Biotin anti-β-Amyloid, 17-24 Antibody (Previously Covance catalog# SIG-39240)

Pricing & Availability
Clone
4G8 (See other available formats)
Regulatory Status
RUO
Workshop
HCDM listed
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# 9240-02
Signet Catalog# 9240-05
Signet Catalog# 9240-10
Covance Catalog# SIG-39240
Isotype
Mouse IgG2b, κ
Ave. Rating
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Product Citations
publications
4G8_Biotin_Beta-Amyloid17-24_Antibody_1_090718
IHC staining of Biotin anti-β-Amyloid, 17-24 antibody (clone 4G8) on formalin-fixed paraffin-embedded human Alzheimer's disease brain tissue. Following antigen retrieval using 70% formic acid for 20 minutes at room temperature, the tissue was incubated with 1 µg/ml of the primary antibody for 60 minutes at room temperature. For detection, the HRP labeling reagent and DAB from BioLegend Ultra Streptavidin (USA) HRP Detection Kit were used (Multi-Species, component #5, DAB; Cat. No. 929901). Slides were counterstained with hematoxylin, according to the protocol provided. The image was captured with a 40X objective. Scale bar: 50 µm
  • 4G8_Biotin_Beta-Amyloid17-24_Antibody_1_090718
    IHC staining of Biotin anti-β-Amyloid, 17-24 antibody (clone 4G8) on formalin-fixed paraffin-embedded human Alzheimer's disease brain tissue. Following antigen retrieval using 70% formic acid for 20 minutes at room temperature, the tissue was incubated with 1 µg/ml of the primary antibody for 60 minutes at room temperature. For detection, the HRP labeling reagent and DAB from BioLegend Ultra Streptavidin (USA) HRP Detection Kit were used (Multi-Species, component #5, DAB; Cat. No. 929901). Slides were counterstained with hematoxylin, according to the protocol provided. The image was captured with a 40X objective. Scale bar: 50 µm
  • 4G8_Biotin_Beta-Amyloid17-24_Antibody_2_090718
    IHC staining of Biotin anti-β-Amyloid, 17-24 antibody (clone 4G8) on formalin-fixed paraffin-embedded human Alzheimer's disease brain tissue. Following antigen retrieval using 70% formic acid for 20 minutes at room temperature, the tissue was incubated with 1 µg/ml of the primary antibody for 60 minutes at room temperature. For detection, the HRP labeling reagent and DAB from BioLegend Ultra Streptavidin (USA) HRP Detection Kit were used (Multi-Species, component #5, DAB; Cat. No. 929901). Slides were counterstained with hematoxylin, according to the protocol provided. The image was captured with a 40X objective. Scale bar: 50 µm
  • 4G8_Biotin_Beta-Amyloid17-24_Antibody_3_090718
    Direct ELISA of Biotin anti-β-Amyloid, 17-24 (clone 4G8) antibody binding to the plate-immobilized human Aβ1-40, human Aβ1-42, and recombinant human APP751 protein. ELISA was performed by coating the wells with 100 ng of peptide or recombinant protein. The wells were then incubated with the primary antibody at 37°C for 45 minutes followed by incubation with HRP labeled streptavidin. TMB (3, 3', 5, 5' tetramethylbenzidine, Cat. No. 421501) was used as the detection system.
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800705 500 µL 1292 CHF
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800706 1 mL 2284 CHF
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800704 200 µL 654 CHF
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Description

Alzheimer’s disease is characterized by the accumulation of aggregated Aβ peptides in senile plaques and vascular deposits. Aβ peptides are derived from amyloid precursor proteins (APP) through sequential proteolytic cleavage of APP by β-secretases and γ-secretases generating diverse Aβ species. Aβ can aggregate to form soluble oligomeric species and insoluble fibrillar or amorphous assemblies. Some forms of the aggregated peptides are toxic to neurons.

