필터
“718” 에 대한 검색 결과 8 건
정렬 기준:
알파벳순 (A-Z)
베스트셀러
huC3
제품 ID:
C001955
계통(Strain):
C57BL/6JCya
상태:
설명:
Complement component C3 plays a central role in activating the complement system and is the most abundant complement protein in human plasma, primarily synthesized in the liver. As part of the innate immune system, the complement system is activated during tissue damage and pathogen invasion, playing a crucial role in the inflammatory response, host homeostasis, and pathogen defense. The complement cascade is activated through the classical pathway, alternative pathway, and lectin pathway, all of which generate C3 convertase, which cleaves C3 into C3a and C3b. C3a is a potent anaphylatoxin with pro-inflammatory activity, while C3b is a regulator that induces C5 cleavage, thereby participating in the dissolution and clearance of immune complexes. Mutations in this gene are associated with atypical hemolytic uremic syndrome (aHUS) and age-related macular degeneration (AMD). Deficiencies in C3 and C3-derived peptides can lead to autoimmune diseases (such as rheumatoid arthritis, systemic lupus erythematosus, and vasculitis) and make individuals susceptible to recurrent respiratory infections and infections caused by encapsulated organisms. Conversely, excessive activation of C3 and related complement components is associated with kidney diseases (immune complex glomerulonephritis, hemolytic uremic syndrome, lupus nephritis, membranous nephropathy, and immune-mediated nephropathy) [1-2].
The huC3 mouse is a mouse C3 humanized model created by replacing the mouse C3 gene with the human C3 gene using gene-editing technology. The humanized regions include the 5’UTR and 3’UTR. Under natural breeding conditions, homozygous huC3 mice exhibit mortality around 10 weeks of age, and it has been observed that heterozygous mice also experience mortality. Additionally, based on the innovative TurboKnockout technology combined with BAC recombination developed by Cyagen Biosciences, customized services are available for different mutations to meet the experimental needs of researchers studying complement-mediated diseases.
Complement component C3 plays a central role in activating the complement system and is the most abundant complement protein in human plasma, primarily synthesized in the liver. As part of the innate immune system, the complement system is activated during tissue damage and pathogen invasion, playing a crucial role in the inflammatory response, host homeostasis, and pathogen defense. The complement cascade is activated through the classical pathway, alternative pathway, and lectin pathway, all of which generate C3 convertase, which cleaves C3 into C3a and C3b. C3a is a potent anaphylatoxin with pro-inflammatory activity, while C3b is a regulator that induces C5 cleavage, thereby participating in the dissolution and clearance of immune complexes. Mutations in this gene are associated with atypical hemolytic uremic syndrome (aHUS) and age-related macular degeneration (AMD). Deficiencies in C3 and C3-derived peptides can lead to autoimmune diseases (such as rheumatoid arthritis, systemic lupus erythematosus, and vasculitis) and make individuals susceptible to recurrent respiratory infections and infections caused by encapsulated organisms. Conversely, excessive activation of C3 and related complement components is associated with kidney diseases (immune complex glomerulonephritis, hemolytic uremic syndrome, lupus nephritis, membranous nephropathy, and immune-mediated nephropathy) [1-2].
The huC3 mouse is a mouse C3 humanized model created by replacing the mouse C3 gene with the human C3 gene using gene-editing technology. The humanized regions include the 5’UTR and 3’UTR. Under natural breeding conditions, homozygous huC3 mice exhibit mortality around 10 weeks of age, and it has been observed that heterozygous mice also experience mortality. Additionally, based on the innovative TurboKnockout technology combined with BAC recombination developed by Cyagen Biosciences, customized services are available for different mutations to meet the experimental needs of researchers studying complement-mediated diseases.
