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huCD7
製品ID :
C002067
系統:
C57BL/6NCya
状況:
説明:
The CD7 gene encodes a transmembrane glycoprotein belonging to the immunoglobulin superfamily (IgSF). As an important co-receptor on the T cell surface, CD7 plays a critical regulatory role in T cell activation, proliferation, and signal transduction. CD7 is primarily expressed on T cells and natural killer (NK) cells, with expression observed from the early stages of thymocyte development through to mature T cells. It is also expressed in some hematopoietic progenitor cells, but its expression level is relatively low in most normal non-T/NK cell tissues [1]. Aberrant expression or dysregulated signaling of CD7 is closely associated with various diseases. As a key therapeutic target in immunotherapy, CD7 is highly expressed in T cell acute lymphoblastic leukemia (T-ALL) and T cell lymphomas, making it a critical molecule for targeting T cell malignancies [1]. In addition, CD7 is associated with systemic sclerosis (SSc) and graft-versus-host disease (GvHD) [2-3]. Currently, multiple therapeutic strategies targeting CD7 are under development, including anti-CD7 CAR-T cell therapy, CD7 CAR-iNK cells, and bispecific CAR-T therapies targeting CD7, which have demonstrated promising preclinical and early clinical potential in relapsed/refractory T-ALL and T cell lymphomas [4-5].
The huCD7 mouse is a humanized model generated using gene editing technology, in which the endogenous signal peptide and extracellular domain sequence of the mouse Cd7 gene were replaced with the corresponding sequence of the human CD7 gene. This model is suitable for the in vivo efficacy and safety evaluation of antibody drugs and CAR-T cell therapies targeting human CD7, as well as for studies on T cell development and function. It also serves as an ideal platform for investigating the functional mechanisms of CD7+ T cells in T cell acute lymphoblastic leukemia (T-ALL), T cell lymphomas, and autoimmune diseases such as systemic sclerosis (SSc).
The CD7 gene encodes a transmembrane glycoprotein belonging to the immunoglobulin superfamily (IgSF). As an important co-receptor on the T cell surface, CD7 plays a critical regulatory role in T cell activation, proliferation, and signal transduction. CD7 is primarily expressed on T cells and natural killer (NK) cells, with expression observed from the early stages of thymocyte development through to mature T cells. It is also expressed in some hematopoietic progenitor cells, but its expression level is relatively low in most normal non-T/NK cell tissues [1]. Aberrant expression or dysregulated signaling of CD7 is closely associated with various diseases. As a key therapeutic target in immunotherapy, CD7 is highly expressed in T cell acute lymphoblastic leukemia (T-ALL) and T cell lymphomas, making it a critical molecule for targeting T cell malignancies [1]. In addition, CD7 is associated with systemic sclerosis (SSc) and graft-versus-host disease (GvHD) [2-3]. Currently, multiple therapeutic strategies targeting CD7 are under development, including anti-CD7 CAR-T cell therapy, CD7 CAR-iNK cells, and bispecific CAR-T therapies targeting CD7, which have demonstrated promising preclinical and early clinical potential in relapsed/refractory T-ALL and T cell lymphomas [4-5].
The huCD7 mouse is a humanized model generated using gene editing technology, in which the endogenous signal peptide and extracellular domain sequence of the mouse Cd7 gene were replaced with the corresponding sequence of the human CD7 gene. This model is suitable for the in vivo efficacy and safety evaluation of antibody drugs and CAR-T cell therapies targeting human CD7, as well as for studies on T cell development and function. It also serves as an ideal platform for investigating the functional mechanisms of CD7+ T cells in T cell acute lymphoblastic leukemia (T-ALL), T cell lymphomas, and autoimmune diseases such as systemic sclerosis (SSc).
B6-huTFRC/htau*P301L
製品ID :
C001924
系統:
C57BL/6Cya
状況:
説明:
The Transferrin receptor (TFRC) gene encodes Transferrin Receptor 1 (TFR1), a protein that is expressed at low levels in most normal cells but shows increased expression in highly proliferative cells, such as basal epidermal cells, intestinal epithelium, and certain activated immune cells. Brain capillary endothelial cells, which constitute the blood-brain barrier (BBB), also express this receptor at high levels [1]. TFR1 plays a critical role in maintaining iron metabolism and homeostasis by facilitating receptor-mediated endocytosis of iron-bound transferrin (Tf) via Tf cycling, thereby promoting iron uptake [2]. Cellular iron deficiency can lead to apoptosis, while cellular transformation requires substantial iron to sustain proliferation, with iron overload contributing to tumor progression. The high expression of TFR1 in many tumors makes it a potential tumor marker, offering a target for therapies to inhibit tumor growth and metastasis [1]. Moreover, TFR1 is implicated in anemia and iron metabolism disorders. Studies have shown that elevated TFR1 expression in cardiomyocytes is associated with exacerbated inflammation in myocarditis patients [3]. As a target for antibody-mediated cancer therapy, TFR1 can be leveraged through two approaches: one involves the use of antibodies conjugated to anti-cancer drugs, which are indirectly internalized via receptor-mediated endocytosis; the other employs antibodies that directly disrupt receptor function or induce Fc effector functions such as antibody-dependent cellular cytotoxicity (ADCC), antibody-dependent cellular phagocytosis (ADCP), or complement-dependent cytotoxicity (CDC). Various clinical drugs targeting TFR1 are currently under development, including antisense oligonucleotides (ASOs), antibody-drug conjugates (ADCs), and antibody-oligonucleotide conjugates, applicable to diseases such as cancer, anemia, and neurodegenerative disorders. Research indicates that enhancing antibody transport across the blood-brain barrier via TFR1, by forming specific bispecific antibodies with anti-β-amyloid antibodies, can improve therapeutic outcomes in Alzheimer's patients [4-5]. As research progresses, TFR1 is expected to become an effective clinical target for multiple diseases and a synergistic target for drug delivery across the blood-brain barrier (BBB).
