Anti-FGD2 antibody [EPR15306] - N-terminal (ab185968)


  • Product name
    Anti-FGD2 antibody [EPR15306] - N-terminal
    See all FGD2 primary antibodies
  • Description
    Rabbit monoclonal [EPR15306] to FGD2 - N-terminal
  • Host species
  • Tested applications
    Suitable for: WB, IHC-P, ICC/IFmore details
  • Species reactivity
    Reacts with: Mouse, Rat, Human
  • Immunogen

    Recombinant fragment within Human FGD2 aa 1-150 (N terminal). The exact sequence is proprietary.
    Database link: Q7Z6J4

  • Positive control
    • Human tonsil, Human lymph node and Raji lysates; Human colon tissue; 293T and Raji cells.
  • General notes



    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.


Associated products


Our Abpromise guarantee covers the use of ab185968 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 1/1000 - 1/10000. Detects a band of approximately 75 kDa (predicted molecular weight: 75 kDa).
IHC-P 1/50.
ICC/IF 1/100.


  • Function
    Activates CDC42, a member of the Ras-like family of Rho-and Rac proteins, by exchanging bound GDP for free GTP. Activates JNK1 via CDC42 but not RAC1. Binds to phosphatidylinositol 4,5-bisphosphate, phosphatidylinositol 3,4,5-trisphosphate, phosphatidylinositol 5-monophosphate, phosphatidylinositol 4-monophosphate and phosphatidylinositol 3-monophosphate.
  • Sequence similarities
    Contains 1 DH (DBL-homology) domain.
    Contains 1 FYVE-type zinc finger.
    Contains 2 PH domains.
  • Domain
    The FYVE-type zinc-finger is necessary for early endosome localization. Recruitement to endosomal membranes via this domain requires the presence of phosphatidylinositol 3-phosphate or other phosphatidylinositides.
    The PH domain is necessary for localization to the ruffle membrane. Recruitement to ruffle membrane occurs through binding of phosphoinositides by the PH domain. This domain also contributes to the lipid-binding properties of the protein.
    The DH domain is necessary for its ability to activate JNK1 via CDC42.
  • Cellular localization
    Cytoplasm > cytoskeleton. Cytoplasm. Nucleus. Early endosome. Early endosome membrane. Cell projection > ruffle membrane. Recruitement to the endosome and ruffle membrane requires the presence of phosphoinositides.
  • Information by UniProt
  • Database links
  • Alternative names
    • FGD1 family member 2 antibody
    • Fgd2 antibody
    • FGD2_HUMAN antibody
    • FLJ00276 protein antibody
    • FYVE antibody
    • FYVE RhoGEF and PH domain containing 2 antibody
    • RhoGEF and PH domain-containing protein 2 antibody
    • ZFYVE4 antibody
    • Zinc finger FYVE domain-containing protein 4 antibody
    see all


  • All lanes : Anti-FGD2 antibody [EPR15306] - N-terminal (ab185968) at 1/10000 dilution

    Lane 1 : Human tonsil lysate
    Lane 2 : Human lymph node lysate
    Lane 3 : Raji lysate

    Lysates/proteins at 20 µg per lane.

    All lanes : Anti-Rabbit IgG (HRP), specific to the non-reduced form of IgG at 1/1000 dilution

    Predicted band size: 75 kDa
    Observed band size: 75 kDa

  • Immunohistochemical analysis of paraffin-embedded Human colon tissue labeling FGD2 with ab185968 at 1/50 dilution followed by prediluted HRP Polymer for Rabbit IgG. Counter stained with Hematoxylin.

  • Immunofluorescent analysis of 4% paraformaldehyde-fixed 293T cells labeling FGD2 with ab185968 at 1/100 dilution followed by Goat anti rabbit IgG (Alexa Fluor®555) secondary antibody at 1/200 dilution. Counter stained with Dapi (blue).

  • Immunofluorescent analysis of acetone-fixed Raji cells labeling FGD2 with ab185968 at 1/100 dilution followed by Goat anti rabbit IgG (Alexa Fluor®488) secondary antibody at 1/200 dilution. Counter stained with Dapi (blue).


ab185968 has not yet been referenced specifically in any publications.

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