Recombinant Human RGS17 / RGSZ2 protein (ab162013)

Overview

Description

  • Nature
    Recombinant
  • Source
    Wheat germ
  • Amino Acid Sequence
    • Species
      Human
    • Sequence
      LLFWLACEDLKKEQNKKVIEEKARMIYEDYISILSPKEVSLDSRVREVIN RNLLDPNPHMYEDAQLQIYTLMHRDSFPRFLNSQIYKSFVESTAGSSSES
    • Amino acids
      111 to 210
    • Tags
      proprietary tag N-Terminus

Specifications

Our Abpromise guarantee covers the use of ab162013 in the following tested applications.

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

  • Applications

    Western blot

    ELISA

  • Form
    Liquid
  • Additional notes
    Protein concentration is above or equal to 0.05 mg/ml.
  • Concentration information loading...

Preparation and Storage

  • Stability and Storage

    Shipped on dry ice. Upon delivery aliquot and store at -80ºC. Avoid freeze / thaw cycles.

    pH: 8.00
    Constituents: 0.31% Glutathione, 0.79% Tris HCl

General Info

  • Alternative names
    • hRGS17
    • Regulator of G protein signalling 17
    • Regulator of G protein signalling Z2
    • Regulator of G-protein signaling 17
    • RGS-17
    • RGS17
    • RGS17_HUMAN
    • RGSZ2
    see all
  • Function
    Inhibits signal transduction by increasing the GTPase activity of G protein alpha subunits thereby driving them into their inactive GDP-bound form. Binds selectively to G(z)-alpha and G(alpha)-i2 subunits, accelerates their GTPase activity and regulates their signaling activities. The G(z)-alpha activity is inhibited by the phosphorylation and palmitoylation of the G-protein. Negatively regulates mu-opioid receptor-mediated activation of the G-proteins.
  • Tissue specificity
    Predominantly expressed in the cerebellum. Also expressed in the cortex and medulla. Weakly expressed in a number of peripheral tissues notably spleen, lung and leukocytes.
  • Sequence similarities
    Contains 1 RGS domain.
  • Post-translational
    modifications
    Fatty acylated. Heavily palmitoylated in the cysteine string motif.
    N- and O-glycosylated in synapsomal membranes.
    Serine phosphorylated in synapsomal membranes.
    Sumoylated by SUMO1 and SUM02 in synaptosomes. The sumoylated forms act as a scaffold for sequestering mu-opioid receptor-activated G(alpha) subunits.
  • Cellular localization
    Membrane. Nucleus. Cytoplasm. Shuttles between the cytoplasm/cell membrane and the nucleus. Anchored to the membrane through palmitoylation.
  • Information by UniProt

Images

  • ab162013 on a 12.5% SDS-PAGE stained with Coomassie Blue.

References

ab162013 has not yet been referenced specifically in any publications.

Customer reviews and Q&As

There are currently no Customer reviews or Questions for ab162013.
Please use the links above to contact us or submit feedback about this product.

Please note: All products are "FOR RESEARCH USE ONLY AND ARE NOT INTENDED FOR DIAGNOSTIC OR THERAPEUTIC USE"

Sign up