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  1. Link

    alexa-fluor-647-beta-amyloid-1-42-antibody-moc64-ab224025.pdf

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Neuroscience Neurology process Neurodegenerative disease Alzheimer's disease Amyloid
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RecombinantRabMAb

Recombinant Alexa Fluor® 647 Anti-beta Amyloid 1-42 antibody [mOC64] (ab224025)

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  • SDS
  • Certificate of Compliance
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Immunohistochemistry (Frozen sections) - Alexa Fluor® 647 Anti-beta Amyloid 1-42 antibody [mOC64] (ab224025)
  • Alexa Fluor® 647 Anti-beta Amyloid 1-42 antibody [mOC64] (ab224025)

Key features and details

  • Produced recombinantly (animal-free) for high batch-to-batch consistency and long term security of supply
  • Alexa Fluor® 647 Rabbit monoclonal [mOC64] to beta Amyloid 1-42
  • Suitable for: IHC-Fr
  • Reacts with: Human
  • Conjugation: Alexa Fluor® 647. Ex: 652nm, Em: 668nm

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Overview

  • Product name

    Alexa Fluor® 647 Anti-beta Amyloid 1-42 antibody [mOC64]
    See all beta Amyloid 1-42 primary antibodies
  • Description

    Alexa Fluor® 647 Rabbit monoclonal [mOC64] to beta Amyloid 1-42
  • Host species

    Rabbit
  • Conjugation

    Alexa Fluor® 647. Ex: 652nm, Em: 668nm
  • Tested applications

    Suitable for: IHC-Frmore details
  • Species reactivity

    Reacts with: Human
    Predicted to work with: Mouse
  • Immunogen

    Other Immunogen Type corresponding to Human beta Amyloid 1-42. Amyloid beta 1-42 fibrils were used as the immunogen.
    Database link: P05067

  • Positive control

    • IHC-Fr: human Alzheimer brain tissue sections
  • General notes

    This product is a recombinant monoclonal antibody, which offers several advantages including:

    • - High batch-to-batch consistency and reproducibility
    • - Improved sensitivity and specificity
    • - Long-term security of supply
    • - Animal-free production
    For more information see here.

    Our RabMAb® technology is a patented hybridoma-based technology for making rabbit monoclonal antibodies. For details on our patents, please refer to RabMAb® patents.

    Alexa Fluor® is a registered trademark of Molecular Probes, Inc, a Thermo Fisher Scientific Company. The Alexa Fluor® dye included in this product is provided under an intellectual property license from Life Technologies Corporation. As this product contains the Alexa Fluor® dye, the purchase of this product conveys to the buyer the non-transferable right to use the purchased product and components of the product only in research conducted by the buyer (whether the buyer is an academic or for-profit entity). As this product contains the Alexa Fluor® dye the sale of this product is expressly conditioned on the buyer not using the product or its components, or any materials made using the product or its components, in any activity to generate revenue, which may include, but is not limited to use of the product or its components: in manufacturing; (ii) to provide a service, information, or data in return for payment (iii) for therapeutic, diagnostic or prophylactic purposes; or (iv) for resale, regardless of whether they are sold for use in research. For information on purchasing a license to this product for purposes other than research, contact Life Technologies Corporation, 5781 Van Allen Way, Carlsbad, CA 92008 USA or outlicensing@thermofisher.com.

Properties

  • Form

    Liquid
  • Storage instructions

    Shipped at 4°C. Store at +4°C short term (1-2 weeks). Upon delivery aliquot. Store at -20°C. Avoid freeze / thaw cycle. Store In the Dark.
  • Storage buffer

    pH: 7.40
    Preservative: 0.02% Sodium azide
    Constituents: 1% BSA, 30% Glycerol (glycerin, glycerine), PBS
  • Concentration information loading...
  • Purity

    Protein A purified
  • Clonality

    Monoclonal
  • Clone number

    mOC64
  • Isotype

    IgG
  • Research areas

    • Neuroscience
    • Neurology process
    • Neurodegenerative disease
    • Alzheimer's disease
    • Amyloid
    • Neuroscience
    • Diseases

