Human Anti-MBP(Anti-Myelin Basic Protein Antibody) ELISA Kit

Description: Human (Homo sapiens)

Description: Human (Homo sapiens)

Description: Human (Homo sapiens)

Description: Human (Homo sapiens)

Description: Quantitative sandwich ELISA for measuring Human Myelin basic protein antibody (MBP-Ab) in samples from cell culture supernatants, serum, whole blood, plasma and other biological fluids.

Description: Quantitative sandwich ELISA for measuring Human Myelin basic protein antibody (MBP-Ab) in samples from cell culture supernatants, serum, whole blood, plasma and other biological fluids.

Description: Quantitative sandwich ELISA for measuring Human Myelin basic protein antibody (MBP-Ab) in samples from cell culture supernatants, serum, whole blood, plasma and other biological fluids.

Description: Quantitativesandwich ELISA kit for measuring Rat myelin basic protein (MBP) antibody in samples from serum, plasma. A new trial version of the kit, which allows you to test the kit in your application at a reasonable price.

Description: Quantitativesandwich ELISA kit for measuring Rat myelin basic protein(MBP) antibody in samples from serum, plasma. Now available in a cost efficient pack of 5 plates of 96 wells each, conveniently packed along with the other reagents in 5 separate kits.

Description: ELISA

Description: A competitive ELISA for quantitative measurement of Human Anti myelin basic protein antibody in samples from blood, plasma, serum, cell culture supernatant and other biological fluids. This is a high quality ELISA kit developped for optimal performance with samples from the particular species.

Description: A competitive ELISA for quantitative measurement of Human Anti myelin basic protein antibody in samples from blood, plasma, serum, cell culture supernatant and other biological fluids. This is a high quality ELISA kit developped for optimal performance with samples from the particular species.

Description: A competitive ELISA for quantitative measurement of Human Anti myelin basic protein antibody in samples from blood, plasma, serum, cell culture supernatant and other biological fluids. This is a high quality ELISA kit developped for optimal performance with samples from the particular species.

Description: Myelin Basic Protein is a major constituent of the myelin sheath of oligodendrocytes and Schwann cells in the nervous system.

Description: The classic group of MBP isoforms (isoform 4-isoform 14) are with PLP the most abundant protein components of the myelin membrane in the CNS. They have a role in both its formation and stabilization. [UniProt]

Description: Myelin basic protein (MBP) is the second most abundant protein in central nervous system (CNS) myelin: it comprises 30% of the total protein and about 10% of the dry weight of myelin. It is the only structural protein found so far to be essential for formation of CNS myelin, and has been called the executive molecule of myelin . MBP can interact with a number of polyanionic proteins including actin, tubulin, calmodulin, and clathrin, and negatively charged lipids, and acquires structure on binding to them. It may act as a membrane actin-binding protein, which might allow it to participate in transmission of extracellular signals to the cytoskeleton in oligodendrocytes and tight junctions in myelin. MBP may be applicable as a marker for oligodendrogliomas. MBP/4271 recognizes an epitope in the 129-138 region of MBP, useful in clinical diagnosis to detect MBP levels.

Description: Myelin basic protein (MBP) is the second most abundant protein in central nervous system (CNS) myelin: it comprises 30% of the total protein and about 10% of the dry weight of myelin. It is the only structural protein found so far to be essential for formation of CNS myelin, and has been called the executive molecule of myelin . MBP can interact with a number of polyanionic proteins including actin, tubulin, calmodulin, and clathrin, and negatively charged lipids, and acquires structure on binding to them. It may act as a membrane actin-binding protein, which might allow it to participate in transmission of extracellular signals to the cytoskeleton in oligodendrocytes and tight junctions in myelin. MBP may be applicable as a marker for oligodendrogliomas. MBP/4271 recognizes an epitope in the 129-138 region of MBP, useful in clinical diagnosis to detect MBP levels.

Description: Myelin basic protein (MBP) is the second most abundant protein in central nervous system (CNS) myelin: it comprises 30% of the total protein and about 10% of the dry weight of myelin. It is the only structural protein found so far to be essential for formation of CNS myelin, and has been called the executive molecule of myelin . MBP can interact with a number of polyanionic proteins including actin, tubulin, calmodulin, and clathrin, and negatively charged lipids, and acquires structure on binding to them. It may act as a membrane actin-binding protein, which might allow it to participate in transmission of extracellular signals to the cytoskeleton in oligodendrocytes and tight junctions in myelin. MBP may be applicable as a marker for oligodendrogliomas. MBP/4271 recognizes an epitope in the 129-138 region of MBP, useful in clinical diagnosis to detect MBP levels.

