MABN1839
Anti-Amyloid-β (oligomer) Antibody, clone F11G3
clone F11G3, from mouse
Synonyme(s) :
Amyloid beta oligomer, Abeta oligomer, alpha-synuclein oligomer,, alpha-syn oligomer, Prion protein oligomer, PrP oligomer, TAR DNA-binding protein 43 oligomer, TDP-43 oligomer, Tau oligomer
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About This Item
Code UNSPSC :
12352203
eCl@ss :
32160702
Nomenclature NACRES :
NA.41
Produits recommandés
Source biologique
mouse
Niveau de qualité
Forme d'anticorps
purified immunoglobulin
Type de produit anticorps
primary antibodies
Clone
F11G3, monoclonal
Espèces réactives
all, human, mouse
Technique(s)
ELISA: suitable
dot blot: suitable
immunofluorescence: suitable
immunoprecipitation (IP): suitable
western blot: suitable
Isotype
IgMκ
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) , PRNP(5621) , SNCA(6622) , TARDBP(23435)
Description générale
Accumulations of insoluble deposits/aggregates are the hallmarks of several neurodegenerative diseases. Deposits involving Aβ and tau proteins in Alzheimer′s disease (AD), α-synuclein (α-syn) in Parkinson′s disease (PD), prion protein (PrP) in prion diseases (PrD), TAR DNA-binding protein 43 (TDP-43) in amyotrophic lateral sclerosis (ALS) and frontotemporal lobar dementia-TDP (FTLD-TDP) are well known examples. Evidence suggests that oligomers represent the more toxic species than fibrillar deposits in neurodegenerative conditions, such as AD, PD, and PrD. The number of Aβ deposits, for example, correlates poorly with disease progression, and many researchers consider them to be inert or even protective. Antibodies targeting beta-sheet oligomer conformations are being developed not only to study neurotoxic oligomers, but also for diagnostic and therapeutic purposes.
Spécificité
Clone F11G3 was raised against collodial gold particles coated with a synthetic peptide, Prp-G, whose sequence corresponds to an unstructured region of prion protein (Prp) with Met-to-Gly point mutations, as a beta-sheet oligomer mimetic (Guerrero-Muñoz, M.J., et al. (2013). ACS Chem. Neurosci. 4(12):1520-1523). Clone F11G3 recognizes oligomeric, but not monomeric or fibrillar, forms of Aβ42, α-syn, PrP, TDP-43, and polyQ Ataxin-1, as well as the misfolded oligomeric proteins in human AD brain samples (Lasagna-Reeves, C.A., et al. (2015). eLlife. 4:e07558; Guerrero-Muñoz, M.J., et al. (2014). Neurobiol. Dis.71:14-23).
Target conformation is not species-specific.
Immunogène
Colloidal gold-conjugated Prp-G.
Application
Immunofluorescence Analysis: A representative lot specifically detected amyloid beta-sheet oligomer immunoreactivity in paraffin-embedded brain sections from Alzheimer′s diseased (AD), but not non-AD human brain by fluorescent immunohistochemistry (Courtesy of Dr. Rakez Kayed, University of Texas Medical Branch, Galveston, TX).
Western Blotting Analysis: A representative lot detected Ataxin-1 oligomers in soluble cerebella extracts from Atxn1154Q/+, but not wild-type or Atxn-/-, mice (Lasagna-Reeves, C.A., et al. (2015). eLlife. 4:e07558).
Western Blotting Analysis: A representative lot detected cellular beta-sheet oligomer immunoreactivity in HeLa cells transfected with the pathogenic (82Q), but not the non-pathogenic (30Q) form of polyQ Ataxin-1 in transfected Hela cells. Co-transfecting with the native Atxn-1 binding partner Capicua (CIC), but not the binding defective CIC W37A mutant, enhanced the oligomer formation (Lasagna-Reeves, C.A., et al. (2015). eLlife. 4:e07558).
Western Blotting Analysis: A representative lot detected the highest extend of oligomers accumulation in the soluble cerebella extracts among the 28-week old Atxn1154Q/+ mice when compared with samples from 18-week old and 8-week old Atxn1154Q/+ mice, with the 8-week old mice bearing the least oligomer buildup (Lasagna-Reeves, C.A., et al. (2015). eLlife. 4:e07558).