Associated products

  • Alternative Versions

    • Anti-beta Amyloid antibody [mOC64] (ab201060)
    • Alexa Fluor® 488 Anti-beta Amyloid 1-42 antibody [mOC64] (ab224026)
    • Anti-beta Amyloid 1-42 antibody [mOC64] - Low endotoxin, Azide free (ab224275)
    • Alexa Fluor® 647 Anti-beta Amyloid antibody [mOC64] (ab300742)
    • Alexa Fluor® 555 Anti-beta Amyloid antibody [mOC64] (ab302544)
    • Alexa Fluor® 568 Anti-beta Amyloid antibody [mOC64] (ab302803)
  • Isotype control

    • Alexa Fluor® 647 Rabbit IgG, monoclonal [EPR25A] - Isotype Control (ab199093)

Applications

The Abpromise guarantee

Our Abpromise guarantee covers the use of ab224025 in the following tested applications.

The application notes include recommended starting dilutions; optimal dilutions/concentrations should be determined by the end user.

Application Abreviews Notes
IHC-Fr
1/100.
Notes
IHC-Fr
1/100.

Target

  • Function

    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. Can promote transcription activation through binding to APBB1-KAT5 and inhibits Notch signaling through interaction with Numb. Couples to apoptosis-inducing pathways such as those mediated by G(O) and JIP. Inhibits G(o) alpha ATPase activity (By similarity). Acts as a kinesin I membrane receptor, mediating the axonal transport of beta-secretase and presenilin 1. Involved in copper homeostasis/oxidative stress through copper ion reduction. In vitro, copper-metallated APP induces neuronal death directly or is potentiated through Cu(2+)-mediated low-density lipoprotein oxidation. Can regulate neurite outgrowth through binding to components of the extracellular matrix such as heparin and collagen I and IV. The splice isoforms that contain the BPTI domain possess protease inhibitor activity. Induces a AGER-dependent pathway that involves activation of p38 MAPK, resulting in internalization of amyloid-beta peptide and leading to mitochondrial dysfunction in cultured cortical neurons.
    Beta-amyloid peptides are lipophilic metal chelators with metal-reducing activity. Bind transient metals such as copper, zinc and iron. In vitro, can reduce Cu(2+) and Fe(3+) to Cu(+) and Fe(2+), respectively. Beta-amyloid 42 is a more effective reductant than beta-amyloid 40. Beta-amyloid peptides bind to lipoproteins and apolipoproteins E and J in the CSF and to HDL particles in plasma, inhibiting metal-catalyzed oxidation of lipoproteins. Beta-APP42 may activate mononuclear phagocytes in the brain and elicit inflammatory responses. Promotes both tau aggregation and TPK II-mediated phosphorylation. Interaction with overexpressed HADH2 leads to oxidative stress and neurotoxicity.
    Appicans elicit adhesion of neural cells to the extracellular matrix and may regulate neurite outgrowth in the brain.
    The gamma-CTF peptides as well as the caspase-cleaved peptides, including C31, are potent enhancers of neuronal apoptosis.
    N-APP binds TNFRSF21 triggering caspase activation and degeneration of both neuronal cell bodies (via caspase-3) and axons (via caspase-6).
  • Tissue specificity

    Expressed in all fetal tissues examined with highest levels in brain, kidney, heart and spleen. 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 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.
  • Involvement in disease

    Defects in APP are the cause of Alzheimer disease type 1 (AD1) [MIM:104300]. AD1 is a familial early-onset form of Alzheimer disease. It can be associated with cerebral amyloid angiopathy. Alzheimer disease is a neurodegenerative disorder characterized by progressive dementia, loss of cognitive abilities, and deposition of fibrillar amyloid proteins as intraneuronal neurofibrillary tangles, extracellular amyloid plaques and vascular amyloid deposits. The major constituent of these plaques is the neurotoxic amyloid-beta-APP 40-42 peptide (s), derived proteolytically from the transmembrane precursor protein APP by sequential secretase processing. The cytotoxic C-terminal fragments (CTFs) and the caspase-cleaved products such as C31 derived from APP, are also implicated in neuronal death.
    Defects in APP are the cause of cerebral amyloid angiopathy APP-related (CAA-APP) [MIM:605714]. A hereditary localized amyloidosis due to amyloid-beta A4 peptide(s) deposition in the cerebral vessels. The principal clinical characteristics are recurrent cerebral and cerebellar hemorrhages, recurrent strokes, cerebral ischemia, cerebral infarction, and progressive mental deterioration. Patients develop cerebral hemorrhage because of the severe cerebral amyloid angiopathy. Parenchymal amyloid deposits are rare and largely in the form of pre-amyloid lesions or diffuse plaque-like structures. They are Congo red negative and lack the dense amyloid cores commonly present in Alzheimer disease. Some affected individuals manifest progressive aphasic dementia, leukoencephalopathy, and occipital calcifications.
  • Sequence similarities