B6-huC3*R102G
제품 ID:
C001896
계통(Strain):
C57BL/6JCya
상태:
설명:
Complement component C3 plays a central role in activating the complement system and is the most abundant complement protein in human plasma, primarily synthesized in the liver. As part of the innate immune system, the complement system is activated during tissue damage and pathogen invasion, playing a crucial role in the inflammatory response, host homeostasis, and pathogen defense. The complement cascade is activated through the classical pathway, alternative pathway, and lectin pathway, all of which generate C3 convertase, which cleaves C3 into C3a and C3b. C3a is a potent anaphylatoxin with pro-inflammatory activity, while C3b is a regulator that induces C5 cleavage, thereby participating in the dissolution and clearance of immune complexes. Mutations in this gene are associated with atypical hemolytic uremic syndrome (aHUS) and age-related macular degeneration (AMD). Deficiencies in C3 and C3-derived peptides can lead to autoimmune diseases (such as rheumatoid arthritis, systemic lupus erythematosus, and vasculitis) and make individuals susceptible to recurrent respiratory infections and infections caused by encapsulated organisms. Conversely, excessive activation of C3 and related complement components is associated with kidney diseases (immune complex glomerulonephritis, hemolytic uremic syndrome, lupus nephritis, membranous nephropathy, and immune-mediated nephropathy) [1-2]. Specifically, the C3*R102G mutation involves a substitution of the amino acid arginine (R) with glycine (G) at position 102 of the mature C3 protein, often leading to a gain-of-function that results in the protein being more susceptible to cleavage and thus causing uncontrolled complement activation [3].
The B6-huC3*R102G mouse is a humanized disease model constructed by gene-editing technology. The sequences from upstream of exon 1 to the TGA stop codon of mouse C3 were replaced with the sequences from upstream of exon 1 to downstream of exon 41 of human C3. The p.R102G (CGC to GGC) mutation was introduced into human C3 exon 3. This model is suitable for the mechanistic study of immune-related diseases caused by uncontrolled activation of the complement system (such as age-related macular degeneration (AMD), etc.) and the development of therapies targeting C3 R102G.
Complement component C3 plays a central role in activating the complement system and is the most abundant complement protein in human plasma, primarily synthesized in the liver. As part of the innate immune system, the complement system is activated during tissue damage and pathogen invasion, playing a crucial role in the inflammatory response, host homeostasis, and pathogen defense. The complement cascade is activated through the classical pathway, alternative pathway, and lectin pathway, all of which generate C3 convertase, which cleaves C3 into C3a and C3b. C3a is a potent anaphylatoxin with pro-inflammatory activity, while C3b is a regulator that induces C5 cleavage, thereby participating in the dissolution and clearance of immune complexes. Mutations in this gene are associated with atypical hemolytic uremic syndrome (aHUS) and age-related macular degeneration (AMD). Deficiencies in C3 and C3-derived peptides can lead to autoimmune diseases (such as rheumatoid arthritis, systemic lupus erythematosus, and vasculitis) and make individuals susceptible to recurrent respiratory infections and infections caused by encapsulated organisms. Conversely, excessive activation of C3 and related complement components is associated with kidney diseases (immune complex glomerulonephritis, hemolytic uremic syndrome, lupus nephritis, membranous nephropathy, and immune-mediated nephropathy) [1-2]. Specifically, the C3*R102G mutation involves a substitution of the amino acid arginine (R) with glycine (G) at position 102 of the mature C3 protein, often leading to a gain-of-function that results in the protein being more susceptible to cleavage and thus causing uncontrolled complement activation [3].
The B6-huC3*R102G mouse is a humanized disease model constructed by gene-editing technology. The sequences from upstream of exon 1 to the TGA stop codon of mouse C3 were replaced with the sequences from upstream of exon 1 to downstream of exon 41 of human C3. The p.R102G (CGC to GGC) mutation was introduced into human C3 exon 3. This model is suitable for the mechanistic study of immune-related diseases caused by uncontrolled activation of the complement system (such as age-related macular degeneration (AMD), etc.) and the development of therapies targeting C3 R102G.