Description: Myelin basic protein (MBP) is the second most abundant protein in central nervous system (CNS) myelin: it comprises 30% of the total protein and about 10% of the dry weight of myelin. It is the only structural protein found so far to be essential for formation of CNS myelin, and has been called the executive molecule of myelin. MBP can interact with a number of polyanionic proteins including actin, tubulin, calmodulin, and clathrin, and negatively charged lipids, and acquires structure on binding to them. It may act as a membrane actin-binding protein, which might allow it to participate in transmission of extracellular signals to the cytoskeleton in oligodendrocytes and tight junctions in myelin. MBP may be applicable as a marker for oligodendrogliomas. MBP/4272 recognizes an epitope in the 119-131 region of MBP, useful in clinical diagnosis to detect MBP levels in human, rat and cow MBP.

Description: Myelin basic protein (MBP) is the second most abundant protein in central nervous system (CNS) myelin: it comprises 30% of the total protein and about 10% of the dry weight of myelin. It is the only structural protein found so far to be essential for formation of CNS myelin, and has been called the executive molecule of myelin. MBP can interact with a number of polyanionic proteins including actin, tubulin, calmodulin, and clathrin, and negatively charged lipids, and acquires structure on binding to them. It may act as a membrane actin-binding protein, which might allow it to participate in transmission of extracellular signals to the cytoskeleton in oligodendrocytes and tight junctions in myelin. MBP may be applicable as a marker for oligodendrogliomas. MBP/4272 recognizes an epitope in the 119-131 region of MBP, useful in clinical diagnosis to detect MBP levels in human, rat and cow MBP.

Description: Myelin basic protein (MBP) is the second most abundant protein in central nervous system (CNS) myelin: it comprises 30% of the total protein and about 10% of the dry weight of myelin. It is the only structural protein found so far to be essential for formation of CNS myelin, and has been called the executive molecule of myelin. MBP can interact with a number of polyanionic proteins including actin, tubulin, calmodulin, and clathrin, and negatively charged lipids, and acquires structure on binding to them. It may act as a membrane actin-binding protein, which might allow it to participate in transmission of extracellular signals to the cytoskeleton in oligodendrocytes and tight junctions in myelin. MBP may be applicable as a marker for oligodendrogliomas. MBP/4272 recognizes an epitope in the 119-131 region of MBP, useful in clinical diagnosis to detect MBP levels in human, rat and cow MBP.

Description: Myelin basic protein (MBP) is the second most abundant protein in central nervous system (CNS) myelin: it comprises 30% of the total protein and about 10% of the dry weight of myelin. It is the only structural protein found so far to be essential for formation of CNS myelin, and has been called the executive molecule of myelin . MBP can interact with a number of polyanionic proteins including actin, tubulin, calmodulin, and clathrin, and negatively charged lipids, and acquires structure on binding to them. It may act as a membrane actin-binding protein, which might allow it to participate in transmission of extracellular signals to the cytoskeleton in oligodendrocytes and tight junctions in myelin. MBP may be applicable as a marker for oligodendrogliomas. MBP/4273 recognizes an epitope in the 82-87 region of MBP, useful in clinical diagnosis to detect MBP levels or myelination in human MBP. MBP/4273 is also used in a 2-site ELISA with clone MBP/4275. Both are used interchangeably as capture and detection antibody.

Description: Myelin basic protein (MBP) is the second most abundant protein in central nervous system (CNS) myelin: it comprises 30% of the total protein and about 10% of the dry weight of myelin. It is the only structural protein found so far to be essential for formation of CNS myelin, and has been called the executive molecule of myelin . MBP can interact with a number of polyanionic proteins including actin, tubulin, calmodulin, and clathrin, and negatively charged lipids, and acquires structure on binding to them. It may act as a membrane actin-binding protein, which might allow it to participate in transmission of extracellular signals to the cytoskeleton in oligodendrocytes and tight junctions in myelin. MBP may be applicable as a marker for oligodendrogliomas. MBP/4273 recognizes an epitope in the 82-87 region of MBP, useful in clinical diagnosis to detect MBP levels or myelination in human MBP. MBP/4273 is also used in a 2-site ELISA with clone MBP/4275. Both are used interchangeably as capture and detection antibody.

