产品名称
Anti-Amyloid beta fibrils, clone M98, Rabbit Monoclonal Antibody, clone M98, from rabbit
isotype
IgGκ
technique(s)
western blot: suitable
dot blot: suitable
immunohistochemistry: suitable
biological source
rabbit
antibody form
purified antibody
antibody product type
primary antibodies
clone
M98, monoclonal
species reactivity
human
species reactivity (predicted by homology)
chicken (based on 100% sequence homology), bovine (based on 100% sequence homology), rabbit (based on 100% sequence homology)
NCBI accession no.
UniProt accession no.
shipped in
wet ice
target post-translational modification
unmodified
Gene Information
human ... APP(351)
Analysis Note
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.
Dot Blot Analysis: 0.1 µg/mL of this antibody detected Amyloid beta fibrils in 0.075 µg of Synthetic Abeta40.
Application
Research Category
Neuroscience
Neuroscience
Research Sub Category
Developmental Signaling
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).
Immunohistochemistry Analysis: A representative lot detected Amyloid beta fibrils in Frontal cortex of AD patients (Data courtesy of Prof. C. Glabe, UCI).
Biochem/physiol Actions
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.
Disclaimer
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.
General description
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.
Immunogen
Corresponding to the Beta Amyloid Protein 42 (residue 2-7) of human Amyloid beta fibrils.
Epitope: Beta Amyloid Protein 42 (residue 2-7)
Other Notes
Concentration: Please refer to lot specific datasheet.
Physical form
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.
Preparation Note
Stable for 1 year at 2-8°C from date of receipt.
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存储类别
12 - Non Combustible Liquids
wgk
WGK 1
flash_point_f
Not applicable
flash_point_c
Not applicable
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
Hemraj B Dodiya et al.
The Journal of experimental medicine, 219(1) (2021-12-03)
We previously demonstrated that lifelong antibiotic (ABX) perturbations of the gut microbiome in male APPPS1-21 mice lead to reductions in amyloid β (Aβ) plaque pathology and altered phenotypes of plaque-associated microglia. Here, we show that a short, 7-d treatment 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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