huC3/huC5
제품 ID:
C002009
계통(Strain):
C57BL/6JCya
상태:
hTFRC/huC3
제품 ID:
C001608
계통(Strain):
C57BL/6JCya;C57BL/6NCya
상태:
설명:
Complement component C3 plays a central role in activating the complement system and is the most abundant complement protein in human plasma, primarily synthesized in the liver. As part of the innate immune system, the complement system is activated during tissue damage and pathogen invasion, playing a crucial role in the inflammatory response, host homeostasis, and pathogen defense. The complement cascade is activated through the classical pathway, alternative pathway, and lectin pathway, all of which generate C3 convertase, which cleaves C3 into C3a and C3b. C3a is a potent anaphylatoxin with pro-inflammatory activity, while C3b is a regulator that induces C5 cleavage, thereby participating in the dissolution and clearance of immune complexes. Mutations in this gene are associated with atypical hemolytic uremic syndrome (aHUS) and age-related macular degeneration (AMD). Deficiencies in C3 and C3-derived peptides can lead to autoimmune diseases (such as rheumatoid arthritis, systemic lupus erythematosus, and vasculitis) and make individuals susceptible to recurrent respiratory infections and infections caused by encapsulated organisms. Conversely, excessive activation of C3 and related complement components is associated with kidney diseases (immune complex glomerulonephritis, hemolytic uremic syndrome, lupus nephritis, membranous nephropathy, and immune-mediated nephropathy) [1-2].
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 [3]. 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 [4]. 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 [3]. 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 [5]. 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 [6-7]. 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 hTFRC/huC3 mouse model is a humanized model obtained by breeding huC3 mice (Catalog No.: C001955) with hTFRC mice (Catalog No.: C001584). This model can be used for research on complement-mediated diseases, iron metabolism disorders, neurodegenerative diseases, and tumor development, aiding in studying C3/TFRC-targeted drugs.
Complement component C3 plays a central role in activating the complement system and is the most abundant complement protein in human plasma, primarily synthesized in the liver. As part of the innate immune system, the complement system is activated during tissue damage and pathogen invasion, playing a crucial role in the inflammatory response, host homeostasis, and pathogen defense. The complement cascade is activated through the classical pathway, alternative pathway, and lectin pathway, all of which generate C3 convertase, which cleaves C3 into C3a and C3b. C3a is a potent anaphylatoxin with pro-inflammatory activity, while C3b is a regulator that induces C5 cleavage, thereby participating in the dissolution and clearance of immune complexes. Mutations in this gene are associated with atypical hemolytic uremic syndrome (aHUS) and age-related macular degeneration (AMD). Deficiencies in C3 and C3-derived peptides can lead to autoimmune diseases (such as rheumatoid arthritis, systemic lupus erythematosus, and vasculitis) and make individuals susceptible to recurrent respiratory infections and infections caused by encapsulated organisms. Conversely, excessive activation of C3 and related complement components is associated with kidney diseases (immune complex glomerulonephritis, hemolytic uremic syndrome, lupus nephritis, membranous nephropathy, and immune-mediated nephropathy) [1-2].
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 [3]. 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 [4]. 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 [3]. 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 [5]. 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 [6-7]. 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 hTFRC/huC3 mouse model is a humanized model obtained by breeding huC3 mice (Catalog No.: C001955) with hTFRC mice (Catalog No.: C001584). This model can be used for research on complement-mediated diseases, iron metabolism disorders, neurodegenerative diseases, and tumor development, aiding in studying C3/TFRC-targeted drugs.
B6-hTROP2 (hTACSTD2)
제품 ID:
C001718
계통(Strain):
C57BL/6NCya
상태:
설명:
Tumor-Associated Calcium Signal Transducer 2, encoded by the TACSTD2 gene, is a prominent type I transmembrane glycoprotein critically involved in mediating diverse cellular processes [1]. Acting primarily as a cell surface receptor, TROP2 transduces extracellular signals to initiate intracellular calcium release, thereby influencing key cellular behaviors including proliferation, adhesion, migration, and differentiation. While its expression is notably high during embryonic development, particularly in fetal tissues and trophoblasts, and maintained at lower levels in some normal adult epithelial lineages, aberrant and significant upregulation of TROP2 is a hallmark feature across a wide spectrum of human carcinomas [2]. This dysregulated expression contributes substantially to tumor initiation, progression, and metastasis by modulating various signaling pathways [3]. Beyond its role in oncogenesis, germline mutations in TACSTD2 are identified as the underlying cause of the rare autosomal recessive disorder, gelatinous drop-like corneal dystrophy [4]. The distinct expression profile of TROP2, with its high levels in numerous solid tumors contrasted by limited expression in most healthy adult tissues, positions it as a compelling and clinically relevant target for developing targeted therapies, notably antibody-drug conjugates, aimed at treating TROP2-expressing cancers [3].
