Recombinant
RabMAb

Recombinant Anti-ATP5O (acetyl K139) antibody [NCI-R155-13] (ab214339)

Overview

  • Product name

    Anti-ATP5O (acetyl K139) antibody [NCI-R155-13]
    See all ATP5O primary antibodies
  • Description

    Rabbit monoclonal [NCI-R155-13] to ATP5O (acetyl K139)
  • Host species

    Rabbit
  • Tested applications

    Suitable for: WBmore details
  • Species reactivity

    Reacts with: Human
  • Immunogen

    Synthetic peptide within Human ATP5O aa 150 to the C-terminus (acetyl K139). The exact sequence is proprietary.
    Database link: P48047

  • General notes

    Note that prior to mitochondrial transport and cleavage the acetylation site is K162. 

     

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

    This product is a recombinant rabbit monoclonal antibody.

Properties

Applications

Our Abpromise guarantee covers the use of ab214339 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
WB 1/200. Detects a band of approximately 20 kDa (predicted molecular weight: 23 kDa).

Target

  • Function

    Mitochondrial membrane ATP synthase (F(1)F(0) ATP synthase or Complex V) produces ATP from ADP in the presence of a proton gradient across the membrane which is generated by electron transport complexes of the respiratory chain. F-type ATPases consist of two structural domains, F(1) - containing the extramembraneous catalytic core and F(0) - containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation. Part of the complex F(0) domain and the peripheric stalk, which acts as a stator to hold the catalytic alpha(3)beta(3) subcomplex and subunit a/ATP6 static relative to the rotary elements.
  • Sequence similarities

    Belongs to the ATPase delta chain family.
  • Cellular localization

    Mitochondrion. Mitochondrion inner membrane.
  • Information by UniProt
  • Database links

  • Alternative names

    • ATP synthase O subunit mitochondrial precursor antibody
    • ATP synthase subunit O antibody
    • ATP synthase, H+ transporting, mitochondrial F1 complex, O subunit antibody
    • ATP5O antibody
    • ATPO antibody
    • ATPO_HUMAN antibody
    • mitochondrial antibody
    • Mitochondrial ATP synthase, O subunit antibody
    • Oligomycin sensitivity conferral protein antibody
    • OSCP antibody
    see all

Images

  • ATP5O (acetyl K139) was immunoprecipitated from HEK 293T cells (Human epithelial cell line from embryonic kidney) transfected with Flag-tagged ATP5O expression vector and treated with 1μM Trichostatin A (TSA) for 48 h with anti-FLAG antibody.

    Western blot was performed from the immunoprecipitate using ab214339 at 1/200 dilution. Secondary antibody (Donkey anti-rabbit IgG), was used at 1/10000 dilution.

    Lane 1: IP samples washed and incubated with purified SIRT3 protein without NAD, 10 μg.

    Lane 2: IP samples washed and incubated with purified SIRT3 protein with NAD for 2 hours, 10 μg.

    Lane 3: IP samples washed and incubated with purified SIRT3 protein without NAD, then blocked with control non-acetylated peptide (cont-peptide), 10 μg.

    Lane 4: IP samples washed and incubated with purified SIRT3 protein with NAD for 2 hours, then blocked with control non-acetylated peptide (cont-peptide), 10 μg.

    Lane 5: IP samples washed and incubated with purified SIRT3 protein without NAD, then blocked with acetylated peptide (Ac-peptide), 10 μg.

    Lane 6: IP samples washed and incubated with purified SIRT3 protein with NAD for 2 hours, then blocked with acetylated peptide (Ac-peptide), 10 μg.

    These results indicate that this antibody is specific for acetylated lysine 139 and that SIRT3 deacetylates ATP5O in an in vitro/cell-free experimental model system.

    Note that prior to mitochondrial transport and cleavage the acetylation site is K162.

    This data was kindly provided by Dr. Gius (Northwestern University), and has been published in the literature (PMID: 24252090).

References

ab214339 has not yet been referenced specifically in any publications.

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