    Belongs to the APP family.
    Contains 1 BPTI/Kunitz inhibitor domain.
  • Domain

    The basolateral sorting signal (BaSS) is required for sorting of membrane proteins to the basolateral surface of epithelial cells.
    The NPXY sequence motif found in many tyrosine-phosphorylated proteins is required for the specific binding of the PID domain. However, additional amino acids either N- or C-terminal to the NPXY motif are often required for complete interaction. The PID domain-containing proteins which bind APP require the YENPTY motif for full interaction. These interactions are independent of phosphorylation on the terminal tyrosine residue. The NPXY site is also involved in clathrin-mediated endocytosis.
  • Post-translational
    modifications

    Proteolytically processed under normal cellular conditions. 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).
    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.
    N- and O-glycosylated. O-linkage of chondroitin sulfate to the L-APP isoforms produces the APP proteoglycan core proteins, the appicans. The chondroitin sulfate chain of appicans contains 4-O-sulfated galactose in the linkage region and chondroitin sulfate E in the repeated disaccharide region.
    Phosphorylation in the C-terminal on tyrosine, threonine and serine residues is neuron-specific. Phosphorylation can affect APP processing, neuronal differentiation and interaction with other proteins. Phosphorylated on Thr-743 in neuronal cells by Cdc5 kinase and Mapk10, in dividing cells by Cdc2 kinase in a cell-cycle dependent manner with maximal levels at the G2/M phase and, in vitro, by GSK-3-beta. The Thr-743 phosphorylated form causes a conformational change which reduces binding of Fe65 family members. Phosphorylation on Tyr-757 is required for SHC binding. Phosphorylated in the extracellular domain by casein kinases on both soluble and membrane-bound APP. This phosphorylation is inhibited by heparin.
    Extracellular binding and reduction of copper, results in a corresponding oxidation of Cys-144 and Cys-158, and the formation of a disulfide bond. In vitro, the APP-Cu(+) complex in the presence of hydrogen peroxide results in an increased production of beta-amyloid-containing peptides.
    Trophic-factor deprivation triggers the cleavage of surface APP by beta-secretase to release sAPP-beta which is further cleaved to release an N-terminal fragment of APP (N-APP).
    Beta-amyloid peptides are degraded by IDE.
  • Cellular localization

    Membrane. Membrane > clathrin-coated pit. Cell surface protein that rapidly becomes internalized via clathrin-coated pits. During maturation, the immature APP (N-glycosylated in the endoplasmic reticulum) moves to the Golgi complex where complete maturation occurs (O-glycosylated and sulfated). After alpha-secretase cleavage, soluble APP is released into the extracellular space and the C-terminal is internalized to endosomes and lysosomes. Some APP accumulates in secretory transport vesicles leaving the late Golgi compartment and returns to the cell surface. Gamma-CTF(59) peptide is located to both the cytoplasm and nuclei of neurons. It can be translocated to the nucleus through association with APBB1 (Fe65). Beta-APP42 associates with FRPL1 at the cell surface and the complex is then rapidly internalized. APP sorts to the basolateral surface in epithelial cells. During neuronal differentiation, the Thr-743 phosphorylated form is located mainly in growth cones, moderately in neurites and sparingly in the cell body. Casein kinase phosphorylation can occur either at the cell surface or within a post-Golgi compartment.
  • Target information above from: UniProt accession P05067 The UniProt Consortium
    The Universal Protein Resource (UniProt) in 2010
    Nucleic Acids Res. 38:D142-D148 (2010) .