The B6-hTROP2 (hTACSTD2) mouse is a humanized model constructed by replacing the signal peptide and extracellular domain of the mouse Tacstd2 with the corresponding signal peptide and extracellular domain from the human TACSTD2 gene. The B6-hTROP2 (hTACSTD2) mice can be used for studies on pathogenesis of various cancers, as well as for TACSTD2-targeted drug development.
Tumor-Associated Calcium Signal Transducer 2, encoded by the TACSTD2 gene, is a prominent type I transmembrane glycoprotein critically involved in mediating diverse cellular processes [1]. Acting primarily as a cell surface receptor, TROP2 transduces extracellular signals to initiate intracellular calcium release, thereby influencing key cellular behaviors including proliferation, adhesion, migration, and differentiation. While its expression is notably high during embryonic development, particularly in fetal tissues and trophoblasts, and maintained at lower levels in some normal adult epithelial lineages, aberrant and significant upregulation of TROP2 is a hallmark feature across a wide spectrum of human carcinomas [2]. This dysregulated expression contributes substantially to tumor initiation, progression, and metastasis by modulating various signaling pathways [3]. Beyond its role in oncogenesis, germline mutations in TACSTD2 are identified as the underlying cause of the rare autosomal recessive disorder, gelatinous drop-like corneal dystrophy [4]. The distinct expression profile of TROP2, with its high levels in numerous solid tumors contrasted by limited expression in most healthy adult tissues, positions it as a compelling and clinically relevant target for developing targeted therapies, notably antibody-drug conjugates, aimed at treating TROP2-expressing cancers [3].
The B6-hTROP2 (hTACSTD2) mouse is a humanized model constructed by replacing the signal peptide and extracellular domain of the mouse Tacstd2 with the corresponding signal peptide and extracellular domain from the human TACSTD2 gene. The B6-hTROP2 (hTACSTD2) mice can be used for studies on pathogenesis of various cancers, as well as for TACSTD2-targeted drug development.
Braf-KO
제품 ID:
S-KO-00718
계통(Strain):
C57BL/6JCya
상태:
설명:
Braf is located on chromosome 6 of mice. Nuclease Technology was used to design sgRNA; Braf knockout mice were obtained by applying high-throughput electroporation of fertilized eggs. After sexual maturity, sperm were collected for cryopreservation.
Braf is located on chromosome 6 of mice. Nuclease Technology was used to design sgRNA; Braf knockout mice were obtained by applying high-throughput electroporation of fertilized eggs. After sexual maturity, sperm were collected for cryopreservation.
Cdca2-flox
제품 ID:
S-CKO-00718
계통(Strain):
C57BL/6JCya
상태:
설명:
Cdca2 is located on chromosome 14 of mice. SgRNA and ssDNA will be designed using Nuclease Technology; Cdca2 conditional knockout mice will be obtained by high-throughput electroporation of fertilized eggs. After sexual maturity, sperm will be collected for cryopreservation.
Cdca2 is located on chromosome 14 of mice. SgRNA and ssDNA will be designed using Nuclease Technology; Cdca2 conditional knockout mice will be obtained by high-throughput electroporation of fertilized eggs. After sexual maturity, sperm will be collected for cryopreservation.
