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MABN687 Anti-β-amyloid fibril-specific, clone B10, AP Antibody

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MABN687
200 µL  
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      Descripción

      Replacement Information

      Ofertas especiales

      Tabla espec. clave

      Species ReactivityKey ApplicationsHostFormatAntibody Type
      HIHC, DB, ELISA, IP, IFCamelAlkaline PhosphataseMonoclonal Antibody
      Description
      Catalogue NumberMABN687
      DescriptionAnti-β-amyloid fibril-specific, clone B10, AP Antibody
      Alternate Names
      • Amyloid beta A4 protein
      • ABPP
      • APPI
      • APP
      • Alzheimer disease amyloid protein
      • Cerebral vascular amyloid peptide
      • CVAP
      • PreA4
      • Protease nexin-II
      • PN-II
      • N-APP2.Soluble APP-alpha
      • S-APP-alpha
      • Soluble APP-beta
      • S-APP-beta
      • C99
      • Beta-amyloid protein 42
      • Beta-APP42
      • Beta-amyloid protein 40
      • Beta-PP40
      • C83
      • P3(42)
      • P3(40)
      • C80
      • Gamma-secretase C-terminal fragment 59
      • Amyloid intracellular domain 59
      • AICD-59
      • AID(59)
      • Gamma-CTF(59)
      • Gamma-secretase C-terminal fragment 57
      • Amyloid intracellular domain 57
      • AICD-57
      • AID(57)
      • Gamma-CTF(57)
      • Gamma-secretase C-terminal fragment 50
      • Amyloid intracellular domain 50
      • AICD-50
      • AID(50)
      • Gamma-CTF(50)
      • C31
      Background InformationAmyloid fibrils are naturally occurring polypeptide scaffolds with considerable importance for human health and disease. A recombinant antibody domain fragment termed B10 specifically recognizes an amyloid-specific and conformationally defined epitope. The specificity and conformational specificity have been established by various methods, including, surface plasmon resonance, immunoblots, and immunohistochemistry. All these methods demonstrate that this antibody domain fragment distinguishes Aβ amyloid fibrils from disaggregated Aβ peptide as well as from specific Aβ oligomers. The antibody domain also possesses functional activity in preventing the formation of mature amyloid fibrils by stabilizing Aβ protofibrils, and recent data suggests that the B10 antibody fragment selectively binds to Alzheimer's Aβ(1-40) amyloid fibrils and that fibril recognition depends on positively charged residues within the B10 antigen binding site. Mutation or alternation of specific residues changes B10’s interactions with various fibril configurations, implying that the B10 conformational specificity for amyloid fibrils depends upon specific electrostatic interactions with an acidic moiety, which is common to different amyloid fibrils.
      References
      Product Information
      FormatAlkaline Phosphatase
      PresentationPurified Camelid monoclonal IgG in buffer containing 20mM NaH2PO4, 175mM NaCl, pH8.0 without preservatives.
      Note: This is a Camelid antibody fused to an alkaline phosphatase and does not require a secondary antibody for detection.
      Quality LevelMQ100
      Applications
      ApplicationAnti-β-amyloid fibril-specific, clone B10, AP | MABN687 is an antibody against β-amyloid fibril-specific for use in Immunohistochemistry, Dot Blot, ELISA, Immunoprecipitation, Immunofluorescence.
      Key Applications
      • Immunohistochemistry
      • Dot Blot
      • ELISA
      • Immunoprecipitation
      • Immunofluorescence
      Application NotesThis is a Camelid antibody fused to an alkaline phosphatase and does not require a secondary antibody for detection.
      Dot Blot Analysis: A representative lot detected β-amyloid fibril-specific in synthetic Aβ (1–40) peptide (Habicht, G., et al. (2007). PNAS. 104(49):19232-19237).
      Dot Blot Analysis: A representative lot detected β-amyloid fibril-specific in chemically modified fibrils (Haupt, C., et al. (2011). J. Mol. Biol. 405:341-348).
      Elisa Analysis: A representative lot detected β-amyloid fibril-specific in N-biotinylated Aβ (1–40) conformers (disaggregated peptide, oligomers, or fibrils) (Morgado, I., et al. (2012). PNAS. 109(31):12503-12508).
      Immunohistochemistry Analysis: A representative lot detected β-amyloid fibril-specific in Hippocampal sections from Alzheimer brain tissue (Habicht, G., et al. (2007). PNAS. 104(49):19232-19237).
      Immunoprecipitation Analysis: A representative lot detected β-amyloid fibril-specific in native soluble and dispersible fractions from the brain lysates (Upadhaya, A.R., et al. (2012). J. Cell. Mol. Med. 16(2):287-295).
      Immunofluorescence Analysis: A representative lot detected β-amyloid fibril-specific in cell culture-derived amyloid plaques (Habicht, G., et al. (2007). PNAS. 104(49):19232-19237).
      Biological Information
      Epitope AB (1-40) amyloid fibrils
      CloneB10
      ConcentrationPlease refer to lot specific datasheet.
      HostCamel
      IsotypeIgG
      Species Reactivity
      • Human
      Antibody TypeMonoclonal Antibody
      Entrez Gene Number
      Gene Symbol
      • APP
      • A4
      • AD1
      Purification MethodNi-NTA agarose beads and Mono Q column
      UniProt Number
      Physicochemical Information
      Dimensions
      Materials Information
      Toxicological Information
      Safety Information according to GHS
      Safety Information
      Product Usage Statements
      Quality AssuranceEvaluated by Immunohistochemistry in human Alzheimer's brain tissue.

