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MABN687

Sigma-Aldrich

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

clone B10, from camel, alkaline phosphatase conjugate

Synonym(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

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

biological source

camel

Quality Level

conjugate

alkaline phosphatase conjugate

antibody form

purified immunoglobulin

antibody product type

primary antibodies

clone

B10, monoclonal

species reactivity

human

technique(s)

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

isotype

IgG

NCBI accession no.

UniProt accession no.

shipped in

dry ice

target post-translational modification

unmodified

Gene Information

human ... APP(351)

General description

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.

Immunogen

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).

Quality

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.

Physical form

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.

Other Notes

Concentration: Please refer to lot specific datasheet.

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Storage Class Code

12 - Non Combustible Liquids

WGK

nwg


Certificates of Analysis (COA)

Search for Certificates of Analysis (COA) by entering the products Lot/Batch Number. Lot and Batch Numbers can be found on a product’s label following the words ‘Lot’ or ‘Batch’.

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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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