目录号 | 产品详情 | 靶点 | |
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T3158 | Adrenergic Receptor Monoamine Oxidase Imidazoline Receptor | ||
Harmane (Loturine) 是一种在咖啡和烟草烟雾中发现的 β-咔啉生物碱,是有效的神经毒素,可引起严重的动作震颤和精神病学表现。它还是选择性的单胺氧化酶抑制剂,具有致突变作用,对 MAO A/B 的 IC50值分别为 0.5 和 5 μM。 | |||
T6410 | Retinoid Receptor Autophagy | ||
Bexarotene (LGD1069) 是一种高亲和力的选择性类视黄醇 X 受体 (RXR) 激动剂,对 RXRα、RXRβ和 RXRγ的 EC50分别为 33、24和25 nM。它是一种类视黄醇类似物,用于治疗皮肤 T 细胞淋巴瘤的皮肤表现。 | |||
T0414 | Apoptosis Dehydrogenase Endogenous Metabolite | ||
D-Mannitol (Mannitol) 是与山梨醇相关的利尿剂和肾脏诊断辅助剂,具有较弱的肾脏血管扩张活性。 | |||
T39273 | |||
Lumasiran (ALN-G01), a siRNA product, inhibits hepatic oxalate production by targeting glycolate oxidase. By silencing the gene encoding glycolate oxidase, Lumasiran depletes this enzyme and thereby prevents the synthesis of oxalate, the toxic metabolite directly linked to the clinical manifestations of Primary hyperoxaluria type 1 (PH1). |
目录号 | 产品名/同用名 | 种属 | 表达系统 | ||
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TMPK-00758 | IgE Protein, Human, Recombinant (His & Avi) | Human | HEK293 | ||
Immunoglobulin E (IgE) is well known for its role in allergic disease, the manifestations of which are mediated through its two Fc receptors, FcεRI and CD23 (FcεRII). IgE and its interactions with these receptors are therefore potential targets for therapeutic intervention, and exciting progress has been made in this direction. Furthermore, recent structural studies of IgE-Fc, the two receptors, and of their complexes, have revealed a remarkable degree of plasticity at the IgE-CD23 interface and an even more remarkable degree of dynamic flexibility within the IgE molecule.
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TMPY-05072 | IgE Fc Protein, Human, Recombinant (His) | Human | HEK293 | ||
Immunoglobulin E (IgE) is well known for its role in allergic disease, the manifestations of which are mediated through its two Fc receptors, FcεRI and CD23 (FcεRII). IgE and its interactions with these receptors are therefore potential targets for therapeutic intervention, and exciting progress has been made in this direction. Furthermore, recent structural studies of IgE-Fc, the two receptors, and of their complexes, have revealed a remarkable degree of plasticity at the IgE-CD23 interface and an even more remarkable degree of dynamic flexibility within the IgE molecule.
IgE Protein, Human, Recombinant (His & Avi) is expressed in HEK293.
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TMPY-00828 | Iduronate 2 sulfatase/IDS Protein, Human, Recombinant (His) | Human | HEK293 | ||
Iduronate 2-Sulfatase, also known as IDS, is a member of the highly conserved sulfatase family of enzymes that catalyze the hydrolysis of O- and N-sulfate esters from a variety of substrates. The human Iduronate 2-Sulfatase/IDS consists of a signal peptide, a propeptide, and a mature chain that may be further processed into two chains. Among the identified 18 human sulfatases, Iduronate 2-Sulfatase/IDS is required for the lysosomal degradation of the glycosaminoglycans (GAG), heparan sulfate, and dermatan sulfate. Multiple mutations in this X-chromosome localized gene result in Iduronate 2-Sulfatase/IDS enzymatic deficiency and lead to the sex-linked Mucopolysaccharidosis Type II (MPS II ), also known as Hunter Syndrome characterized by the lysosomal accumulation of the GAG and their excretion in urine. MPS II has a wide spectrum of clinical manifestations ranging from mild to severe due to the level of Iduronate 2-Sulfatase/IDS enzyme. Retroviral-mediated Iduronate 2-Sulfatase/IDS gene transfer into lymphoid cells would be a promising gene therapeutic strategy.
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TMPY-01475 | Jagged 1 Protein, Human, Recombinant (His) | Human | HEK293 | ||
Protein Jagged 1, also known as JAG1, JAGL1, and CD339, is a single-pass type I membrane protein that contains 1 DSL domain and 15 EGF-like domains. JAG1/Jagged 1 is widely expressed in adult and fetal tissues. The expression of JAG1/Jagged 1 is up-regulated in cervical squamous cell carcinoma. JAG1/Jagged 1 is also expressed in bone marrow cell line HS-27a which supports the long-term maintenance of immature progenitor cells. JAG1/Jagged 1 is a ligand for multiple Notch receptors. It is involved in the mediation of Notch signaling. JAG1/Jagged 1 may be involved in cell-fate decisions during hematopoiesis. JAG1/Jagged 1 seems to be involved in the early and late stages of mammalian cardiovascular development. It inhibits myoblast differentiation and enhances fibroblast growth factor-induced angiogenesis. Defects in JAG1/Jagged 1 are the cause of Alagille syndrome type 1 (ALGS1). Alagille syndrome is an autosomal dominant multisystem disorder defined clinically by hepatic bile duct paucity and cholestasis in association with cardiac, skeletal, and ophthalmologic manifestations. Defects in JAG1/Jagged 1 are also a cause of tetralogy of Fallot (TOF). TOF is a congenital heart anomaly that consists of pulmonary stenosis, ventricular septal defect, dextroposition of the aorta (aorta is on the right side instead of the left), and hypertrophy of the right ventricle. This condition results in a blue baby at birth due to inadequate oxygenation.
