protein contains a V-domain, a transmembrane domain, and a cytoplasmic tail. Different splicing patterns of CTLA4 pre-mRNA lead to the appearance of different isoforms, among which the membrane-bound isoform is linked by disulfide bonds to form homodimers, while the soluble isoform exists as a monomer. CTLA4 is homologous to CD28, which delivers T-cell activation signals. Both molecules compete for binding to the natural B7 family ligands B7-1 and B7-2 on antigen-presenting cells, but CTLA4 has a much higher affinity for binding to B7-1 and B7-2 than CD28. This results in the inhibition of T cell activation, allowing tumor cells to escape from T cell attack [2]. The gene is closely associated with the occurrence or progression of insulin-dependent diabetes mellitus, Graves' disease, Hashimoto's thyroiditis, celiac disease, systemic lupus erythematosus, thyroid-associated ophthalmopathy, and other autoimmune diseases [3].
CTLA4 is a membrane protein, with its extracellular domain serving as the receptor/ligand binding region and its intracellular domain responsible for signal transduction [4]. This strain was generated by gene editing to replace the extracellular domain of Ctla4 in mice with the humanized version, resulting in a model that expresses the extracellular domain of human CTLA4 and the intracellular domain of mouse CTLA4. This model can be used for the research of the development and screening of CTLA4-related inhibitors or antibody drugs, the evaluation of pharmacodynamics and safety, the evaluation of tumor immunotherapy, and the mechanisms of the immune system.
Cytotoxic T-lymphocyte-associated protein 4 (CTLA4), also known as cluster of differentiation 152 (CD152), is an immunoglobulin superfamily protein encoded by the CTLA4 gene. CTLA4 is expressed by activated T cells and delivers inhibitory signals to T cells [1]. The structure of the CTLA4 protein contains a V-domain, a transmembrane domain, and a cytoplasmic tail. Different splicing patterns of CTLA4 pre-mRNA lead to the appearance of different isoforms, among which the membrane-bound isoform is linked by disulfide bonds to form homodimers, while the soluble isoform exists as a monomer. CTLA4 is homologous to CD28, which delivers T-cell activation signals. Both molecules compete for binding to the natural B7 family ligands B7-1 and B7-2 on antigen-presenting cells, but CTLA4 has a much higher affinity for binding to B7-1 and B7-2 than CD28. This results in the inhibition of T cell activation, allowing tumor cells to escape from T cell attack [2]. The gene is closely associated with the occurrence or progression of insulin-dependent diabetes mellitus, Graves' disease, Hashimoto's thyroiditis, celiac disease, systemic lupus erythematosus, thyroid-associated ophthalmopathy, and other autoimmune diseases [3].
CTLA4 is a membrane protein, with its extracellular domain serving as the receptor/ligand binding region and its intracellular domain responsible for signal transduction [4]. This strain was generated by gene editing to replace the extracellular domain of Ctla4 in mice with the humanized version, resulting in a model that expresses the extracellular domain of human CTLA4 and the intracellular domain of mouse CTLA4. This model can be used for the research of the development and screening of CTLA4-related inhibitors or antibody drugs, the evaluation of pharmacodynamics and safety, the evaluation of tumor immunotherapy, and the mechanisms of the immune system.
B6-hPD-1/hCTLA4
製品ID :
I001143
系統:
C57BL/6NCya
状況:
説明:
PD-1 and CTLA-4 are checkpoint receptors that critically modulate T cell immunity. The genes PDCD1 and CTLA4 encode PD-1 and CTLA-4 respectively, with CTLA4 expression largely restricted to T cells, while PDCD1 is evident in activated T cells, B cells, and myeloid populations [1]. These transmembrane proteins function as key negative regulators of T cell activation [2]. CTLA-4 primarily operates in lymphoid tissues during early immune responses to restrain T cell proliferation, whereas PD-1 predominantly acts in peripheral tissues during the effector phase to dampen T cell activity and limit immunopathology, particularly in chronically stimulated or ‘exhausted’ T cells [2-3]. Aberrant regulation of PD-1 and CTLA-4 is implicated in the pathogenesis of cancers, including melanoma, non-small cell lung cancer, and renal cell carcinoma, as well as chronic viral infections such as hepatitis B and C [1][4]. Clinically, monoclonal antibodies targeting CTLA-4 (e.g., ipilimumab) and PD-1 (e.g., nivolumab, pembrolizumab) are established immunotherapeutic agents that enhance anti-tumor responses. By blocking these negative signaling pathways, these monoclonal antibodies restore the anti-tumor activity of T cells, significantly enhancing anti-tumor responses [1-2]. These drug applications have not only improved the treatment outcomes for various cancers but also offer new strategies for the treatment of chronic viral infections.
B6-hPD-1/hCTLA4 mouse is a dual humanized model of PD1 and CTLA4 constructed by humanizing the mouse Pdcd1 gene based on the CTLA4 humanized mouse model (Catalog No. C001413), due to the fact that the mouse Pdcd1 gene and Ctla4 gene are on the same chromosome. These mice express human CTLA4 and PDCD1 genomic sequences under the control of mouse promoters. This model is capable of reproducing the human PD-1/CTLA4 signaling pathway and is a valuable tool for studying cancers and chronic viral infections. Furthermore, this model provides a powerful preclinical research platform for evaluating the efficacy and mechanism of therapeutic drugs targeting the PD-1/CTLA4 signaling pathway.
