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Purified anti-β-Amyloid, 1-42 Antibody (Previously Covance catalog# SIG-39142)

Pricing & Availability
Clone
12F4 (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# 9142-02
Signet Catalog# 9142-05
Signet Catalog# 9142-10
Covance Catalog# SIG-39142
Isotype
Mouse IgG1, κ
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Product Citations
publications
A_12F4_PURE_bAmyloid_1-42_IHCP_042618
IHC staining of the purified anti-β-Amyloid, 1-42 antibody (12F4) on the formalin-fixed paraffin-embedded brain tissues from normal human (left panel) and patients with Alzheimer’s disease (left panel) and normal human brain tissue (right panel). Following antigen retrieval using 70% formic acid for 20 min, the tissue was incubated overnight with 1µg/mL of the primary antibody at 4°C. BioLegend´s Ultra-Streptavidin (USA) HRP kit (Multi-Species, DAB, Cat. No. 929901) was used for detection followed by hematoxylin and bluing solution counterstaining, according to the protocol provided. The image was captured with a 40X objective. Scale bar: 50 µm.
  • A_12F4_PURE_bAmyloid_1-42_IHCP_042618
    IHC staining of the purified anti-β-Amyloid, 1-42 antibody (12F4) on the formalin-fixed paraffin-embedded brain tissues from normal human (left panel) and patients with Alzheimer’s disease (left panel) and normal human brain tissue (right panel). Following antigen retrieval using 70% formic acid for 20 min, the tissue was incubated overnight with 1µg/mL of the primary antibody at 4°C. BioLegend´s Ultra-Streptavidin (USA) HRP kit (Multi-Species, DAB, Cat. No. 929901) was used for detection followed by hematoxylin and bluing solution counterstaining, according to the protocol provided. The image was captured with a 40X objective. Scale bar: 50 µm.
  • B_12F4_PURE_bAmyloid_1-42_ELISA_042618
    Direct ELISA of the purified anti-β-amyloid 1-42 (clone 12F4) antibody binding to the plate-immobilized human and rodent Aβ1-42, human Aβ1-40 peptides, 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 the horseradish peroxidase labeled goat anti-mouse IgG secondary antibody. TMB (3, 3', 5, 5' tetramethylbenzidine, Cat. No. 421501) was used as the detection system.
  • C_12F4_PURE_bAmyloid_1-42_WB_042618
    Western blot of the purified anti-β-amyloid, 1-42 antibody (clone 12F4). Lane 1: Molecular weight marker; Lane 2: 50 ng of the human Aβ1-40 peptide; Lane 3: 50 ng of the Aβ1-42 peptide. The blot was incubated with 1 µg/ml of the primary antibody overnight at 4oC, followed by incubation with the HRP-labeled goat anti-mouse IgG (cat: 405306). Enhanced chemiluminescence was used as the detection system.
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805509 50 µL 118€
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805501 200 µL 423€
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805502 500 µL 828€
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805503 1 mL 1372€
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Description

Amyloid beta (Aβ or Abeta) 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
Human, Mouse, Rat
Antibody Type
Monoclonal
Host Species
Mouse
Formulation
Phosphate-buffered solution (no preservatives or carrier proteins).
Preparation
The antibody was purified by affinity chromatography.
Concentration
0.5 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

IHC-P - Qualty tested
Direct ELISA, WB - Verified
IHC-F, ELISA - Reported in the literature, not verified in house
Recommended Usage

Each lot of this antibody is quality control tested by formalin-fixed paraffin-embedded immunohistochemical staining. For immunohistochemistry, a concentration range of 0.2 - 5.0 µg/ml is suggested. For Direct ELISA, a concentration range of 0.015 - 1.5 µg/ml is suggested. For Western blotting, the suggested use of this reagent is 1.0 - 5.0 µg/ml. It is recommended that the reagent be titrated for optimal performance for each application.

Application Notes

This antibody is effective in immunoblotting (WB), immunohistochemistry (IHC), and ELISA.

This antibody is reactive to the C-terminus of beta amyloid and is specific for the isoform ending at the 42nd amino acid.

Additional reported applications (for the relevant formats) includes: immunohistochemical staining of paraformaldehyde-fixed frozen sections6 and ELISA3,4,5.