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TMPK-00779 | IgE Protein, Mouse, Recombinant (His & Avi) | Mouse | HEK293 | ||
Immunoglobulin E (IgE) is well known for its role in allergic disease, the manifestations of which are mediated through its two Fc receptors, FcεRI and CD23 (FcεRII). IgE and its interactions with these receptors are therefore potential targets for therapeutic intervention, and exciting progress has been made in this direction. Furthermore, recent structural studies of IgE-Fc, the two receptors, and of their complexes, have revealed a remarkable degree of plasticity at the IgE-CD23 interface and an even more remarkable degree of dynamic flexibility within the IgE molecule.
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TMPK-00670 | IgE Protein, Cynomolgus, Recombinant (His & Avi) | Cynomolgus | HEK293 | ||
Immunoglobulin E (IgE) is well known for its role in allergic disease, the manifestations of which are mediated through its two Fc receptors, FcεRI and CD23 (FcεRII). IgE and its interactions with these receptors are therefore potential targets for therapeutic intervention, and exciting progress has been made in this direction. Furthermore, recent structural studies of IgE-Fc, the two receptors, and of their complexes, have revealed a remarkable degree of plasticity at the IgE-CD23 interface and an even more remarkable degree of dynamic flexibility within the IgE molecule.
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TMPK-00818 | Glycophorin A Protein, Mouse, Recombinant (His) | Mouse | HEK293 | ||
Granulomatosis with polyangiitis (GPA) presents a wide spectrum of manifestations from the common respiratory symptoms to infrequent neurological and cardiac complications. The challenge in diagnosis and management makes the rapidly progressive disorder one of the most challenging dilemmas in clinical medicine.The ultimate goal is an improved prognosis through outcome measures which assesses the disease control with minimal adverse effects of intensive immunosuppressive regimens, an integral part of the clinical approach to improve the quality of life of GPA patients.
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TMPK-01158 | Kallikrein 5/KLK5 Protein, Mouse, Recombinant (His) | Mouse | HEK293 | ||
The inhibition of kallikrein 5 (KLK5) has been identified as a potential strategy for treatment of the genetic skin disorder Netherton syndrome, in which loss-of-function mutations in the SPINK5 gene lead to down-regulation of the endogenous inhibitor LEKTI-1 and profound skin-barrier defects with severe allergic manifestations. To aid in the development of a medicine for this target, an X-ray crystallographic system was developed to facilitate fragment-guided chemistry and knowledge-based drug-discovery approaches.
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TMPJ-01002 | SGSH Protein, Human, Recombinant (His) | Human | Human Cells | ||
N-Sulphoglucosamine Sulphohydrolase (SGSH) is an important member of the sulfatase family which is involved in the degradation of heparin sulfate. SGSH binds one calcium ion per subunit as a cofactor. SGSH catalyzes N-sulfo-D-glucosamine and H2O to D-glucosamine and sulfate. SGSH deficiency is result in mucopolysaccharidosis type 3A (MPS3A), a recessive lysosomal storage disease characterized by neurological dysfunction but relatively mild somatic manifestations.
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TMPK-00817 | Glycophorin A Protein, Mouse, Recombinant (hFc) | Mouse | HEK293 | ||
Granulomatosis with polyangiitis (GPA) presents a wide spectrum of manifestations from the common respiratory symptoms to infrequent neurological and cardiac complications. The challenge in diagnosis and management makes the rapidly progressive disorder one of the most challenging dilemmas in clinical medicine.The ultimate goal is an improved prognosis through outcome measures which assesses the disease control with minimal adverse effects of intensive immunosuppressive regimens, an integral part of the clinical approach to improve the quality of life of GPA patients.
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TMPJ-00876 | FAH Protein, Human, Recombinant (His) | Human | Human Cells | ||
Fumarylacetoacetase belongs to the FAH family. Fumarylacetoacetase is primary expressed in liver and kidney. It exists as a homodimer and catalyzes the hydrolysis of 4-fumarylacetoacetate into fumarate and acetoacetate. Defects in Fumarylacetoacetase cause tyrosinemia type 1, which is congenital metabolism defect characterized by elevated levels of tyrosine in the blood and urine, and hepatorenal manifestations. Typical features include renal tubular injury, self-mutilation, hepatic necrosis, episodic weakness, and seizures.
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TMPJ-00863 | GNS Protein, Human, Recombinant (His) | Human | Human Cells | ||
N-Acetylglucosamine-6-Sulfatase is a member of the Sulfatase family. N-Acetylglucosamine-6-Sulfatase is required for the lysosomal degradation of the Glycosaminoglycans (GAG) Heparan Sulfate and Keratan Sulfate. N-Acetylglucosamine-6-Sulfatase hydrolyzes the 6-Sulfate groups of the N-Acetyl-D-Glucosamine 6-Sulfate units of Heparan Sulfate and Keratan Sulfate. N-Acetylglucosamine-6-Sulfatase binds 1 Calcium ion per subunit. N-Acetylglucosamine-6-Sulfatase deficiency are the cause of Mucopolysaccharidosis Type 3D (MPS3D), an inborn error leading to lysosomal accumulation of heparan sulfate. MPS3D has profound mental deterioration, hyperactivity, and relatively mild somatic manifestations.