Description: Myelin basic protein (MBP) is the second most abundant protein in central nervous system (CNS) myelin: it comprises 30% of the total protein and about 10% of the dry weight of myelin. It is the only structural protein found so far to be essential for formation of CNS myelin, and has been called the executive molecule of myelin . MBP can interact with a number of polyanionic proteins including actin, tubulin, calmodulin, and clathrin, and negatively charged lipids, and acquires structure on binding to them. It may act as a membrane actin-binding protein, which might allow it to participate in transmission of extracellular signals to the cytoskeleton in oligodendrocytes and tight junctions in myelin. MBP may be applicable as a marker for oligodendrogliomas. MBP/4273 recognizes an epitope in the 82-87 region of MBP, useful in clinical diagnosis to detect MBP levels or myelination in human MBP. MBP/4273 is also used in a 2-site ELISA with clone MBP/4275. Both are used interchangeably as capture and detection antibody.

Description: Myelin basic protein (MBP) is the second most abundant protein in central nervous system (CNS) myelin: it comprises 30% of the total protein and about 10% of the dry weight of myelin. It is the only structural protein found so far to be essential for formation of CNS myelin, and has been called the executive molecule of myelin . MBP can interact with a number of polyanionic proteins including actin, tubulin, calmodulin, and clathrin, and negatively charged lipids, and acquires structure on binding to them. It may act as a membrane actin-binding protein, which might allow it to participate in transmission of extracellular signals to the cytoskeleton in oligodendrocytes and tight junctions in myelin. MBP may be applicable as a marker for oligodendrogliomas. MBP/4274 recognizes an epitope in the 36-50 region of MBP, useful in clinical diagnosis to detect MBP levels or myelination in human MBP.

Description: Myelin basic protein (MBP) is the second most abundant protein in central nervous system (CNS) myelin: it comprises 30% of the total protein and about 10% of the dry weight of myelin. It is the only structural protein found so far to be essential for formation of CNS myelin, and has been called the executive molecule of myelin . MBP can interact with a number of polyanionic proteins including actin, tubulin, calmodulin, and clathrin, and negatively charged lipids, and acquires structure on binding to them. It may act as a membrane actin-binding protein, which might allow it to participate in transmission of extracellular signals to the cytoskeleton in oligodendrocytes and tight junctions in myelin. MBP may be applicable as a marker for oligodendrogliomas. MBP/4274 recognizes an epitope in the 36-50 region of MBP, useful in clinical diagnosis to detect MBP levels or myelination in human MBP.

Description: Myelin basic protein (MBP) is the second most abundant protein in central nervous system (CNS) myelin: it comprises 30% of the total protein and about 10% of the dry weight of myelin. It is the only structural protein found so far to be essential for formation of CNS myelin, and has been called the executive molecule of myelin . MBP can interact with a number of polyanionic proteins including actin, tubulin, calmodulin, and clathrin, and negatively charged lipids, and acquires structure on binding to them. It may act as a membrane actin-binding protein, which might allow it to participate in transmission of extracellular signals to the cytoskeleton in oligodendrocytes and tight junctions in myelin. MBP may be applicable as a marker for oligodendrogliomas. MBP/4274 recognizes an epitope in the 36-50 region of MBP, useful in clinical diagnosis to detect MBP levels or myelination in human MBP.

Description: Myelin basic protein (MBP) is the second most abundant protein in central nervous system (CNS) myelin: it comprises 30% of the total protein and about 10% of the dry weight of myelin. It is the only structural protein found so far to be essential for formation of CNS myelin, and has been called the executive molecule of myelin . MBP can interact with a number of polyanionic proteins including actin, tubulin, calmodulin, and clathrin, and negatively charged lipids, and acquires structure on binding to them. It may act as a membrane actin-binding protein, which might allow it to participate in transmission of extracellular signals to the cytoskeleton in oligodendrocytes and tight junctions in myelin. MBP may be applicable as a marker for oligodendrogliomas. MBP/4275 is used in clinical diagnostics to detect MBP levels or myelination in human MBP. MBP/4275 is used in a two-site ELISA with clone MBP/4273. Both are used interchangeably as capture and detection antibody.

