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MABN640

Sigma-Aldrich

Anti-Amyloid beta fibrils, clone M98, Rabbit Monoclonal Antibody

clone M98, from rabbit

Sinónimos:

Amyloid Beta, Amyloid B, 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, C995.Bet

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About This Item

Código UNSPSC:
12352203
eCl@ss:
32160702
NACRES:
NA.41
clon:
M98, monoclonal
application:
DB
IHC
WB
reactividad de especies:
human
técnicas:
dot blot: suitable
immunohistochemistry: suitable
western blot: suitable
citations:
3

origen biológico

rabbit

forma del anticuerpo

purified antibody

tipo de anticuerpo

primary antibodies

clon

M98, monoclonal

reactividad de especies

human

reactividad de especies (predicha por homología)

chicken (based on 100% sequence homology), bovine (based on 100% sequence homology), rabbit (based on 100% sequence homology)

técnicas

dot blot: suitable
immunohistochemistry: suitable
western blot: suitable

isotipo

IgGκ

Nº de acceso NCBI

Nº de acceso UniProt

Condiciones de envío

wet ice

modificación del objetivo postraduccional

unmodified

Información sobre el gen

human ... APP(351)

Descripción general

The protein named Amyloid beta A4, or ABPP, APP, APPI, Alzheimer disease amyloid protein, Cerebral vascular amyloid peptide, CVAP, PreA4, or Protease nexin II (PN-II) protein and encoded by human gene A4/AD1 is a precursor to 14 peptides some of which are associated with neurological disease such as Alzheimer′s Disease. In pathological conditions Amyloid beta A4 protein is the precursor for the disease associated proteins, Beta amyloid 40, and Beta amyloid 42, major components of plaques in Alzheimer’s Disease. Normally APP plays a role in neuronal development and mediates aspects of axonal transport as well as neurite outgrowth. It is also involved in copper homeostasis/oxidative stress through copper ion reduction in neurons. Amyloid Beta A4 protein is localized to the plasma membrane and Golgi complex until cleaved. Amyloid Beta A4 protein is normally expressed in all fetal tissues and in the adult, frontal cortex expression predominates although there are isoforms widely expressed in non-neuronal cells as well. Normally, amyloid beta A4 is proteolytically processed and the cleavage and secretion of fragments are non-amyloidogenic. However under presenilin/nicastrin mediated processing of the C99 fragment releases beta amyloid proteins that are associated with neurological disease. MABN640 recognizes a specific conformation of residues 2-7 of the amyloid Aß peptide sequence (AEFRHD) found in amyloid fibrils. It does not detectably react with APP, IAPP, a-synuclein or polyQ fibrils A different antibody MABN637, recognizes a specific conformation of residues 3-6 of the amyloid Aß peptide sequence (EFRH) found in amyloid fibrils. It does not recognize pyroglutamyl Aß at residue 3 (1). MABN640 displays a distinct specificity from MABN638 on dot blots of Aß preparations (1). It also reacts with polyQ40 fibrils but not monomers, indicating that it recognizes a generic, sequence independent epitope.

Especificidad

MABN640 recognizes a specific conformation of residues 2-7 of the amyloid Aß peptide sequence (AEFRHD) found in amyloid fibrils. It does not detectably react with APP, IAPP, a-synuclein or polyQ fibrils (Hatami et al., manuscript in preparation). This antibody reconizes both Abeta40 and ABeta42.
Other homologies: Broad species cross-reactivity is expected.

Inmunógeno

Corresponding to the Beta Amyloid Protein 42 (residue 2-7) of human Amyloid beta fibrils.
Epitope: Beta Amyloid Protein 42 (residue 2-7)

Aplicación

Research Category
Neuroscience
Research Sub Category
Developmental Signaling
This Anti-Amyloid beta fibrils, clone M98, Rabbit Monoclonal Antibody is validated for use in Dot Blot and Western Blotting and Immunohistochemistry for the detection of Amyloid beta fibrils.
Western Blotting Analysis: 0.1 µg/mL from a representative lot detected Amyloid beta fibrils in Abeta42 aggregates (Data courtesy of Prof. C. Glabe, UCI).
Immunohistochemistry Analysis: A representative lot detected Amyloid beta fibrils in Frontal cortex of AD patients (Data courtesy of Prof. C. Glabe, UCI).

Calidad

Evaluated by Dot Blot in Synthetic Abeta40.

Dot Blot Analysis: 0.1 µg/mL of this antibody detected Amyloid beta fibrils in 0.075 µg of Synthetic Abeta40.

Forma física

Format: Purified
Protein A purified
Purified rabbit monoclonal IgGκ in buffer containing 0.1 M Tris-Glycine (pH 7.4), 150 mM NaCl with 0.05% sodium azide.

Almacenamiento y estabilidad

Stable for 1 year at 2-8°C from date of receipt.

Otras notas

Concentration: Please refer to lot specific datasheet.

Cláusula de descargo de responsabilidad

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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Opcional

Referencia del producto
Descripción
Precios

Código de clase de almacenamiento

12 - Non Combustible Liquids

Clase de riesgo para el agua (WGK)

WGK 1

Punto de inflamabilidad (°F)

Not applicable

Punto de inflamabilidad (°C)

Not applicable


Certificados de análisis (COA)

Busque Certificados de análisis (COA) introduciendo el número de lote del producto. Los números de lote se encuentran en la etiqueta del producto después de las palabras «Lot» o «Batch»

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Aaron T Balana et al.
Nature chemistry, 13(5), 441-450 (2021-03-17)
A major role for the intracellular post-translational modification O-GlcNAc appears to be the inhibition of protein aggregation. Most of the previous studies in this area focused on O-GlcNAc modification of the amyloid-forming proteins themselves. Here we used synthetic protein chemistry
Positron emission tomography imaging of fibrillar parenchymal and vascular amyloid-? in TgCRND8 mice.
McLean, Daniel, et al.
ACS Chemical Neuroscience, 4, 613-623 (2013)
Justin M Nussbaum et al.
Nature, 485(7400), 651-655 (2012-06-05)
Extracellular plaques of amyloid-β and intraneuronal neurofibrillary tangles made from tau are the histopathological signatures of Alzheimer's disease. Plaques comprise amyloid-β fibrils that assemble from monomeric and oligomeric intermediates, and are prognostic indicators of Alzheimer's disease. Despite the importance of
Fuyan Chen et al.
Experimental and therapeutic medicine, 20(5), 88-88 (2020-09-26)
Alzheimer's disease (AD), the leading cause of age-related dementia, is characterized by abnormal β-amyloid accumulation. During learning, memory formation and consolidation, increased levels of histone H3 and H4 acetylation are observed. The present study reported significantly decreased level of H4K16ac

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