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TMPK-00780 | IgE Protein, Mouse, Recombinant (His) | Mouse | HEK293 | ||
Immunoglobulin E (IgE) is well known for its role in allergic disease, the manifestations of which are mediated through its two Fc receptors, FcεRI and CD23 (FcεRII). IgE and its interactions with these receptors are therefore potential targets for therapeutic intervention, and exciting progress has been made in this direction. Furthermore, recent structural studies of IgE-Fc, the two receptors, and of their complexes, have revealed a remarkable degree of plasticity at the IgE-CD23 interface and an even more remarkable degree of dynamic flexibility within the IgE molecule.
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TMPK-00029 | Glycophorin A Protein, Human, Recombinant (hFc) | Human | HEK293 | ||
Granulomatosis with polyangiitis (GPA) presents a wide spectrum of manifestations from the common respiratory symptoms to infrequent neurological and cardiac complications. The challenge in diagnosis and management makes the rapidly progressive disorder one of the most challenging dilemmas in clinical medicine.The ultimate goal is an improved prognosis through outcome measures which assesses the disease control with minimal adverse effects of intensive immunosuppressive regimens, an integral part of the clinical approach to improve the quality of life of GPA patients.
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TMPK-00534 | Glycophorin A Protein, Cynomolgus, Recombinant (His) | Cynomolgus | HEK293 | ||
Granulomatosis with polyangiitis (GPA) presents a wide spectrum of manifestations from the common respiratory symptoms to infrequent neurological and cardiac complications. The challenge in diagnosis and management makes the rapidly progressive disorder one of the most challenging dilemmas in clinical medicine.The ultimate goal is an improved prognosis through outcome measures which assesses the disease control with minimal adverse effects of intensive immunosuppressive regimens, an integral part of the clinical approach to improve the quality of life of GPA patients.
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TMPJ-00704 | SCO1 Protein, Human, Recombinant (GST) | Human | E. coli | ||
Protein SCO1 Homolog, Mitochondrial (SCO1) is a member of the SCO1/2 family. SCO1 has a homodimer structure. SCO1 is located in mitochondrion and is highly expressed in muscle, heart, and brain. It is characterized by high rates of Oxidative Phosphorylation (OxPhos). SCO1 is thought to play a important role in cellular copper homeostasis, mitochondrial redox signaling and insertion of copper into the active site of COX. The defects of SCO1 can result in Mitochondrial Complex IV Deficiency (MT-C4D). A disorder of the mitochondrial respiratory chain has heterogeneous clinical manifestations, ranging from isolated myopathy to severe multisystem disease affecting several tissues and organs.
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TMPY-02799 | ALDH4A1 Protein, Human, Recombinant (His & GST) | Human | Baculovirus-Insect Cells | ||
ALDH4A1 is a member of the aldehyde dehydrogenase family. Aldehyde dehydrogenase enzymes function in the metabolism of many molecules including certain fats (cholesterol and other fatty acids) and protein building blocks (amino acids). Additional aldehyde dehydrogenase enzymes detoxify external substances, such as alcohol and pollutants, and internal substances, such as toxins that are formed within cells. ALDH4A1 is expressed abundantly in liver followed by skeletal muscle, kidney, heart, brain, placenta, lung and pancreas. It is a mitochondrial matrix NAD-dependent dehydrogenase which catalyzes the second step of the proline degradation pathway, converting pyrroline-5-carboxylate to glutamate. Defects in ALDH4A1 are the cause of hyperprolinemia type 2 (HP-2). HP-2 is characterized by the accumulation of delta-1-pyrroline-5-carboxylate (P5C) and proline. The disorder may be causally related to neurologic manifestations, including seizures and mental retardation.
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TMPY-03433 | ALDH4A1 Protein, Human, Recombinant | Human | Baculovirus-Insect Cells | ||
ALDH4A1 is a member of the aldehyde dehydrogenase family. Aldehyde dehydrogenase enzymes function in the metabolism of many molecules including certain fats (cholesterol and other fatty acids) and protein building blocks (amino acids). Additional aldehyde dehydrogenase enzymes detoxify external substances, such as alcohol and pollutants, and internal substances, such as toxins that are formed within cells. ALDH4A1 is expressed abundantly in liver followed by skeletal muscle, kidney, heart, brain, placenta, lung and pancreas. It is a mitochondrial matrix NAD-dependent dehydrogenase which catalyzes the second step of the proline degradation pathway, converting pyrroline-5-carboxylate to glutamate. Defects in ALDH4A1 are the cause of hyperprolinemia type 2 (HP-2). HP-2 is characterized by the accumulation of delta-1-pyrroline-5-carboxylate (P5C) and proline. The disorder may be causally related to neurologic manifestations, including seizures and mental retardation.
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TMPY-04996 | Coagulation Factor II Protein, Rat, Recombinant (His) | Rat | HEK293 | ||
Coagulation Factor II Protein (FII, F2 Protein or Prothrombin) is proteolytically cleaved to form thrombin in the first step of the coagulation cascade which ultimately results in the stemming of blood loss. Coagulation Factor II Protein (FII, F2 Protein) also plays a role in maintaining vascular integrity during development and postnatal life. Prothrombin / Coagulation Factor II is activated on the surface of a phospholipid membrane that binds the amino end of prothrombin / Coagulation Factor II and factor Va and Xa in Ca-dependent interactions; factor Xa removes the activation peptide and cleaves the remaining part into light and heavy chains. The activation process starts slowly because factor V itself has to be activated by the initial, small amounts of thrombin. Prothrombin / Coagulation Factor II is expressed by the liver and secreted in plasma. Defects in prothrombin / Coagulation Factor II are the cause of factor II deficiency (FA2D). It is very rare blood coagulation disorder characterized by mucocutaneous bleeding symptoms. The severity of the bleeding manifestations correlates with blood factor II levels. Defects in Coagulation Factor II are also a cause of susceptibility to thrombosis. It is a multifactorial disorder of hemostasis characterized by abnormal platelet aggregation in response to various agents and recurrent thrombi formation.