Description: Myelin basic protein (MBP) is the second most abundant protein in central nervous system (CNS) myelin: it comprises 30% of the total protein and about 10% of the dry weight of myelin. It is the only structural protein found so far to be essential for formation of CNS myelin, and has been called the executive molecule of myelin . MBP can interact with a number of polyanionic proteins including actin, tubulin, calmodulin, and clathrin, and negatively charged lipids, and acquires structure on binding to them. It may act as a membrane actin-binding protein, which might allow it to participate in transmission of extracellular signals to the cytoskeleton in oligodendrocytes and tight junctions in myelin. MBP may be applicable as a marker for oligodendrogliomas. MBP/4275 is used in clinical diagnostics to detect MBP levels or myelination in human MBP. MBP/4275 is used in a two-site ELISA with clone MBP/4273. Both are used interchangeably as capture and detection antibody.

Description: Myelin basic protein (MBP) is the second most abundant protein in central nervous system (CNS) myelin: it comprises 30% of the total protein and about 10% of the dry weight of myelin. It is the only structural protein found so far to be essential for formation of CNS myelin, and has been called the executive molecule of myelin . MBP can interact with a number of polyanionic proteins including actin, tubulin, calmodulin, and clathrin, and negatively charged lipids, and acquires structure on binding to them. It may act as a membrane actin-binding protein, which might allow it to participate in transmission of extracellular signals to the cytoskeleton in oligodendrocytes and tight junctions in myelin. MBP may be applicable as a marker for oligodendrogliomas. MBP/4275 is used in clinical diagnostics to detect MBP levels or myelination in human MBP. MBP/4275 is used in a two-site ELISA with clone MBP/4273. Both are used interchangeably as capture and detection antibody.

Description: Myelin basic protein (MBP) is the second most abundant protein in central nervous system (CNS) myelin: it comprises 30% of the total protein and about 10% of the dry weight of myelin. It is the only structural protein found so far to be essential for formation of CNS myelin, and has been called the executive molecule of myelin . MBP can interact with a number of polyanionic proteins including actin, tubulin, calmodulin, and clathrin, and negatively charged lipids, and acquires structure on binding to them. It may act as a membrane actin-binding protein, which might allow it to participate in transmission of extracellular signals to the cytoskeleton in oligodendrocytes and tight junctions in myelin. MBP may be applicable as a marker for oligodendrogliomas. Phosphorylation been shown to decrease its ability to aggregate lipid vesicles and consequently destabilising the compact structure ofmyelin, a destruction that has been observed in demyelinating diseases such as Multiple Sclerosis. MBP/4276 is a useful detector of phosphorylated MBP by binding to Thr98 of human MBP in the phosphorylated state.

Description: Myelin basic protein (MBP) is the second most abundant protein in central nervous system (CNS) myelin: it comprises 30% of the total protein and about 10% of the dry weight of myelin. It is the only structural protein found so far to be essential for formation of CNS myelin, and has been called the executive molecule of myelin . MBP can interact with a number of polyanionic proteins including actin, tubulin, calmodulin, and clathrin, and negatively charged lipids, and acquires structure on binding to them. It may act as a membrane actin-binding protein, which might allow it to participate in transmission of extracellular signals to the cytoskeleton in oligodendrocytes and tight junctions in myelin. MBP may be applicable as a marker for oligodendrogliomas. Phosphorylation been shown to decrease its ability to aggregate lipid vesicles and consequently destabilising the compact structure ofmyelin, a destruction that has been observed in demyelinating diseases such as Multiple Sclerosis. MBP/4276 is a useful detector of phosphorylated MBP by binding to Thr98 of human MBP in the phosphorylated state.

Description: Myelin basic protein (MBP) is the second most abundant protein in central nervous system (CNS) myelin: it comprises 30% of the total protein and about 10% of the dry weight of myelin. It is the only structural protein found so far to be essential for formation of CNS myelin, and has been called the executive molecule of myelin . MBP can interact with a number of polyanionic proteins including actin, tubulin, calmodulin, and clathrin, and negatively charged lipids, and acquires structure on binding to them. It may act as a membrane actin-binding protein, which might allow it to participate in transmission of extracellular signals to the cytoskeleton in oligodendrocytes and tight junctions in myelin. MBP may be applicable as a marker for oligodendrogliomas. Phosphorylation been shown to decrease its ability to aggregate lipid vesicles and consequently destabilising the compact structure ofmyelin, a destruction that has been observed in demyelinating diseases such as Multiple Sclerosis. MBP/4276 is a useful detector of phosphorylated MBP by binding to Thr98 of human MBP in the phosphorylated state.

