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Key Documents

MABN687

Sigma-Aldrich

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

clone B10, from camel, alkaline phosphatase conjugate

Synonyme(s) :

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

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About This Item

Code UNSPSC :
12352203
eCl@ss :
32160702
Nomenclature NACRES :
NA.41

Source biologique

camel

Niveau de qualité

Conjugué

alkaline phosphatase conjugate

Forme d'anticorps

purified immunoglobulin

Type de produit anticorps

primary antibodies

Clone

B10, monoclonal

Espèces réactives

human

Technique(s)

ELISA: suitable
dot blot: suitable
immunofluorescence: suitable
immunohistochemistry: suitable
immunoprecipitation (IP): suitable

Isotype

IgG

Numéro d'accès NCBI

Numéro d'accès UniProt

Conditions d'expédition

dry ice

Modification post-traductionnelle de la cible

unmodified

Informations sur le gène

human ... APP(351)

Description générale

Amyloid 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.

Immunogène

Epitope: AB (1-40) amyloid fibrils

Application

Anti-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.
This 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. Mole. 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. (2014). BRAIN. 1-17).
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).

Qualité

Evaluated 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.

Forme physique

Ni-NTA agarose beads and Mono Q column
Purified 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.

Autres remarques

Concentration: Please refer to lot specific datasheet.

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Code de la classe de stockage

12 - Non Combustible Liquids

Classe de danger pour l'eau (WGK)

nwg


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Consulter la Bibliothèque de documents

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 et al.
Proceedings of the National Academy of Sciences of the USA null
Christian Haupt et al.
Journal of molecular biology, 405(2), 341-348 (2010-11-10)
Amyloid fibrils are naturally occurring polypeptide scaffolds with considerable importance for human health and disease. These supermolecular assemblies are β-sheet rich and characterized by a high structural order. Clinical diagnosis and emerging therapeutic strategies of amyloid-dependent diseases, such as Alzheimer's
Proceedings of the National Academy of Sciences of the United States of America
Morgado, I; Wieligmann, K; Bereza, M; Ronicke, R; Meinhardt, K; Annamalai, K; Baumann et al.
Proceedings of the National Academy of Sciences of the USA null

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