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TMPY-01791 | Coagulation Factor II Protein, Mouse, Recombinant (His) | Mouse | HEK293 | ||
Coagulation Factor II Protein (FII, F2 Protein or Prothrombin) is proteolytically cleaved to form thrombin in the first step of the coagulation cascade which ultimately results in the stemming of blood loss. Coagulation Factor II Protein (FII, F2 Protein) also plays a role in maintaining vascular integrity during development and postnatal life. Prothrombin / Coagulation Factor II is activated on the surface of a phospholipid membrane that binds the amino end of prothrombin / Coagulation Factor II and factor Va and Xa in Ca-dependent interactions; factor Xa removes the activation peptide and cleaves the remaining part into light and heavy chains. The activation process starts slowly because factor V itself has to be activated by the initial, small amounts of thrombin. Prothrombin / Coagulation Factor II is expressed by the liver and secreted in plasma. Defects in prothrombin / Coagulation Factor II are the cause of factor II deficiency (FA2D). It is very rare blood coagulation disorder characterized by mucocutaneous bleeding symptoms. The severity of the bleeding manifestations correlates with blood factor II levels. Defects in Coagulation Factor II are also a cause of susceptibility to thrombosis. It is a multifactorial disorder of hemostasis characterized by abnormal platelet aggregation in response to various agents and recurrent thrombi formation.
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TMPY-01470 | Jagged 1 Protein, Human, Recombinant (hFc) | Human | HEK293 | ||
Protein Jagged 1, also known as JAG1, JAGL1, and CD339, is a single-pass type I membrane protein that contains 1 DSL domain and 15 EGF-like domains. JAG1/Jagged 1 is widely expressed in adult and fetal tissues. The expression of JAG1/Jagged 1 is up-regulated in cervical squamous cell carcinoma. JAG1/Jagged 1 is also expressed in bone marrow cell line HS-27a which supports the long-term maintenance of immature progenitor cells. JAG1/Jagged 1 is a ligand for multiple Notch receptors. It is involved in the mediation of Notch signaling. JAG1/Jagged 1 may be involved in cell-fate decisions during hematopoiesis. JAG1/Jagged 1 seems to be involved in the early and late stages of mammalian cardiovascular development. It inhibits myoblast differentiation and enhances fibroblast growth factor-induced angiogenesis. Defects in JAG1/Jagged 1 are the cause of Alagille syndrome type 1 (ALGS1). Alagille syndrome is an autosomal dominant multisystem disorder defined clinically by hepatic bile duct paucity and cholestasis in association with cardiac, skeletal, and ophthalmologic manifestations. Defects in JAG1/Jagged 1 are also a cause of tetralogy of Fallot (TOF). TOF is a congenital heart anomaly that consists of pulmonary stenosis, ventricular septal defect, dextroposition of the aorta (aorta is on the right side instead of the left), and hypertrophy of the right ventricle. This condition results in a blue baby at birth due to inadequate oxygenation.
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TMPY-05411 | Human Papilloma Virus type 58 (HPV 58) L1 Protein-VLP | HPV | Baculovirus-Insect Cells | ||
Papillomaviruses are highly species-specific and can cause squamous epithelial and fibroepithelial tumors in their hosts. Human papillomaviruses (HPVs) are associated with benign and malignant hyperproliferation of cells, with a wide variety of clinical manifestations ranging from condyloma acuminatum to cervical carcinoma. HPV infection is the most common sexually transmitted disease. More than 4 HPV types so far identified are known to infect the genital tract. Genital HPVs are divided into `low risk' HPVs such as HPV 6 and 11 and ‘high risk’ HPV types such as 16, 18, 31, 33, 35, 39, 45 and 52, 58 which are responsible for more than 95% of HPV-induced cervical cancer. Vaccination against these high-risk types seems to be the most feasible prevention for cervical cancer. Indeed, clinical trials have shown prophylactic HPV vaccines to be effective against HPV infection, cervical intraepithelial neoplasia (CIN), and genital warts, but protection is type-specific and the currently developed vaccines target only a few types. These vaccines are based on papillomavirus-like particles (VLPs) composed of the major capsid protein, L1. The L1 protein self assembles into VLPs when expressed at high levels in eukaryotic or insect cells. VLPs are composed of 36 copies of L1 protein organized into 72 pentamers, so-called capsomeres, to form particles that are immunologically indistinguishable from native virions. Experimentally induced VLP antisera are mostly type-specific for neutralization. Minor cross-neutralization has been observed only between closely related HPV types, e.g. HPV6 and 11, HPV18 and 45, or HPV16 and 31. Structure analysis has revealed the presence of several hypervariable loops on the outer surface of the capsid. With a few exceptions, all HPV-neutralizing monoclonal antibodies analyzed so far are type-specific and recognize conformational epitopes within surface-exposed hypervariable loops of the major capsid protein L1.