Description: Myelin basic protein (MBP) is the second most abundant protein in central nervous system (CNS) myelin: it comprises 30% of the total protein and about 10% of the dry weight of myelin. It is the only structural protein found so far to be essential for formation of CNS myelin, and has been called the executive molecule of myelin . MBP can interact with a number of polyanionic proteins including actin, tubulin, calmodulin, and clathrin, and negatively charged lipids, and acquires structure on binding to them. It may act as a membrane actin-binding protein, which might allow it to participate in transmission of extracellular signals to the cytoskeleton in oligodendrocytes and tight junctions in myelin. MBP may be applicable as a marker for oligodendrogliomas.

Description: Myelin basic protein (MBP) is the second most abundant protein in central nervous system (CNS) myelin: it comprises 30% of the total protein and about 10% of the dry weight of myelin. It is the only structural protein found so far to be essential for formation of CNS myelin, and has been called the executive molecule of myelin . MBP can interact with a number of polyanionic proteins including actin, tubulin, calmodulin, and clathrin, and negatively charged lipids, and acquires structure on binding to them. It may act as a membrane actin-binding protein, which might allow it to participate in transmission of extracellular signals to the cytoskeleton in oligodendrocytes and tight junctions in myelin. MBP may be applicable as a marker for oligodendrogliomas.

Description: Myelin basic protein (MBP) is the second most abundant protein in central nervous system (CNS) myelin: it comprises 30% of the total protein and about 10% of the dry weight of myelin. It is the only structural protein found so far to be essential for formation of CNS myelin, and has been called the executive molecule of myelin . MBP can interact with a number of polyanionic proteins including actin, tubulin, calmodulin, and clathrin, and negatively charged lipids, and acquires structure on binding to them. It may act as a membrane actin-binding protein, which might allow it to participate in transmission of extracellular signals to the cytoskeleton in oligodendrocytes and tight junctions in myelin. MBP may be applicable as a marker for oligodendrogliomas.

Description: Myelin basic protein (MBP) is the second most abundant protein in central nervous system (CNS) myelin: it comprises 30% of the total protein and about 10% of the dry weight of myelin. It is the only structural protein found so far to be essential for formation of CNS myelin, and has been called the executive molecule of myelin . MBP can interact with a number of polyanionic proteins including actin, tubulin, calmodulin, and clathrin, and negatively charged lipids, and acquires structure on binding to them. It may act as a membrane actin-binding protein, which might allow it to participate in transmission of extracellular signals to the cytoskeleton in oligodendrocytes and tight junctions in myelin. MBP may be applicable as a marker for oligodendrogliomas.

Description: Myelin basic protein (MBP) is the second most abundant protein in central nervous system (CNS) myelin: it comprises 30% of the total protein and about 10% of the dry weight of myelin. It is the only structural protein found so far to be essential for formation of CNS myelin, and has been called the executive molecule of myelin . MBP can interact with a number of polyanionic proteins including actin, tubulin, calmodulin, and clathrin, and negatively charged lipids, and acquires structure on binding to them. It may act as a membrane actin-binding protein, which might allow it to participate in transmission of extracellular signals to the cytoskeleton in oligodendrocytes and tight junctions in myelin. MBP may be applicable as a marker for oligodendrogliomas.

Description: Myelin basic protein (MBP) is the second most abundant protein in central nervous system (CNS) myelin: it comprises 30% of the total protein and about 10% of the dry weight of myelin. It is the only structural protein found so far to be essential for formation of CNS myelin, and has been called the executive molecule of myelin . MBP can interact with a number of polyanionic proteins including actin, tubulin, calmodulin, and clathrin, and negatively charged lipids, and acquires structure on binding to them. It may act as a membrane actin-binding protein, which might allow it to participate in transmission of extracellular signals to the cytoskeleton in oligodendrocytes and tight junctions in myelin. MBP may be applicable as a marker for oligodendrogliomas.