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Purified anti-mouse/rat β-Amyloid Antibody (Previously Covance catalog# SIG-39153)

Pricing & Availability
Clone
Poly18058 (See other available formats)
Regulatory Status
RUO
Other Names
AAA, ABETA, ABPP, AD1, APPI, CTFgamma, CVAP, PN-II, PN2, Amyloid beta A4 protein, preA4, protease nexin-II, peptidase nexin-II, beta-amyloid peptide, alzheimer disease amyloid protein, cerebral vascular amyloid peptide, APP, Amyloid Precursor Protein
Previously
Signet Catalog# 9153-005
Covance Catalog# SIG-39153
Isotype
Rabbit Polyclonal IgG
Ave. Rating
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Product Citations
publications
Poly18058_PURE_beta-Amyloid_2_011020_update.png
Western blot of purified anti-mouse/rat β-Amyloid antibody (Poly18058). Lane 1: Molecular weight marker; Lane 2: 20 µg of human brain lysate; Lane 3: 20 µg of mouse brain lysate; Lane 4: 20 µg of rat brain lysate. The blot was incubated with 1 µg/mL of the primary antibody overnight at 4°C, followed by incubation with HRP donkey anti-rabbit IgG antibody (Cat. No. 406401). Enhanced chemiluminescence was used as the detection system.
  • Poly18058_PURE_beta-Amyloid_2_011020_update.png
    Western blot of purified anti-mouse/rat β-Amyloid antibody (Poly18058). Lane 1: Molecular weight marker; Lane 2: 20 µg of human brain lysate; Lane 3: 20 µg of mouse brain lysate; Lane 4: 20 µg of rat brain lysate. The blot was incubated with 1 µg/mL of the primary antibody overnight at 4°C, followed by incubation with HRP donkey anti-rabbit IgG antibody (Cat. No. 406401). Enhanced chemiluminescence was used as the detection system.
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805801 50 µg 524€
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Description

Amyloid beta (Aβ or Amyloid beta) denotes peptides of 36-43 amino acids in length that are crucially involved in Alzheimer's disease as the main component of the amyloid plaques found in the brains of Alzheimer patients. The peptides result from the amyloid precursor protein (APP), which is cut by certain enzymes to yield Aβ. Aβ molecules can aggregate to form oligomers (known as "seeds") which are believed to be able to induce other Aβ molecules to also take the misfolded oligomeric form, leading to a chain reaction akin to a prion infection. The seeds or the resulting amyloid plaques are toxic to nerve cells. The other protein implicated in Alzheimer's disease, tau protein, also forms such prion-like misfolded oligomers, and there is some evidence that misfolded Aβ can induce tau to misfold.

Product Details
Technical Data Sheet (pdf)

Product Details

Verified Reactivity
Mouse, Rat
Antibody Type
Polyclonal
Host Species
Rabbit
Formulation
Phosphate-buffered solution (no preservatives or carrier proteins).
Preparation
The antibody was purified by affinity chromatography.
Concentration
1.0 mg/mL
Storage & Handling
Do not store antibody diluted below 50 µg/mL in the absence of protein (i.e.: add 2% of bovine serum albumin). The antibody solution should be stored undiluted between 2°C and 8°C. Please note the storage condition for this antibody has been changed from -20°C to between 2°C and 8°C. You can also check your vial or your CoA to find the most accurate storage condition for this antibody.
Application

WB - Quality tested
ELISA - Reported in the literature, not verified in house
Recommended Usage

Each lot of this antibody is quality control tested by western blotting. For western blotting, the suggested use of this reagent is 1.0 - 10.0 µg/mL. It is recommended that the reagent be titrated for optimal performance for each application.

Application Notes

This antibody is specific for the rodent Aß. The rabbit anti-rodent Aß reacts extremely well with all isoforms. The rabbit anti-rodent Aß antibody has negligible cross-reactivity to human Aß using immunohistochemistry.

This product may contain other non-IgG subtypes.

Application References
  1. Rose C, et al. 2012. BMC Neurosci. 13:84. (WB) PubMed
  2. Suon S, et al. 2010. Mol. NEurodegener. 5:44. (ELISA) PubMed
  3. Liu M, et al. 2010. J. Lipid Res. 9:2611. (ELISA) PubMed
Product Citations
  1. Liu M, et al. 2010. J Lipid Res. 51:2611-2618. PubMed
  2. Welch G, et al. 2022. Sci Adv. 8:eabo4662. PubMed
  3. Prox J, et al. 2013. J Neurosci. 33:12915-12928. PubMed
  4. Fowler AJ, et al. 2019. Drugs R D. 19:149. PubMed
  5. Suon S, et al. 2010. Mol Neurodegener. 5:44. PubMed
  6. Rose C, et al. 2012. BMC Neurosci. 13:84. PubMed
RRID
AB_2564689 (BioLegend Cat. No. 805801)

Antigen Details

Structure
Amyloid precursor protein is a 770 amino acid protein with a molecular mass of ~100 kD. According to the UniProtKB database, APP (ID# P05067) has 11 isoforms (34 to ~90 kD) and the 770 form has been designated as the canonical form. Isoform APP695 is the predominant form expressed in neuronal tissue. Isoforms APP751 and APP770 are widely expressed in non-neuronal cells. Isoform APP751 is the most abundant form in T-lymphocytes. Aβ denotes peptides of 36-43 amino acids generated from cleavage of APP by secretases. Aβ has an apparent molecular mass of about 4 kD.
Distribution

Tissue distribution: Primarily nervous system, but also adipose tissue, intestine, and muscle.
Cellular distribution: Cytosol, endosomes, nucleus, plasma membrane, extracellular, and Golgi apparatus.

Function
The normal function of Aβ is not well understood. Several potential physiological roles have been proposed, including: activation of kinase enzymes; protection against oxidative stress; regulation of cholesterol transport; transcription factor, and as an anti-microbial agent.
Biology Area
Cell Biology, Neurodegeneration, Neuroscience, Protein Misfolding and Aggregation
Molecular Family
APP/β-Amyloid
Antigen References
  1. Kumar A, et al. 2015. Pharmacol. Rep. 67(2):195.
  2. Sadigh-Eteghad S, et al. 2015. Med. Princ. Pract. 24(1):1
  3. Hampel H, et al. 2015. Expert Rev. Neurother. 15(1):83.
  4. Puig KL, et al. 2012.  Exp. Gerontol. 48(7): 608.
  5. Selkoe DJ, et al. 2016. EMBO Mol. Med. 8(6):595.
  6. Walsh DM, et al.  2007. J. Neurochem. 101(5):1172.
Gene ID
351 View all products for this Gene ID
UniProt
View information about beta-Amyloid on UniProt.org

Related FAQs

There are no FAQs for this product.
Go To Top Version: 4    Revision Date: 01/10/2020

For research use only. Not for diagnostic use. Not for resale. BioLegend will not be held responsible for patent infringement or other violations that may occur with the use of our products.

 

*These products may be covered by one or more Limited Use Label Licenses (see the BioLegend Catalog or our website, www.biolegend.com/ordering#license). BioLegend products may not be transferred to third parties, resold, modified for resale, or used to manufacture commercial products, reverse engineer functionally similar materials, or to provide a service to third parties without written approval of BioLegend. By use of these products you accept the terms and conditions of all applicable Limited Use Label Licenses. Unless otherwise indicated, these products are for research use only and are not intended for human or animal diagnostic, therapeutic or commercial use.

 

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This data display is provided for general comparisons between formats.
Your actual data may vary due to variations in samples, target cells, instruments and their settings, staining conditions, and other factors.
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