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TMPY-05399 | Human Papilloma Virus type 6 (HPV 6) L1 Protein-VLP | HPV | Baculovirus-Insect Cells | ||
Papillomaviruses are highly species-specific and can cause squamous epithelial and fibroepithelial tumors in their hosts. Human papillomaviruses (HPVs) are associated with benign and malignant hyperproliferation of cells, with a wide variety of clinical manifestations ranging from condyloma acuminatum to cervical carcinoma. HPV infection is the most common sexually transmitted disease. More than 4 HPV types so far identified are known to infect the genital tract. Genital HPVs are divided into `low risk' HPVs such as HPV 6 and 11 and ‘high risk’ HPV types such as 16, 18, 31, 33, 35, 39, 45 and 52, 58 which are responsible for more than 95% of HPV-induced cervical cancer. Vaccination against these high-risk types seems to be the most feasible prevention for cervical cancer. Indeed, clinical trials have shown prophylactic HPV vaccines to be effective against HPV infection, cervical intraepithelial neoplasia (CIN), and genital warts, but protection is type-specific and the currently developed vaccines target only a few types. These vaccines are based on papillomavirus-like particles (VLPs) composed of the major capsid protein, L1. The L1 protein self assembles into VLPs when expressed at high levels in eukaryotic or insect cells. VLPs are composed of 36 copies of L1 protein organized into 72 pentamers, so-called capsomeres, to form particles that are immunologically indistinguishable from native virions. Experimentally induced VLP antisera are mostly type-specific for neutralization. Minor cross-neutralization has been observed only between closely related HPV types, e.g. HPV6 and 11, HPV18 and 45, or HPV16 and 31. Structure analysis has revealed the presence of several hypervariable loops on the outer surface of the capsid. With a few exceptions, all HPV-neutralizing monoclonal antibodies analyzed so far are type-specific and recognize conformational epitopes within surface-exposed hypervariable loops of the major capsid protein L1.
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TMPY-05400 | Human Papilloma Virus type 11 (HPV 11) L1 Protein-VLP | HPV | Baculovirus-Insect Cells | ||
Papillomaviruses are highly species-specific and can cause squamous epithelial and fibroepithelial tumors in their hosts. Human papillomaviruses (HPVs) are associated with benign and malignant hyperproliferation of cells, with a wide variety of clinical manifestations ranging from condyloma acuminatum to cervical carcinoma. HPV infection is the most common sexually transmitted disease. More than 4 HPV types so far identified are known to infect the genital tract. Genital HPVs are divided into `low risk' HPVs such as HPV 6 and 11 and ‘high risk’ HPV types such as 16, 18, 31, 33, 35, 39, 45 and 52, 58 which are responsible for more than 95% of HPV-induced cervical cancer. Vaccination against these high-risk types seems to be the most feasible prevention for cervical cancer. Indeed, clinical trials have shown prophylactic HPV vaccines to be effective against HPV infection, cervical intraepithelial neoplasia (CIN), and genital warts, but protection is type-specific and the currently developed vaccines target only a few types. These vaccines are based on papillomavirus-like particles (VLPs) composed of the major capsid protein, L1. The L1 protein self assembles into VLPs when expressed at high levels in eukaryotic or insect cells. VLPs are composed of 36 copies of L1 protein organized into 72 pentamers, so-called capsomeres, to form particles that are immunologically indistinguishable from native virions. Experimentally induced VLP antisera are mostly type-specific for neutralization. Minor cross-neutralization has been observed only between closely related HPV types, e.g. HPV6 and 11, HPV18 and 45, or HPV16 and 31. Structure analysis has revealed the presence of several hypervariable loops on the outer surface of the capsid. With a few exceptions, all HPV-neutralizing monoclonal antibodies analyzed so far are type-specific and recognize conformational epitopes within surface-exposed hypervariable loops of the major capsid protein L1.
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TMPY-05405 | Human Papilloma Virus type 35 (HPV 35) L1 Protein-VLP | HPV | Baculovirus-Insect Cells | ||
Papillomaviruses are highly species-specific and can cause squamous epithelial and fibroepithelial tumors in their hosts. Human papillomaviruses (HPVs) are associated with benign and malignant hyperproliferation of cells, with a wide variety of clinical manifestations ranging from condyloma acuminatum to cervical carcinoma. HPV infection is the most common sexually transmitted disease. More than 4 HPV types so far identified are known to infect the genital tract. Genital HPVs are divided into `low risk' HPVs such as HPV 6 and 11 and ‘high risk’ HPV types such as 16, 18, 31, 33, 35, 39, 45 and 52, 58 which are responsible for more than 95% of HPV-induced cervical cancer. Vaccination against these high-risk types seems to be the most feasible prevention for cervical cancer. Indeed, clinical trials have shown prophylactic HPV vaccines to be effective against HPV infection, cervical intraepithelial neoplasia (CIN), and genital warts, but protection is type-specific and the currently developed vaccines target only a few types. These vaccines are based on papillomavirus-like particles (VLPs) composed of the major capsid protein, L1. The L1 protein self assembles into VLPs when expressed at high levels in eukaryotic or insect cells. VLPs are composed of 36 copies of L1 protein organized into 72 pentamers, so-called capsomeres, to form particles that are immunologically indistinguishable from native virions. Experimentally induced VLP antisera are mostly type-specific for neutralization. Minor cross-neutralization has been observed only between closely related HPV types, e.g. HPV6 and 11, HPV18 and 45, or HPV16 and 31. Structure analysis has revealed the presence of several hypervariable loops on the outer surface of the capsid. With a few exceptions, all HPV-neutralizing monoclonal antibodies analyzed so far are type-specific and recognize conformational epitopes within surface-exposed hypervariable loops of the major capsid protein L1.