PD-1 and CTLA-4 are checkpoint receptors that critically modulate T cell immunity. The genes PDCD1 and CTLA4 encode PD-1 and CTLA-4 respectively, with CTLA4 expression largely restricted to T cells, while PDCD1 is evident in activated T cells, B cells, and myeloid populations [1]. These transmembrane proteins function as key negative regulators of T cell activation [2]. CTLA-4 primarily operates in lymphoid tissues during early immune responses to restrain T cell proliferation, whereas PD-1 predominantly acts in peripheral tissues during the effector phase to dampen T cell activity and limit immunopathology, particularly in chronically stimulated or ‘exhausted’ T cells [2-3]. Aberrant regulation of PD-1 and CTLA-4 is implicated in the pathogenesis of cancers, including melanoma, non-small cell lung cancer, and renal cell carcinoma, as well as chronic viral infections such as hepatitis B and C [1][4]. Clinically, monoclonal antibodies targeting CTLA-4 (e.g., ipilimumab) and PD-1 (e.g., nivolumab, pembrolizumab) are established immunotherapeutic agents that enhance anti-tumor responses. By blocking these negative signaling pathways, these monoclonal antibodies restore the anti-tumor activity of T cells, significantly enhancing anti-tumor responses [1-2]. These drug applications have not only improved the treatment outcomes for various cancers but also offer new strategies for the treatment of chronic viral infections.
B6-hPD-1/hCTLA4 mouse is a dual humanized model of PD1 and CTLA4 constructed by humanizing the mouse Pdcd1 gene based on the CTLA4 humanized mouse model (Catalog No. C001413), due to the fact that the mouse Pdcd1 gene and Ctla4 gene are on the same chromosome. These mice express human CTLA4 and PDCD1 genomic sequences under the control of mouse promoters. This model is capable of reproducing the human PD-1/CTLA4 signaling pathway and is a valuable tool for studying cancers and chronic viral infections. Furthermore, this model provides a powerful preclinical research platform for evaluating the efficacy and mechanism of therapeutic drugs targeting the PD-1/CTLA4 signaling pathway.
FVB-Abcb1a & Abcb1b DKO (Mdr1a/b KO)
製品ID :
C001493
系統:
FVB/NJCya
状況:
説明:
P-glycoprotein (P-gp), also known as multidrug resistance protein 1 (MDR1), is an ATP-binding cassette transporter that acts as a biological barrier by expelling toxins and foreign substances from cells. P-gp is capable of transporting many structurally and functionally different compounds out of cells [1]. However, the mechanism of MDR1 also prevents the uptake of many cancer treatment drugs by cells, leading to multidrug resistance (MDR) [2]. In normal organisms, MDR1’s distribution in the blood-brain barrier and blood-placenta barrier prevents exogenous drugs and toxins from entering the central nervous system and placenta of the organism, thereby protecting the organism and enabling it to perform normal physiological functions. In pathological conditions, however, the MDR1 in the blood-brain barrier prevents drugs from entering the central nervous system, and in tumor cells, leads to the development of MDR. The evolution of MDR remains one of the major obstacles to controlling or curing cancer [3-4].
In humans, the MDR1 protein is encoded by the ABCB1 gene. In mice, two closely located genes, Abcb1a and Abcb1b, encode the MDR1a and MDR1b subtypes of this protein. Mouse MDR1a and MDR1b have 80% homology with human MDR1. MDR1a and MDR1b have the same function as human MDR1 protein in resisting anticancer drugs. Although mouse MDR1a and MDR1b proteins are distributed in different tissues of the body, their overall distribution is consistent with that of human MDR1 protein [5-6]. In summary, the distribution and function of mouse MDR1a and MDR1b are consistent with those of human MDR1.
This strain is an MDR1 knockout model, in which the human ABCB1 gene’s homologous genes, Abcb1a and Abcb1b, were knocked out in mice using gene editing technology. This model lacks the expression of MDR1 protein and can be used for research in areas such as blood-brain barrier permeability-related diseases and multidrug resistance of anti-tumor drugs.
P-glycoprotein (P-gp), also known as multidrug resistance protein 1 (MDR1), is an ATP-binding cassette transporter that acts as a biological barrier by expelling toxins and foreign substances from cells. P-gp is capable of transporting many structurally and functionally different compounds out of cells [1]. However, the mechanism of MDR1 also prevents the uptake of many cancer treatment drugs by cells, leading to multidrug resistance (MDR) [2]. In normal organisms, MDR1’s distribution in the blood-brain barrier and blood-placenta barrier prevents exogenous drugs and toxins from entering the central nervous system and placenta of the organism, thereby protecting the organism and enabling it to perform normal physiological functions. In pathological conditions, however, the MDR1 in the blood-brain barrier prevents drugs from entering the central nervous system, and in tumor cells, leads to the development of MDR. The evolution of MDR remains one of the major obstacles to controlling or curing cancer [3-4].
In humans, the MDR1 protein is encoded by the ABCB1 gene. In mice, two closely located genes, Abcb1a and Abcb1b, encode the MDR1a and MDR1b subtypes of this protein. Mouse MDR1a and MDR1b have 80% homology with human MDR1. MDR1a and MDR1b have the same function as human MDR1 protein in resisting anticancer drugs. Although mouse MDR1a and MDR1b proteins are distributed in different tissues of the body, their overall distribution is consistent with that of human MDR1 protein [5-6]. In summary, the distribution and function of mouse MDR1a and MDR1b are consistent with those of human MDR1.
This strain is an MDR1 knockout model, in which the human ABCB1 gene’s homologous genes, Abcb1a and Abcb1b, were knocked out in mice using gene editing technology. This model lacks the expression of MDR1 protein and can be used for research in areas such as blood-brain barrier permeability-related diseases and multidrug resistance of anti-tumor drugs.
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