    Information by UniProt
  • Database links

    • Entrez Gene: 351 Human
    • Entrez Gene: 11820 Mouse
    • Omim: 104760 Human
    • SwissProt: P05067 Human
    • SwissProt: P12023 Mouse
    • Unigene: 434980 Human
    • Unigene: 277585 Mouse
    • Alternative names

      • A4 antibody
      • A4_HUMAN antibody
      • AAA antibody
      • ABETA antibody
      • ABPP antibody
      • AICD-50 antibody
      • AICD-57 antibody
      • AICD-59 antibody
      • AID(50) antibody
      • AID(57) antibody
      • AID(59) antibody
      • Alzheimer disease amyloid protein antibody
      • Amyloid intracellular domain 50 antibody
      • Amyloid intracellular domain 57 antibody
      • Amyloid intracellular domain 59 antibody
      • APP antibody
      • APPI antibody
      • Beta amyloid protein 42 antibody
      • Beta APP42 antibody
      • Beta-APP40 antibody
      • Beta-APP42 antibody
      • C31 antibody
      • Cerebral vascular amyloid peptide antibody
      • CVAP antibody
      • Gamma-CTF(50) antibody
      • Gamma-CTF(57) antibody
      • Gamma-CTF(59) antibody
      • PN-II antibody
      • PreA4 antibody
      • Protease nexin-II antibody
      • S-APP-alpha antibody
      • S-APP-beta antibody
      see all

    Images

    • Immunohistochemistry (Frozen sections) - Alexa Fluor® 647 Anti-beta Amyloid 1-42 antibody [mOC64] (ab224025)
      Immunohistochemistry (Frozen sections) - Alexa Fluor® 647 Anti-beta Amyloid 1-42 antibody [mOC64] (ab224025)

      IHC image of beta Amyloid 1-42 staining in a section of frozen human Alzheimer brain*.

      The section was fixed using 10% formaldehyde in 1XPBS for 10 minutes. No antigen retrieval step was performed prior to staining. Non-specific protein-protein interactions were then blocked in TBS containing 0.025% (v/v) Triton X-100, 0.3M (w/v) glycine and 1% (w/v) BSA for 1h at room temperature.  The section was then incubated overnight at +4°C in TBS containing 0.025% (v/v) Triton X-100 and 1% (w/v) BSA with ab224025 at 1/100 dilution (shown in red) and counterstained using ab195887, Mouse monoclonal to alpha Tubulin (Alexa Fluor® 488), at 1/250 dilution (shown in green). Nuclear DNA was labelled with DAPI (shown in blue). The section was then mounted using Fluoromount®.

      Image was taken with a confocal microscope (Leica-Microsystems, TCS SP8).

      For other IHC staining systems (automated and non-automated), customers should optimize variable parameters such as antigen retrieval conditions, antibody concentrations and incubation times.

      *Tissue obtained from the Human Research Tissue Bank, supported by the NIHR Cambridge Biomedical Research Centre.

    • Alexa Fluor® 647 Anti-beta Amyloid 1-42 antibody [mOC64] (ab224025)
      Alexa Fluor® 647 Anti-beta Amyloid 1-42 antibody [mOC64] (ab224025)

    Protocols

    To our knowledge, customised protocols are not required for this product. Please try the standard protocols listed below and let us know how you get on.

    Click here to view the general protocols

    Datasheets and documents

    • SDS download

    • Datasheet download

      Download

    Certificate of Compliance

    To download a Certificate of Compliance, please enter your Lot number below:

    References (0)

    Publishing research using ab224025? Please let us know so that we can cite the reference in this datasheet.

    ab224025 has not yet been referenced specifically in any publications.

    Customer reviews and Q&As

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    Immunocytochemistry/ Immunofluorescence abreview for Alexa Fluor® 647 Anti-beta Amyloid 1-42 antibody [mOC64]

    Excellent
    Abreviews
    Abreviews
    abreview image
    Application
    Immunocytochemistry/ Immunofluorescence
    Sample
    Mouse Cell (retina and cerebellum)
    Permeabilization
    Yes - 0.1% triton
    Specification
    retina and cerebellum
    Blocking step
    BSA as blocking agent for 1 hour(s) and 0 minute(s) · Concentration: 1% · Temperature: 25°C
    Fixative
    Paraformaldehyde
    Read More
    The reviewer received a reward from Abcam’s Loyalty Program in thanks for submitting this Abreview and for helping the scientific community make better-informed decisions.

    Abcam user community

    Verified customer

    Submitted Aug 05 2022

    Please note: All products are "FOR RESEARCH USE ONLY. NOT FOR USE IN DIAGNOSTIC PROCEDURES"
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