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TMPY-05401 | Human Papilloma Virus type 16 (HPV 16) L1 Protein-VLP | HPV | Baculovirus-Insect Cells | ||
Papillomaviruses are highly species-specific and can cause squamous epithelial and fibroepithelial tumors in their hosts. Human papillomaviruses (HPVs) are associated with benign and malignant hyperproliferation of cells, with a wide variety of clinical manifestations ranging from condyloma acuminatum to cervical carcinoma. HPV infection is the most common sexually transmitted disease. More than 4 HPV types so far identified are known to infect the genital tract. Genital HPVs are divided into `low risk' HPVs such as HPV 6 and 11 and ‘high risk’ HPV types such as 16, 18, 31, 33, 35, 39, 45 and 52, 58 which are responsible for more than 95% of HPV-induced cervical cancer. Vaccination against these high-risk types seems to be the most feasible prevention for cervical cancer. Indeed, clinical trials have shown prophylactic HPV vaccines to be effective against HPV infection, cervical intraepithelial neoplasia (CIN), and genital warts, but protection is type-specific and the currently developed vaccines target only a few types. These vaccines are based on papillomavirus-like particles (VLPs) composed of the major capsid protein, L1. The L1 protein self assembles into VLPs when expressed at high levels in eukaryotic or insect cells. VLPs are composed of 36 copies of L1 protein organized into 72 pentamers, so-called capsomeres, to form particles that are immunologically indistinguishable from native virions. Experimentally induced VLP antisera are mostly type-specific for neutralization. Minor cross-neutralization has been observed only between closely related HPV types, e.g. HPV6 and 11, HPV18 and 45, or HPV16 and 31. Structure analysis has revealed the presence of several hypervariable loops on the outer surface of the capsid. With a few exceptions, all HPV-neutralizing monoclonal antibodies analyzed so far are type-specific and recognize conformational epitopes within surface-exposed hypervariable loops of the major capsid protein L1.
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TMPY-05403 | Human Papilloma Virus type 31 (HPV 31) L1 Protein-VLP | HPV | Baculovirus-Insect Cells | ||
Papillomaviruses are highly species-specific and can cause squamous epithelial and fibroepithelial tumors in their hosts. Human papillomaviruses (HPVs) are associated with benign and malignant hyperproliferation of cells, with a wide variety of clinical manifestations ranging from condyloma acuminatum to cervical carcinoma. HPV infection is the most common sexually transmitted disease. More than 4 HPV types so far identified are known to infect the genital tract. Genital HPVs are divided into `low risk' HPVs such as HPV 6 and 11 and ‘high risk’ HPV types such as 16, 18, 31, 33, 35, 39, 45 and 52, 58 which are responsible for more than 95% of HPV-induced cervical cancer. Vaccination against these high-risk types seems to be the most feasible prevention for cervical cancer. Indeed, clinical trials have shown prophylactic HPV vaccines to be effective against HPV infection, cervical intraepithelial neoplasia (CIN), and genital warts, but protection is type-specific and the currently developed vaccines target only a few types. These vaccines are based on papillomavirus-like particles (VLPs) composed of the major capsid protein, L1. The L1 protein self assembles into VLPs when expressed at high levels in eukaryotic or insect cells. VLPs are composed of 36 copies of L1 protein organized into 72 pentamers, so-called capsomeres, to form particles that are immunologically indistinguishable from native virions. Experimentally induced VLP antisera are mostly type-specific for neutralization. Minor cross-neutralization has been observed only between closely related HPV types, e.g. HPV6 and 11, HPV18 and 45, or HPV16 and 31. Structure analysis has revealed the presence of several hypervariable loops on the outer surface of the capsid. With a few exceptions, all HPV-neutralizing monoclonal antibodies analyzed so far are type-specific and recognize conformational epitopes within surface-exposed hypervariable loops of the major capsid protein L1.
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TMPY-05409 | Human Papilloma Virus type 52 (HPV 52) L1 Protein-VLP | HPV | Baculovirus-Insect Cells | ||
Papillomaviruses are highly species-specific and can cause squamous epithelial and fibroepithelial tumors in their hosts. Human papillomaviruses (HPVs) are associated with benign and malignant hyperproliferation of cells, with a wide variety of clinical manifestations ranging from condyloma acuminatum to cervical carcinoma. HPV infection is the most common sexually transmitted disease. More than 4 HPV types so far identified are known to infect the genital tract. Genital HPVs are divided into `low risk' HPVs such as HPV 6 and 11 and ‘high risk’ HPV types such as 16, 18, 31, 33, 35, 39, 45 and 52, 58 which are responsible for more than 95% of HPV-induced cervical cancer. Vaccination against these high-risk types seems to be the most feasible prevention for cervical cancer. Indeed, clinical trials have shown prophylactic HPV vaccines to be effective against HPV infection, cervical intraepithelial neoplasia (CIN), and genital warts, but protection is type-specific and the currently developed vaccines target only a few types. These vaccines are based on papillomavirus-like particles (VLPs) composed of the major capsid protein, L1. The L1 protein self assembles into VLPs when expressed at high levels in eukaryotic or insect cells. VLPs are composed of 36 copies of L1 protein organized into 72 pentamers, so-called capsomeres, to form particles that are immunologically indistinguishable from native virions. Experimentally induced VLP antisera are mostly type-specific for neutralization. Minor cross-neutralization has been observed only between closely related HPV types, e.g. HPV6 and 11, HPV18 and 45, or HPV16 and 31. Structure analysis has revealed the presence of several hypervariable loops on the outer surface of the capsid. With a few exceptions, all HPV-neutralizing monoclonal antibodies analyzed so far are type-specific and recognize conformational epitopes within surface-exposed hypervariable loops of the major capsid protein L1.
