MABN1839

Anti-Amyloid-β (oligomer) Antibody, clone F11G3

clone F11G3, from mouse

• 別名: 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
• UNSPSCコード: 12352203
• eCl@ss: 32160702
• NACRES: NA.41

特性

• 由来生物: mouse
• 品質水準: 100
• 抗体製品の状態: purified immunoglobulin
• 抗体製品タイプ: primary antibodies
• クローン: F11G3, monoclonal
• 化学種の反応性: all, human, mouse
• テクニック: ELISA: suitable; dot blot: suitable; immunofluorescence: suitable; immunoprecipitation (IP): suitable; western blot: suitable
• アイソタイプ: IgMκ
• NCBIアクセッション番号: NM_000311.3
• UniProtアクセッション番号: P04156
• 輸送温度: dry ice
• ターゲットの翻訳後修飾: unmodified
• 遺伝子情報: human ... APP(351) , PRNP(5621) , SNCA(6622) , TARDBP(23435)

詳細

詳細

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.

特異性

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.

免疫原

Colloidal gold-conjugated Prp-G.

アプリケーション

Research Category
ニューロサイエンス

Research Sub Category
神経変性疾患

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).

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.

品質

Evaluated by Western Blotting of oligomeric amyloid.

Western Blotting Analysis: 2.0 µg/mL of this antibody detected 10 µg of oligomeric amyloid.

ターゲットの説明

Variable, depending on the sizes and the species of the oligomers formed.

物理的形状

Protein A purified

Format: Purified

Purified mouse monoclonal IgMκ antibody in PBS without preservatives.

保管および安定性

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.

その他情報

Concentration: Please refer to lot specific datasheet.

免責事項

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.

安全性情報

• 保管分類コード: 12 - Non Combustible Liquids
• WGK: WGK 2
• 引火点(°F): Not applicable
• 引火点(℃): Not applicable