Purified anti-sAPPβ Antibody (Previously Covance catalog# SIG-39138)

Pricing & Availability
Clone
Poly8134 (See other available formats)
Regulatory Status
RUO
Other Names
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# 9138-005
Covance Catalog# SIG-39138
Isotype
Rabbit Polyclonal IgG
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Product Citations
publications
Poly8134_Purified_sAPPbeta_Antibody_2_062419.png
Western blot of purified anti-sAPPβ antibody (Poly8134). Lane 1: Molecular weight marker; Lane 2: 20 µg of Alzheimer's disease human brain lysate; Lane 3: 20 µg of normal human brain lysate. The blot was incubated with 1 µg/mL of the primary antibody overnight at 4°C, followed by incubation with HRP labeled goat anti-rabbit IgG (Cat. No. 410406). Enhanced chemiluminescence was used as the detection system.
  • Poly8134_Purified_sAPPbeta_Antibody_2_062419.png
    Western blot of purified anti-sAPPβ antibody (Poly8134). Lane 1: Molecular weight marker; Lane 2: 20 µg of Alzheimer's disease human brain lysate; Lane 3: 20 µg of normal human brain lysate. The blot was incubated with 1 µg/mL of the primary antibody overnight at 4°C, followed by incubation with HRP labeled goat anti-rabbit IgG (Cat. No. 410406). Enhanced chemiluminescence was used as the detection system.
  • Poly8134_Purified_sAPPbeta_Antibody_3_062419.png
    Western blot of purified anti-sAPPβ antibody (Poly8134). Lane 1: Molecular weight marker; Lane 2: 20 µg of human cerebrospinal fluid (CSF). The blot was incubated with 1 µg/mL of the primary antibody overnight at 4°C, followed by incubation with HRP labeled goat anti-rabbit IgG (Cat. No. 410406). Enhanced chemiluminescence was used as the detection system.
Cat # Size Price Save
813401 50 µg ¥143,880
Description

APP (Amyloid Precursor Protein) is a single-pass type I membrane protein expressed in all fetal tissues examined with highest levels in brain, kidney, heart and spleen, and with weak expression in liver. In adult brain, highest expression found in the frontal lobe of the cortex and in the anterior perisylvian cortex-opercular gyri. Moderate expression in the cerebellar cortex, the posterior perisylvian cortex-opercular gyri and the temporal associated cortex. Weak expression is found in the striate, extra-striate and motor cortices. Expressed in cerebrospinal fluid, and plasma. Isoform APP695 is the predominant form in neuronal tissue, isoform APP751 and isoform APP770 are widely expressed in non-neuronal cells. Isoform APP751 is the most abundant form in T-lymphocytes. Appican is expressed in astrocytes.

APP functions as a cell surface receptor and performs physiological functions on the surface of neurons relevant to neurite growth, neuronal adhesion and axonogenesis. Involved in cell mobility and transcription regulation through protein-protein interactions. Cleavage either by alpha-secretase, beta-secretase or theta-secretase leads to generation and extracellular release of soluble APP peptides, S-APP-alpha and S-APP-beta, and the retention of corresponding membrane-anchored C-terminal fragments, C80, C83 and C99. Subsequent processing of C80 and C83 by gamma-secretase yields P3 peptides. This is the major secretory pathway and is non-amyloidogenic. Alternatively, presenilin/nicastrin-mediated gamma-secretase processing of C99 releases the amyloid beta proteins, amyloid-beta 40 (Abeta40) and amyloid-beta 42 (Abeta42), major components of amyloid plaques, and the cytotoxic C-terminal fragments, gamma-CTF(50), gamma-CTF(57) and gamma-CTF(59). Many other minor beta-amyloid peptides, beta-amyloid 1-X peptides, are found in cerebral spinal fluid (CSF) including the beta-amyloid X-15 peptides, produced from the cleavage by alpha-secretase and all terminating at Gln-686. It is proteolytically cleaved by caspases during neuronal apoptosis. Cleavage at Asp-739 by either caspase-6, -8 or -9 results in the production of the neurotoxic C31 peptide and the increased production of beta-amyloid peptides.

