MABN687
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
Sign Into View Organizational & Contract Pricing
All Photos(1)
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).
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.
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.
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.
Not finding the right product?
Try our Product Selector Tool.
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’.
Already Own This Product?
Find documentation for the products that you have recently purchased in the Document Library.
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
Our team of scientists has experience in all areas of research including Life Science, Material Science, Chemical Synthesis, Chromatography, Analytical and many others.
Contact Technical Service