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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 654 CHF
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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
This antibody should be handled aseptically as it is free of preservatives such as Sodium Azide. Store this antibody 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 the vial label or CoA to find the proper storage conditions.
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

(PubMed link indicates BioLegend citation)
  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. Prox J, et al. 2013. J Neurosci. 33:12915-12928. PubMed
  3. Welch G, et al. 2022. Sci Adv. 8:eabo4662. 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
Go To Top Version: 5    Revision Date: 07.09.2024

For Research Use Only. Not for diagnostic or therapeutic use.

 

This product is supplied subject to the terms and conditions, including the limited license, located at www.biolegend.com/terms) ("Terms") and may be used only as provided in the Terms. Without limiting the foregoing, BioLegend products may not be used for any Commercial Purpose as defined in the Terms, resold in any form, used in manufacturing, or reverse engineered, sequenced, or otherwise studied or used to learn its design or composition without express written approval of BioLegend. Regardless of the information given in this document, user is solely responsible for determining any license requirements necessary for user’s intended use and assumes all risk and liability arising from use of the product. BioLegend is not responsible for patent infringement or any other risks or liabilities whatsoever resulting from the use of its products.

 

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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.
If you need assistance with selecting the best format contact our expert technical support team.

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