Human SIAH Interacting Protein peptide (ab23014)

Overview

Description

  • Nature
    Synthetic
  • Amino Acid Sequence
    • Species
      Human
    • Sequence
      C-VESREKQAKGDTEF
    • Amino acids
      215 to 228

Specifications

Our Abpromise guarantee covers the use of ab23014 in the following tested applications.

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

  • Applications

    Blocking

  • Form
    Liquid
  • Concentration information loading...

Preparation and Storage

  • Stability and Storage

    Shipped at 4°C. Upon delivery aliquot and store at -20°C or -80°C. Avoid repeated freeze / thaw cycles.

General Info

  • Alternative names
    • CacyBP
    • Calcyclin binding protein
    • Calcyclin-binding protein
    • CYBP_HUMAN
    • GIG 5
    • GIG5
    • Growth inhibiting gene 5
    • Growth inhibiting gene 5 protein
    • hCacyBP
    • MGC87971
    • PNAS 107
    • PNAS107
    • RP1 102G20.6
    • S100A6 binding protein
    • S100A6-binding protein
    • S100A6BP
    • Siah-interacting protein
    • SIP
    see all
  • Function
    May be involved in calcium-dependent ubiquitination and subsequent proteasomal degradation of target proteins. Probably serves as a molecular bridge in ubiquitin E3 complexes. Participates in the ubiquitin-mediated degradation of beta-catenin (CTNNB1).
  • Sequence similarities
    Contains 1 CS domain.
    Contains 1 SGS domain.
  • Post-translational
    modifications
    Phosphorylated on serine residues. Phosphorylated upon induction by RA or at high calcium concentrations.
  • Cellular localization
    Nucleus. Cytoplasm. Cytoplasmic at low calcium concentrations. In neuroblastoma cells, after a retinoic acid (RA) induction and calcium increase, it localizes in both the nucleus and cytoplasm. The nuclear fraction may be phosphorylated.
  • Information by UniProt

References for Human SIAH Interacting Protein peptide (ab23014)

ab23014 has not yet been referenced specifically in any publications.

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