Western Blotting Analysis: A representative lot specifically detected oligomeric, but not monomeric or fibrillar, forms of Aβ42, α-Syn, PrP, and TDP-43 (Guerrero-Muñoz, M.J., et al. (2014). Neurobiol. Dis.71:14-23).
App3/DB/ A representative lot specifically detected oligomeric, but not monomeric or fibrillar, forms of Aβ42, α-Syn, PrP, and TDP-43 (Guerrero-Muñoz, M.J., et al. (2014). Neurobiol. Dis.71:14-23).
ELISA Analysis: A representative lot detected in vitro Aβ42, α-Syn, PrP, and TDP-43 oligomers formation with or without Aβ42 oligomer seeding (Guerrero-Muñoz, M.J., et al. (2014). Neurobiol. Dis.71:14-23).
Immunofluorescence Analysis: A representative lot detected a positive correlation between the ATXN1 beta-sheet oligomer immunoreactivity and the degeneration progression in calbindin-positive Purkinje cells (PCs) by fluorescent immunohistochemistry using paraffin-embedded cerebellum sections from Atxn1154Q/+ mice (Lasagna-Reeves, C.A., et al. (2015). eLlife. 4:e07558).
Immunofluorescence Analysis: A representative lot selectively detected beta-sheet oligomer immunoreactivity colocalized with those of Aβ, α-Syn, PrP, and TDP-43 in paraffin-embedded frontal cortex sections from Alzheimer′s diseased brain by fluorescent immunohistochemistry. The beta-sheet oligomer immunoreactivity is not detected in non-AD brains and is distinct from the staining pattern obtained with Thioflavin S (Guerrero-Muñoz, M.J., et al. (2014). Neurobiol. Dis.71:14-23).
Immunoprecipitation Analysis: A representative lot immunoprecipitated Ataxin-1 oligomers from the soluble cerebella extracts of Atxn1154Q/+, but not Atxn-/-, mice (Lasagna-Reeves, C.A., et al. (2015). eLlife. 4:e07558).
Immunocytochemistry Analysis: A representative lot detected cellular beta-sheet oligomer immunoreactivity in HeLa cells transfected with the pathogenic polyQ Ataxin-1 mRFP fusion construct mRFP-ATXN1(82Q) by fluorescent immunocytochemistry. Co-transfecting with the N-terminal fragment of the Atxn-1 binding partner Capicua (CIC), but not the binding defective CIC W37A mutant fragment, enhanced the oligomer formation (Lasagna-Reeves, C.A., et al. (2015). eLlife. 4:e07558).
Immunohistochemistry Analysis: A representative lot detected beta-sheet oligomer immunoreactivity in paraffin-embedded cerebellum and cortex sections of Atxn1154Q/+, but not wild-type, mice (Lasagna-Reeves, C.A., et al. (2015). eLlife. 4:e07558).
Western Blotting Analysis: A representative lot detected Ataxin-1 oligomers in soluble cerebella extracts from Atxn1154Q/+, but not wild-type or Atxn-/-, mice (Lasagna-Reeves, C.A., et al. (2015). eLlife. 4:e07558).
Western Blotting Analysis: A representative lot detected cellular beta-sheet oligomer immunoreactivity in HeLa cells transfected with the pathogenic (82Q), but not the non-pathogenic (30Q) form of polyQ Ataxin-1 in transfected Hela cells. Co-transfecting with the native Atxn-1 binding partner Capicua (CIC), but not the binding defective CIC W37A mutant, enhanced the oligomer formation (Lasagna-Reeves, C.A., et al. (2015). eLlife. 4:e07558).
Western Blotting Analysis: A representative lot detected the highest extend of oligomers accumulation in the soluble cerebella extracts among the 28-week old Atxn1154Q/+ mice when compared with samples from 18-week old and 8-week old Atxn1154Q/+ mice, with the 8-week old mice bearing the least oligomer buildup (Lasagna-Reeves, C.A., et al. (2015). eLlife. 4:e07558).
Western Blotting Analysis: A representative lot specifically detected oligomeric, but not monomeric or fibrillar, forms of Aβ42, α-Syn, PrP, and TDP-43 (Guerrero-Muñoz, M.J., et al. (2014). Neurobiol. Dis.71:14-23).