      Immunohistochemistry Analysis: A 1:50 dilution of this antibody detected β-amyloid fibril-specific in human Alzheimer's brain tissue.
      Usage Statement
      • Unless otherwise stated in our catalog or other company documentation accompanying the product(s), our products are intended for research use only and are not to be used for any other purpose, which includes but is not limited to, unauthorized commercial uses, in vitro diagnostic uses, ex vivo or in vivo therapeutic uses or any type of consumption or application to humans or animals.
      Storage and Shipping Information
      Storage ConditionsStable for 1 year at -20°C from date of receipt.
      Handling Recommendations: Upon receipt and prior to removing the cap, centrifuge the vial and gently mix the solution. Aliquot into microcentrifuge tubes and store at -20°C. Avoid repeated freeze/thaw cycles, which may damage IgG and affect product performance.
      Packaging Information
      Material Size200 µL
      Transport Information
      Supplemental Information
      Specifications
      Global Trade Item Number
      Número de referencia GTIN
      MABN687 04055977126495

      Documentation

      Anti-β-amyloid fibril-specific, clone B10, AP Antibody Ficha datos de seguridad (MSDS)

      Título

      Ficha técnica de seguridad del material (MSDS) 

      Anti-β-amyloid fibril-specific, clone B10, AP Antibody Certificados de análisis

      CargoNúmero de lote
      Anti-β-amyloid fibril-specific, clone B10, AP - 3438032 3438032
      Anti-β-amyloid fibril-specific, clone B10, AP - 3782209 3782209
      Anti-β-amyloid fibril-specific, clone B10, AP -Q2499608 Q2499608
      Anti-β-amyloid fibril-specific, clone B10, AP Monoclonal Antibody 2950520

      Referencias bibliográficas

      Visión general referenciasPub Med ID
      Proceedings of the National Academy of Sciences of the United States of America
      Morgado, I; Wieligmann, K; Bereza, M; Rönicke, R; Meinhardt, K; Annamalai, K; Baumann, M; Wacker, J; Hortschansky, P; Malešević, M; Parthier, C; Mawrin, C; Schiene-Fischer, C; Reymann, KG; Stubbs, MT; Balbach, J; Görlach, M; Horn, U; Fändrich, M
      Proceedings of the National Academy of Sciences of the United States of America  109  12503-8  2011

      Mostrar resumen
      22814377 22814377
      Journal of molecular biology
      Haupt, C; Morgado, I; Kumar, ST; Parthier, C; Bereza, M; Hortschansky, P; Stubbs, MT; Horn, U; Fändrich, M
      Journal of molecular biology  405  341-8  2010

      Mostrar resumen
      21059358 21059358
      Proceedings of the National Academy of Sciences of the United States of America
      Habicht, G; Haupt, C; Friedrich, RP; Hortschansky, P; Sachse, C; Meinhardt, J; Wieligmann, K; Gellermann, GP; Brodhun, M; Götz, J; Halbhuber, KJ; Röcken, C; Horn, U; Fändrich, M
      Proceedings of the National Academy of Sciences of the United States of America  104  19232-7  2007

      Mostrar resumen
      18042730 18042730