B6-huCFTR*c.3718-2477C>T
제품 ID:
C001880
계통(Strain):
C57BL/6NCya
상태:
설명:
The cystic fibrosis transmembrane conductance regulator (CFTR) is a critical protein that maintains the salt and water balance across various human organs, including the lungs, pancreas, and sweat glands. The primary function of CFTR is to act as a chloride channel, regulating the transport of chloride and bicarbonate ions across epithelial cell membranes, thereby maintaining tissue fluid balance and pH. This process is ATP-dependent and also modulates the activity of other ion channels and transport proteins [1-2]. Mutations in the CFTR gene can lead to chloride channel dysfunction, resulting in various diseases, with cystic fibrosis (CF) being the most common. CF is the most prevalent lethal genetic disease among Caucasians, with an incidence of approximately 1/2,500 to 1/1,800, and about 90,000 cases globally [3-4]. The disease is characterized by thickened mucus in the lungs, frequent respiratory infections, pancreatic insufficiency, and male infertility, typically due to vas deferens obstruction. The c.3718-2477C>T mutation is a relatively rare pathogenic cause of Cystic Fibrosis (CF). As a deep intronic variant, c.3718-2477C>T is classified as a splicing mutation, meaning its primary effect is likely to disrupt the normal process of mRNA splicing (the removal of non-coding introns and joining of coding exons) after transcription. This disruption can lead to a faulty or absent CFTR protein, ultimately resulting in the clinical manifestations of CF. Current treatments for CF mainly focus on CFTR modulators to restore the function of the mutated CFTR protein. CFTR modulators are classified into potentiators (which enhance CFTR function) and correctors (which assist in the proper folding and trafficking of CFTR to the cell membrane). Representative drugs include Ivacaftor, Lumacaftor, and triple-combination CFTR modulating therapy Elexacaftor-Tezacaftor-Ivacaftor [5].
B6-huCFTR*c.3718-2477C>T mice were developed by introducing the c.3718-2477C>T mutation into the CFTR-humanized mouse model (Catalog Number: C001964), creating a humanized disease model. It is suitable for research into CF mechanisms and the development of therapies targeting the CFTR c.3718-2477C>T mutation. This strain requires feeding with intestinal cleansers to maintain survival. In addition, based on the independently developed TurboKnockout fusion BAC recombination technology, Cyagen can also generate hot mutation models based on the CFTR-humanized strain and provide customized services for specific mutations to meet the experimental needs in pharmacology and other fields.
The cystic fibrosis transmembrane conductance regulator (CFTR) is a critical protein that maintains the salt and water balance across various human organs, including the lungs, pancreas, and sweat glands. The primary function of CFTR is to act as a chloride channel, regulating the transport of chloride and bicarbonate ions across epithelial cell membranes, thereby maintaining tissue fluid balance and pH. This process is ATP-dependent and also modulates the activity of other ion channels and transport proteins [1-2]. Mutations in the CFTR gene can lead to chloride channel dysfunction, resulting in various diseases, with cystic fibrosis (CF) being the most common. CF is the most prevalent lethal genetic disease among Caucasians, with an incidence of approximately 1/2,500 to 1/1,800, and about 90,000 cases globally [3-4]. The disease is characterized by thickened mucus in the lungs, frequent respiratory infections, pancreatic insufficiency, and male infertility, typically due to vas deferens obstruction. The c.3718-2477C>T mutation is a relatively rare pathogenic cause of Cystic Fibrosis (CF). As a deep intronic variant, c.3718-2477C>T is classified as a splicing mutation, meaning its primary effect is likely to disrupt the normal process of mRNA splicing (the removal of non-coding introns and joining of coding exons) after transcription. This disruption can lead to a faulty or absent CFTR protein, ultimately resulting in the clinical manifestations of CF. Current treatments for CF mainly focus on CFTR modulators to restore the function of the mutated CFTR protein. CFTR modulators are classified into potentiators (which enhance CFTR function) and correctors (which assist in the proper folding and trafficking of CFTR to the cell membrane). Representative drugs include Ivacaftor, Lumacaftor, and triple-combination CFTR modulating therapy Elexacaftor-Tezacaftor-Ivacaftor [5].
B6-huCFTR*c.3718-2477C>T mice were developed by introducing the c.3718-2477C>T mutation into the CFTR-humanized mouse model (Catalog Number: C001964), creating a humanized disease model. It is suitable for research into CF mechanisms and the development of therapies targeting the CFTR c.3718-2477C>T mutation. This strain requires feeding with intestinal cleansers to maintain survival. In addition, based on the independently developed TurboKnockout fusion BAC recombination technology, Cyagen can also generate hot mutation models based on the CFTR-humanized strain and provide customized services for specific mutations to meet the experimental needs in pharmacology and other fields.
Items: 1 to 8 of 8
1