Product Details
Technical data sheet

Product Details

Verified Reactivity
Human, 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% 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

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 - 2 µg per ml. It is recommended that the reagent be titrated for optimal performance for each application.

Application Notes

This antibody is specific for the soluble fragment cleaved n-terminus to the beta secretase cleavage site of amyloid precursor protein. It has neglible cross reactivity to sAPPa or full length APP.

This product may contain other non-IgG subtypes.

Application References

(PubMed link indicates BioLegend citation)
  1. Freude, Kristine K., et al. Soluble Amyloid Precursor Protein Induces Rapid Neural Differentiation of Human Embryonic Stem Cells. J. Biol. Chem.:286(27): 24264 - 24274, Jul 2011. (WB) PubMed
  2. Ellen Jorissen, et al. The Disintegrin/Metalloproteinase ADAM10 Is Essential for the Establishment of the Brain Cortex. J. Neurosci.: 30(14): 4833 - 4844, Apr 2010. (WB) PubMed
  3. Qiu-Lan Ma, MD, PhD, et al. Reduction of SorLA/LR11, a Sorting Protein Limiting beta-Amyloid Production, in Alzheimer Disease Cerebrospinal Fluid. Arch Neurol:66(4): 448-457, Apr 2009. (WB) PubMed
  4. Corbett GT, et al. 2015. PNAS. PubMed
Product Citations
  1. Qin X, Wang Y, Paudel H 2016. J Biol Chem. 291: 22276 - 22287. PubMed
  2. Wang X, et al. 2022. Int J Mol Sci. 23: . PubMed
  3. Mohammad A, et al. 2022. Front Endocrinol (Lausanne). 13:1069404. PubMed
  4. Zhong BR, et al. 2021. The FASEB Journal. 35(5):e21445. PubMed
  5. Jorissen E, et al. 2010. J Neurosci. 30:4833-4844. PubMed
  6. Zheng Q, et al. 2022. J Clin Invest. 132:. PubMed
  7. Li KY, et al. 2020. Journal of Neurochemistry. 157(4):1351-1365. PubMed
  8. Kotfis K, et al. 2020. British Journal of Pharmacology. 49(1):66-72. PubMed
  9. Freude K, et al. 2011. J Biol Chem. 286:24264-24274. PubMed
  10. Tambini MD, et al. 2020. Elife. 9:e52612. PubMed
  11. Rabinovich-Toidman P, et al. 2015. PLoS One. 10: 0143420. PubMed
  12. Wu Z, et al. 2020. Br J Pharmacol. 1967:177. PubMed
  13. Xiang J, et al. 2019. Mol Ther Nucleic Acids. 16:302. PubMed
  14. Jean-Louis T, et al. 2018. Neurobiol Aging. 62:130. PubMed
  15. Corbett G, et al. 2015. Proc Natl Acad Sci U S A. 112: 8445 - 8450. PubMed
  16. Salta E, et al. 2016. EMBO Mol Med. 8: 1005 - 1018. PubMed
  17. Ma Q, et al. 2009. Arch Neurol. 66:448-457. PubMed
  18. Wang W et al. 2019. EBioMedicine. 42:174-187 . PubMed
  19. Marwarha G, et al. 2018. J Neurochem. 144:761. PubMed
RRID
AB_2564769 (BioLegend Cat. No. 813401)

Antigen Details

Biology Area
Cell Biology, Neurodegeneration, Neuroscience, Protein Misfolding and Aggregation
Molecular Family
APP/β-Amyloid
Gene ID
351 View all products for this Gene ID
UniProt
View information about sAPPbeta on UniProt.org

Related FAQs

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Go To Top Version: 7    Revision Date: 08/12/2022

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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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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