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TMPY-05407 | Human Papilloma Virus type 45 (HPV 45) L1 Protein-VLP | HPV | Baculovirus-Insect Cells | ||
Papillomaviruses are highly species-specific and can cause squamous epithelial and fibroepithelial tumors in their hosts. Human papillomaviruses (HPVs) are associated with benign and malignant hyperproliferation of cells, with a wide variety of clinical manifestations ranging from condyloma acuminatum to cervical carcinoma. HPV infection is the most common sexually transmitted disease. More than 4 HPV types so far identified are known to infect the genital tract. Genital HPVs are divided into `low risk' HPVs such as HPV 6 and 11 and ‘high risk’ HPV types such as 16, 18, 31, 33, 35, 39, 45 and 52, 58 which are responsible for more than 95% of HPV-induced cervical cancer. Vaccination against these high-risk types seems to be the most feasible prevention for cervical cancer. Indeed, clinical trials have shown prophylactic HPV vaccines to be effective against HPV infection, cervical intraepithelial neoplasia (CIN), and genital warts, but protection is type-specific and the currently developed vaccines target only a few types. These vaccines are based on papillomavirus-like particles (VLPs) composed of the major capsid protein, L1. The L1 protein self assembles into VLPs when expressed at high levels in eukaryotic or insect cells. VLPs are composed of 36 copies of L1 protein organized into 72 pentamers, so-called capsomeres, to form particles that are immunologically indistinguishable from native virions. Experimentally induced VLP antisera are mostly type-specific for neutralization. Minor cross-neutralization has been observed only between closely related HPV types, e.g. HPV6 and 11, HPV18 and 45, or HPV16 and 31. Structure analysis has revealed the presence of several hypervariable loops on the outer surface of the capsid. With a few exceptions, all HPV-neutralizing monoclonal antibodies analyzed so far are type-specific and recognize conformational epitopes within surface-exposed hypervariable loops of the major capsid protein L1.
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TMPY-05402 | Human Papilloma Virus type 18 (HPV 18) L1 Protein-VLP | HPV | Baculovirus-Insect Cells | ||
Papillomaviruses are highly species-specific and can cause squamous epithelial and fibroepithelial tumors in their hosts. Human papillomaviruses (HPVs) are associated with benign and malignant hyperproliferation of cells, with a wide variety of clinical manifestations ranging from condyloma acuminatum to cervical carcinoma. HPV infection is the most common sexually transmitted disease. More than 4 HPV types so far identified are known to infect the genital tract. Genital HPVs are divided into `low risk' HPVs such as HPV 6 and 11 and ‘high risk’ HPV types such as 16, 18, 31, 33, 35, 39, 45 and 52, 58 which are responsible for more than 95% of HPV-induced cervical cancer. Vaccination against these high-risk types seems to be the most feasible prevention for cervical cancer. Indeed, clinical trials have shown prophylactic HPV vaccines to be effective against HPV infection, cervical intraepithelial neoplasia (CIN), and genital warts, but protection is type-specific and the currently developed vaccines target only a few types. These vaccines are based on papillomavirus-like particles (VLPs) composed of the major capsid protein, L1. The L1 protein self assembles into VLPs when expressed at high levels in eukaryotic or insect cells. VLPs are composed of 36 copies of L1 protein organized into 72 pentamers, so-called capsomeres, to form particles that are immunologically indistinguishable from native virions. Experimentally induced VLP antisera are mostly type-specific for neutralization. Minor cross-neutralization has been observed only between closely related HPV types, e.g. HPV6 and 11, HPV18 and 45, or HPV16 and 31. Structure analysis has revealed the presence of several hypervariable loops on the outer surface of the capsid. With a few exceptions, all HPV-neutralizing monoclonal antibodies analyzed so far are type-specific and recognize conformational epitopes within surface-exposed hypervariable loops of the major capsid protein L1.
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TMPY-05406 | Human Papilloma Virus type 39 (HPV 39) L1 Protein-VLP | HPV | Baculovirus-Insect Cells | ||
Papillomaviruses are highly species-specific and can cause squamous epithelial and fibroepithelial tumors in their hosts. Human papillomaviruses (HPVs) are associated with benign and malignant hyperproliferation of cells, with a wide variety of clinical manifestations ranging from condyloma acuminatum to cervical carcinoma. HPV infection is the most common sexually transmitted disease. More than 4 HPV types so far identified are known to infect the genital tract. Genital HPVs are divided into `low risk' HPVs such as HPV 6 and 11 and ‘high risk’ HPV types such as 16, 18, 31, 33, 35, 39, 45 and 52, 58 which are responsible for more than 95% of HPV-induced cervical cancer. Vaccination against these high-risk types seems to be the most feasible prevention for cervical cancer. Indeed, clinical trials have shown prophylactic HPV vaccines to be effective against HPV infection, cervical intraepithelial neoplasia (CIN), and genital warts, but protection is type-specific and the currently developed vaccines target only a few types. These vaccines are based on papillomavirus-like particles (VLPs) composed of the major capsid protein, L1. The L1 protein self assembles into VLPs when expressed at high levels in eukaryotic or insect cells. VLPs are composed of 36 copies of L1 protein organized into 72 pentamers, so-called capsomeres, to form particles that are immunologically indistinguishable from native virions. Experimentally induced VLP antisera are mostly type-specific for neutralization. Minor cross-neutralization has been observed only between closely related HPV types, e.g. HPV6 and 11, HPV18 and 45, or HPV16 and 31. Structure analysis has revealed the presence of several hypervariable loops on the outer surface of the capsid. With a few exceptions, all HPV-neutralizing monoclonal antibodies analyzed so far are type-specific and recognize conformational epitopes within surface-exposed hypervariable loops of the major capsid protein L1.