App3/DB/ A representative lot specifically detected oligomeric, but not monomeric or fibrillar, forms of Aβ42, α-Syn, PrP, and TDP-43 (Guerrero-Muñoz, M.J., et al. (2014). Neurobiol. Dis.71:14-23).
ELISA Analysis: A representative lot detected in vitro Aβ42, α-Syn, PrP, and TDP-43 oligomers formation with or without Aβ42 oligomer seeding (Guerrero-Muñoz, M.J., et al. (2014). Neurobiol. Dis.71:14-23).
Immunofluorescence Analysis: A representative lot detected a positive correlation between the ATXN1 beta-sheet oligomer immunoreactivity and the degeneration progression in calbindin-positive Purkinje cells (PCs) by fluorescent immunohistochemistry using paraffin-embedded cerebellum sections from Atxn1154Q/+ mice (Lasagna-Reeves, C.A., et al. (2015). eLlife. 4:e07558).
Immunofluorescence Analysis: A representative lot selectively detected beta-sheet oligomer immunoreactivity colocalized with those of Aβ, α-Syn, PrP, and TDP-43 in paraffin-embedded frontal cortex sections from Alzheimer′s diseased brain by fluorescent immunohistochemistry. The beta-sheet oligomer immunoreactivity is not detected in non-AD brains and is distinct from the staining pattern obtained with Thioflavin S (Guerrero-Muñoz, M.J., et al. (2014). Neurobiol. Dis.71:14-23).
Immunoprecipitation Analysis: A representative lot immunoprecipitated Ataxin-1 oligomers from the soluble cerebella extracts of Atxn1154Q/+, but not Atxn-/-, mice (Lasagna-Reeves, C.A., et al. (2015). eLlife. 4:e07558).
Immunocytochemistry Analysis: A representative lot detected cellular beta-sheet oligomer immunoreactivity in HeLa cells transfected with the pathogenic polyQ Ataxin-1 mRFP fusion construct mRFP-ATXN1(82Q) by fluorescent immunocytochemistry. Co-transfecting with the N-terminal fragment of the Atxn-1 binding partner Capicua (CIC), but not the binding defective CIC W37A mutant fragment, enhanced the oligomer formation (Lasagna-Reeves, C.A., et al. (2015). eLlife. 4:e07558).
Immunohistochemistry Analysis: A representative lot detected beta-sheet oligomer immunoreactivity in paraffin-embedded cerebellum and cortex sections of Atxn1154Q/+, but not wild-type, mice (Lasagna-Reeves, C.A., et al. (2015). eLlife. 4:e07558).
Research Category
Neuroscience
Neuroscience
Research Sub Category
Neurodegenerative Diseases
Neurodegenerative Diseases
This Anti-Amyloid-β (oligomer) Antibody, clone F11G3 is validated for use in Western Blotting, Dot Blot, ELISA, Immunofluorescence, Immunoprecipitation for the detection of Amyloid-β.
Qualité
Evaluated by Western Blotting of oligomeric amyloid.
Western Blotting Analysis: 2.0 µg/mL of this antibody detected 10 µg of oligomeric amyloid.
Western Blotting Analysis: 2.0 µg/mL of this antibody detected 10 µg of oligomeric amyloid.
Description de la cible
Variable, depending on the sizes and the species of the oligomers formed.
Forme physique
Format: Purified
Protein A purified
Purified mouse monoclonal IgMκ antibody in PBS without preservatives.
Stockage et stabilité
Stable 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.
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.
Autres remarques
Concentration: Please refer to lot specific datasheet.
Clause de non-responsabilité
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.
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Réf. du produit
Description
Tarif
Code de la classe de stockage
12 - Non Combustible Liquids
Classe de danger pour l'eau (WGK)
WGK 2
Point d'éclair (°F)
Not applicable
Point d'éclair (°C)
Not applicable
Certificats d'analyse (COA)
Recherchez un Certificats d'analyse (COA) en saisissant le numéro de lot du produit. Les numéros de lot figurent sur l'étiquette du produit après les mots "Lot" ou "Batch".
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Chuang Guo et al.
Scientific reports, 6, 29396-29396 (2016-07-14)
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Notre équipe de scientifiques dispose d'une expérience dans tous les secteurs de la recherche, notamment en sciences de la vie, science des matériaux, synthèse chimique, chromatographie, analyse et dans de nombreux autres domaines..
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