The tau protein, a microtubule-associated protein encoded by MAPT, is primarily localized to neuronal axons and plays a critical role in microtubule stability and assembly. By binding to microtubules, the tau protein helps to maintain neuronal cell shape. Mutations in MAPT can promote tau aggregation, leading to pathological tau protein accumulation and death of glutamatergic cortical neurons [6]. Additionally, certain MAPT mutations can affect pre-mRNA exon splicing, altering the ratio of 3R to 4R tau protein isoforms and increasing the relative production of 4R-tau protein, which is more prone to fibril formation [7]. Common mutations include P301L, P301S, and Intron10+3 G>A [8].
The B6-huTFRC/htau*P301L mouse is a humanized disease model obtained by mating B6-huTFRC mice (catalog number: C001860) with B6-htau*P301L mice (catalog number: C001835). This model can be used for the research of Alzheimer's disease (AD), frontotemporal dementia (FTD), neurodegenerative diseases, and tumorigenesis and development, as well as the development of TFRC/MAPT-targeted drugs.
The Transferrin receptor (TFRC) gene encodes Transferrin Receptor 1 (TFR1), a protein that is expressed at low levels in most normal cells but shows increased expression in highly proliferative cells, such as basal epidermal cells, intestinal epithelium, and certain activated immune cells. Brain capillary endothelial cells, which constitute the blood-brain barrier (BBB), also express this receptor at high levels [1]. TFR1 plays a critical role in maintaining iron metabolism and homeostasis by facilitating receptor-mediated endocytosis of iron-bound transferrin (Tf) via Tf cycling, thereby promoting iron uptake [2]. Cellular iron deficiency can lead to apoptosis, while cellular transformation requires substantial iron to sustain proliferation, with iron overload contributing to tumor progression. The high expression of TFR1 in many tumors makes it a potential tumor marker, offering a target for therapies to inhibit tumor growth and metastasis [1]. Moreover, TFR1 is implicated in anemia and iron metabolism disorders. Studies have shown that elevated TFR1 expression in cardiomyocytes is associated with exacerbated inflammation in myocarditis patients [3]. As a target for antibody-mediated cancer therapy, TFR1 can be leveraged through two approaches: one involves the use of antibodies conjugated to anti-cancer drugs, which are indirectly internalized via receptor-mediated endocytosis; the other employs antibodies that directly disrupt receptor function or induce Fc effector functions such as antibody-dependent cellular cytotoxicity (ADCC), antibody-dependent cellular phagocytosis (ADCP), or complement-dependent cytotoxicity (CDC). Various clinical drugs targeting TFR1 are currently under development, including antisense oligonucleotides (ASOs), antibody-drug conjugates (ADCs), and antibody-oligonucleotide conjugates, applicable to diseases such as cancer, anemia, and neurodegenerative disorders. Research indicates that enhancing antibody transport across the blood-brain barrier via TFR1, by forming specific bispecific antibodies with anti-β-amyloid antibodies, can improve therapeutic outcomes in Alzheimer's patients [4-5]. As research progresses, TFR1 is expected to become an effective clinical target for multiple diseases and a synergistic target for drug delivery across the blood-brain barrier (BBB).
The tau protein, a microtubule-associated protein encoded by MAPT, is primarily localized to neuronal axons and plays a critical role in microtubule stability and assembly. By binding to microtubules, the tau protein helps to maintain neuronal cell shape. Mutations in MAPT can promote tau aggregation, leading to pathological tau protein accumulation and death of glutamatergic cortical neurons [6]. Additionally, certain MAPT mutations can affect pre-mRNA exon splicing, altering the ratio of 3R to 4R tau protein isoforms and increasing the relative production of 4R-tau protein, which is more prone to fibril formation [7]. Common mutations include P301L, P301S, and Intron10+3 G>A [8].
The B6-huTFRC/htau*P301L mouse is a humanized disease model obtained by mating B6-huTFRC mice (catalog number: C001860) with B6-htau*P301L mice (catalog number: C001835). This model can be used for the research of Alzheimer's disease (AD), frontotemporal dementia (FTD), neurodegenerative diseases, and tumorigenesis and development, as well as the development of TFRC/MAPT-targeted drugs.
Add2-KO
製品ID :
S-KO-00924
系統:
C57BL/6JCya
状況:
説明:
Add2 is located on chromosome 6 of mice. Nuclease Technology will be used to design sgRNA; Add2 knockout mice will be obtained by applying high-throughput electroporation of fertilized eggs. After sexual maturity, sperm were collected for cryopreservation.
Add2 is located on chromosome 6 of mice. Nuclease Technology will be used to design sgRNA; Add2 knockout mice will be obtained by applying high-throughput electroporation of fertilized eggs. After sexual maturity, sperm were collected for cryopreservation.
Tas2r116-flox
製品ID :
S-CKO-00924
系統:
C57BL/6JCya
状況:
説明:
Tas2r116 is located on chromosome 6 of mice. SgRNA and ssDNA will be designed using Nuclease Technology; Tas2r116 conditional knockout mice will be obtained by high-throughput electroporation of fertilized eggs. After sexual maturity, sperm will be collected for cryopreservation.
Tas2r116 is located on chromosome 6 of mice. SgRNA and ssDNA will be designed using Nuclease Technology; Tas2r116 conditional knockout mice will be obtained by high-throughput electroporation of fertilized eggs. After sexual maturity, sperm will be collected for cryopreservation.
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