Anti-Go α (GTP binding protein Go α subunit) (Bovine) pAb

  • Applications
    • IHC
    • IP
    • WB
  • Target GTP binding protein Go α subunit
  • Host Species Rabbit
  • Species Reactivities Human, Mouse, Rat
  • Code # 551
  • Size 100 µl
  • Price
    $278.49
Specifications

Alternative Names

GNAO1, GNAO, G-ALPHA-o, guanine nucleotide binding protein (G protein), alpha activating activity polypeptide O

Background

The heterotrimeric guanine nucleotide-binding regulatory proteins (G-proteins) mediate signaling from transmembrane cell surface receptors to a variety of intracellular effectors. G-proteins are composed of a 36-52 kDa -subunit, a 35-36 kDa -subunit, and an 8-10 kDa -subunit. The  subunits bind and hydrolyze GTP and are involved in regulation of intracellular effectors. In mammals, G  proteins are encoded by at least 16 genes.
  • Antibody Type:
    Polyclonal
  • Application:
    IHC, IP, WB
  • Conjugate:
    Unlabeled
  • Description:
    Polyclonal antibody of 100 µl targeting GTP binding protein Go alpha subunit for WB, IHC,IPP.
  • Formulation:
    In PBS/50% glycerol, pH 7.2
  • Gene ID (Human):
  • Gene ID (Mouse):
  • Gene ID (Rat):
  • Host Species:
    Rabbit
  • Immunogen:
    Goα cattle
  • Isotype:
    IgG
  • Product Type:
    Antibody
  • Reactivity:
    This antibody reacts with Go  (39 kDa) on Western blotting, Immunoprecipitation and Immunohistochemistry.
  • Research Area:
    Epitope Tag
  • Short Description:
    GTP binding protein Go alpha subunit polyclonal antibody.
  • Size:
    100 µl
  • Species Reactivity:
    Human, Mouse, Rat
  • Storage Temperature:
    -20°C
  • Target:
    GTP binding protein Go α subunit
Citations
  1. Obuse C et al. A conserved Mis12 centromere complex is linked to heterochromatic HP1 and outer kinetochore protein Zwint-1. Nat Cell Biol. 6, 1135-41 (2004),
  2. Qi Q et al. Involvement of the N-terminal B-box domain of Arabidopsis BBX32 protein in interaction with soybean BBX62 protein. J Biol Chem. 287, 31482-93 (2012),
  3. Sakurai T et al. Membrane microdomain switching: a regulatory mechanism of amyloid precursor protein processing. J Cell Biol. 183, 339-52 (2008),
  4. Sugiyama T et al. Red5 and three nuclear pore components are essential for efficient suppression of specific mRNAs during vegetative growth of fission yeast. Nucleic Acids Res. 41, 6674-86 (2013)
References
  1. Prince, J. E. A. et al., J. Neurosci. 29, 14211-14222 (2009)
  2. Takigami, S., et al., Chem. Senses 29, 301-310 (2004)
  3. Matsuoka, M., et al., Chem. Senses 26, 161-166 (2001)
  4. Takigami, S., et al., Chem. Senses 25, 387-393 (2000)
  5. Krsmanovic, L. Z., et al., Endocrinology 139, 4037-4043 (1998)
  6. Kato, K., et al., Cancer Res. 47, 5800-5805 (1987)
  7. Asano, T., et al., J. Neurochem. 48, 1617-1623 (1987)
  8. Worley, P.F., et al., PNAS 83, 4561-4565 (1986)