Application References
  1. Helwig M, et al. 2013. J. Biol. Chem. 288:1114. (IHC-P)
  2. Takami M, et al.2009. J. Neurosci.; 29: 13042. (IHC-P)
  3. Cenini G, et al. 2012. Biochim Biophys Acta. 1822(2):130. (ELISA) PubMed
  4. Sundaram RK, et al. 2012. Int. J. Pept. Res. Ther. 18(2):99. (ELISA) PubMed
  5. Savage MJ, et al. 2014. J. Neurosci. 8:2884. (ELISA) PubMed
  6. Mastrangelo MA, Bowers WJ. 2008. BMC Neurosci. 9:81. (IHC-F) PubMed
Product Citations
  1. Bishay J, et al. 2022. Sci Rep. 12:15287. PubMed
  2. Jin J, et al. 2023. Gut Microbes. 15:2167172. PubMed
  3. Barbato C, et al. 2020. Molecular Neurobiology. 57(7):3183-3194. PubMed
  4. Willumsen N, et al. 2023. Brain Commun. 5:fcac321. PubMed
  5. Jordà-Siquier T, et al. 2022. Alzheimers Dement. 18:2099. PubMed
  6. Nick H, et al. 2022. Front Aging Neurosci. 14:1025402. PubMed
  7. Vingtdeux V, et al. 2011. FASEB J. 25:219-231. PubMed
  8. Kim C, et al. 2017. Mol Neurobiol. 10.1007/s12035-017-0683-3. PubMed
  9. Townsend M, et al. 2010. J Pharmacol Exp Ther. 333:110:119. PubMed
  10. Ruiz-Riquelme A, et al. 2021. Acta Neuropathol Commun. 9:83. PubMed
  11. Helwig M, et al. 2013. J Biol Chem. 288:1114-1124. PubMed
  12. Moreno F, et al. 2017. PLoS One. 12(6):e0178093. PubMed
  13. Koh HS, et al. 2021. Int J Mol Sci. 22:. PubMed
  14. Gutknecht MF, et al. 2022. Cell Rep Methods. 2:100214. PubMed
  15. Owen JE, et al. 2021. Sleep. 44:zsab057. PubMed
  16. Kim H, et al. 2021. Front Aging Neurosci. 13:709091. PubMed
  17. Olah M, et al. 2020. Nat Commun. 4.714583333. PubMed
  18. Augé E, et al. 2017. Sci Rep. 7:41807. PubMed
  19. Shi H, et al. 2020. Acta Neuropathol. 139:813. PubMed
  20. Takami M, et al. 2009. J Neurosci. 29:13042-13052. PubMed
  21. Maheshwari M, et al. 2010. Biochemistry. 49:10371-10380. PubMed
  22. Sudol K, et al. 2009. Mol Ther. 17:2031-2040. PubMed
  23. Lee CYD et al. 2018. Neuron. 97(5):1032-1048 . PubMed
  24. Plowey ED, et al. 2022. Acta Neuropathol. 144:143. PubMed
  25. Kim K, et al. 2020. Nat Commun. 0.540972222. PubMed
  26. Chan HN, et al. 2019. Theranostics. 9:2939. PubMed
  27. Kommaddi RP et al. 2018. The Journal of Neuroscience. 38(5):1085-1099 . PubMed
  28. Piccirillo S, et al. 2022. Cell Death Discov. 8:391. PubMed
  29. Li K, et al. 2020. ACS Chemical Neuroscience. 11(24):4316-4328. PubMed
  30. Ohmi K, et al. 2011. PLoS One. 6:e27461. PubMed
  31. Vassar W 2013. Mol Neurodegener. 8:2. PubMed
  32. Faraz A, et al. 2017. Antioxid Redox Signal. . 10.1089/ars.2016.6860. PubMed
  33. Maxwell AM, et al. 2021. Acta Neuropathol Commun. 9:201. PubMed
  34. Parker H, et al. 2020. EMBO Mol Med. 12:e11185. PubMed
  35. Ruiz–Riquelme A, et al. 2018. Acta Neuropathol Commun. 6:26. PubMed
RRID
AB_2564682 (BioLegend Cat. No. 805509)
AB_2564682 (BioLegend Cat. No. 805501)
AB_2564682 (BioLegend Cat. No. 805502)
AB_2564682 (BioLegend Cat. No. 805503)

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 sources: Primarily nervous system, but also adipose tissue, intestine, muscle. 
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 1-42 on UniProt.org

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Go To Top Version: 4    Revision Date: 07/09/2024

For Research Use Only. Not for diagnostic or therapeutic 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.
If you need assistance with selecting the best format contact our expert technical support team.

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