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TMPY-05404 | Human Papilloma Virus type 33 (HPV 33) L1 Protein-VLP | HPV | Baculovirus-Insect Cells | ||
Papillomaviruses are highly species-specific and can cause squamous epithelial and fibroepithelial tumors in their hosts. Human papillomaviruses (HPVs) are associated with benign and malignant hyperproliferation of cells, with a wide variety of clinical manifestations ranging from condyloma acuminatum to cervical carcinoma. HPV infection is the most common sexually transmitted disease. More than 4 HPV types so far identified are known to infect the genital tract. Genital HPVs are divided into `low risk' HPVs such as HPV 6 and 11 and ‘high risk’ HPV types such as 16, 18, 31, 33, 35, 39, 45 and 52, 58 which are responsible for more than 95% of HPV-induced cervical cancer. Vaccination against these high-risk types seems to be the most feasible prevention for cervical cancer. Indeed, clinical trials have shown prophylactic HPV vaccines to be effective against HPV infection, cervical intraepithelial neoplasia (CIN), and genital warts, but protection is type-specific and the currently developed vaccines target only a few types. These vaccines are based on papillomavirus-like particles (VLPs) composed of the major capsid protein, L1. The L1 protein self assembles into VLPs when expressed at high levels in eukaryotic or insect cells. VLPs are composed of 36 copies of L1 protein organized into 72 pentamers, so-called capsomeres, to form particles that are immunologically indistinguishable from native virions. Experimentally induced VLP antisera are mostly type-specific for neutralization. Minor cross-neutralization has been observed only between closely related HPV types, e.g. HPV6 and 11, HPV18 and 45, or HPV16 and 31. Structure analysis has revealed the presence of several hypervariable loops on the outer surface of the capsid. With a few exceptions, all HPV-neutralizing monoclonal antibodies analyzed so far are type-specific and recognize conformational epitopes within surface-exposed hypervariable loops of the major capsid protein L1.
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TMPY-05410 | Human Papilloma Virus type 56 (HPV 56) L1 Protein-VLP | HPV | Baculovirus-Insect Cells | ||
Papillomaviruses are highly species-specific and can cause squamous epithelial and fibroepithelial tumors in their hosts. Human papillomaviruses (HPVs) are associated with benign and malignant hyperproliferation of cells, with a wide variety of clinical manifestations ranging from condyloma acuminatum to cervical carcinoma. HPV infection is the most common sexually transmitted disease. More than 4 HPV types so far identified are known to infect the genital tract. Genital HPVs are divided into `low risk' HPVs such as HPV 6 and 11 and ‘high risk’ HPV types such as 16, 18, 31, 33, 35, 39, 45 and 52, 58 which are responsible for more than 95% of HPV-induced cervical cancer. Vaccination against these high-risk types seems to be the most feasible prevention for cervical cancer. Indeed, clinical trials have shown prophylactic HPV vaccines to be effective against HPV infection, cervical intraepithelial neoplasia (CIN), and genital warts, but protection is type-specific and the currently developed vaccines target only a few types. These vaccines are based on papillomavirus-like particles (VLPs) composed of the major capsid protein, L1. The L1 protein self assembles into VLPs when expressed at high levels in eukaryotic or insect cells. VLPs are composed of 36 copies of L1 protein organized into 72 pentamers, so-called capsomeres, to form particles that are immunologically indistinguishable from native virions. Experimentally induced VLP antisera are mostly type-specific for neutralization. Minor cross-neutralization has been observed only between closely related HPV types, e.g. HPV6 and 11, HPV18 and 45, or HPV16 and 31. Structure analysis has revealed the presence of several hypervariable loops on the outer surface of the capsid. With a few exceptions, all HPV-neutralizing monoclonal antibodies analyzed so far are type-specific and recognize conformational epitopes within surface-exposed hypervariable loops of the major capsid protein L1.
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TMPY-05412 | Human Papilloma Virus type 59 (HPV 59) L1 Protein-VLP | HPV | Baculovirus-Insect Cells | ||
Papillomaviruses are highly species-specific and can cause squamous epithelial and fibroepithelial tumors in their hosts. Human papillomaviruses (HPVs) are associated with benign and malignant hyperproliferation of cells, with a wide variety of clinical manifestations ranging from condyloma acuminatum to cervical carcinoma. HPV infection is the most common sexually transmitted disease. More than 4 HPV types so far identified are known to infect the genital tract. Genital HPVs are divided into `low risk' HPVs such as HPV 6 and 11 and ‘high risk’ HPV types such as 16, 18, 31, 33, 35, 39, 45 and 52, 58 which are responsible for more than 95% of HPV-induced cervical cancer. Vaccination against these high-risk types seems to be the most feasible prevention for cervical cancer. Indeed, clinical trials have shown prophylactic HPV vaccines to be effective against HPV infection, cervical intraepithelial neoplasia (CIN), and genital warts, but protection is type-specific and the currently developed vaccines target only a few types. These vaccines are based on papillomavirus-like particles (VLPs) composed of the major capsid protein, L1. The L1 protein self assembles into VLPs when expressed at high levels in eukaryotic or insect cells. VLPs are composed of 36 copies of L1 protein organized into 72 pentamers, so-called capsomeres, to form particles that are immunologically indistinguishable from native virions. Experimentally induced VLP antisera are mostly type-specific for neutralization. Minor cross-neutralization has been observed only between closely related HPV types, e.g. HPV6 and 11, HPV18 and 45, or HPV16 and 31. Structure analysis has revealed the presence of several hypervariable loops on the outer surface of the capsid. With a few exceptions, all HPV-neutralizing monoclonal antibodies analyzed so far are type-specific and recognize conformational epitopes within surface-exposed hypervariable loops of the major capsid protein L1.
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