Product Details
Technical Data Sheet (pdf)

Product Details

Verified Reactivity
Human, Mouse
Antibody Type
Monoclonal
Host Species
Mouse
Formulation
Phosphate-buffered solution (no preservatives or carrier proteins).
Preparation
The antibody was purified by affinity chromatography.
Concentration
1 mg/ml
Storage & Handling
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

IHC-P - Quality tested
Direct ELISA - Verified

Recommended Usage

Each lot of this antibody is quality control tested by formalin-fixed paraffin-embedded immunohistochemical staining. For immunohistochemistry, a concentration range of 1.0 - 2.0 µg/ml is suggested. For Direct ELISA applications, a concentration range of 0.5 - 2.0 µg/mL is recommended. It is recommended that the reagent be titrated for optimal performance for each application.

Application Notes

This antibody is reactive to amino acid residues 17-24 of ß amyloid. The epitope lies within amino acids 18-22 of ß amyloid (VFFAE). 4G8 ß-amyloid antibody reacts to abnormally processed isoforms, as well as precursor forms.

This antibody clone has been reported for use on IHC of free-floating sections in PBS containing 1% Triton incubated with 0.1 m citrate buffer (4).

Additional reported applications (for the relevant formats) include: immunohistochemical staining on frozen tissue sections (IHC-F) and immunocytochemistry (ICC)

Additional Product Notes

View more applications data for this product in our Scientific Poster Library.

Application References

(PubMed link indicates BioLegend citation)
  1. Poduslo JF, et al. 2004. Biochem. 43:6064. (IHC-F) PubMed
  2. Forny-Germano L, et al. 2014. J Neurosci. 34:13629. (IHC-Other) PubMed
  3. Vallino Costassa E, et al. 2016. J Alzheimers Dis. 51: 875-87. (IHC-P) PubMed
  4. Chen X, et al. 2013. Neurobiol Aging. 34:2370. (ICC) PubMed
  5. Hatami A, et al. 2016. J Alzheimers Dis. 50:517. (IHC-P) PubMed
  6. Kawarabayashi T, et al. 2001. J Neurosci 21:372 (IP)
  7. Fonte V, et al. 2002. PNAS. 110:4853 (IP)
Product Citations
  1. Sun XY, et al. 2023. Signal Transduct Target Ther. 8:30. PubMed
  2. Lam S, et al. 2022. Acta Neuropathol Commun. 10:112. PubMed
  3. Jung ES, et al. 2022. Aging Cell. 21:e13623. PubMed
  4. Townsend M, et al. 2010. J Pharmacol Exp Ther. 333:110:119. PubMed
  5. Chen J, et al. 2019. Int J Mol Med. 44:313. PubMed
  6. Elmer BM, et al. 2019. PLoS One. 14:e0226245. PubMed
  7. Yao Q, et al. 2018. Acta Biochim Biophys Sin (Shanghai). 50(5):447-455. PubMed
  8. Watanabe H, et al. 2012. J Neurosci. 32:5085-5096. PubMed
  9. Hong J, et al. 2016. J Lipid Res. 57: 36 - 45. PubMed
  10. Clayton K, et al. 2021. Mol Neurodegener. 18:16. PubMed
  11. Bales K, et al. 2016. Brain. 139: 563 - 577. PubMed
  12. Luo M, et al. 2022. Genes Dis. 9:1315. PubMed
  13. Forgrave LM, et al. 2022. Clin Chem Lab Med. 60:198. PubMed
  14. Do TM, et al. 2020. Mol Ther Methods Clin Dev. 19:58. PubMed
RRID
AB_2564650 (BioLegend Cat. No. 800705)
AB_2564650 (BioLegend Cat. No. 800706)
AB_2564650 (BioLegend Cat. No. 800704)

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 Neruother. 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 17-24 on UniProt.org

Related FAQs

How many biotin molecules are per antibody structure?
We don't routinely measure the number of biotins with our antibody products but the number of biotin molecules range from 3-6 molecules per antibody.
Go To Top Version: 4    Revision Date: 12.16.2021

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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