Description

  • Product name

    Recombinant Human G3BP protein
  • Purity

    > 85 % SDS-PAGE.
    ab103304 was purified using conventional chromatography techniques.
  • Expression system

    Escherichia coli
  • Accession

  • Protein length

    Full length protein
  • Animal free

    No
  • Nature

    Recombinant
    • Species

      Human
    • Sequence

      MVMEKPSPLLVGREFVRQYYTLLNQAPDMLHRFYGKNSSYVHGGLDSNGK PADAVYGQKEIHRKVMSQNFTNCHTKIRHVDAHATLNDGVVVQVMGLLSN NNQALRRFMQTFVLAPEGSVANKFYVHNDIFRYQDEVFGGFVTEPQEESE EEVEEPEERQQTPEVVPDDSGTFYDQAVVSNDMEEHLEEPVAEPEPDPEP EPEQEPVSEIQEEKPEPVLEETAPEDAQKSSSPAPADIAQTVQEDLRTFS WASVTSKNLPPSGAVPVTGIPPHVVKVPASQPRPESKPESQIPPQRPQRD QRVREQRINIPPQRGPRPIREAGEQGDIEPRRMVRHPDSHQLFIGNLPHE VDKSELKDFFQSYGNVVELRINSGGKLPNFGFVVFDDSEPVQKVLSNRPI MFRGEVRLNVEEKKTRAAREGDRRDNRLRGPGGPRGGLGGGMRGPPRGGM VQKPGFGVGRGLAPRQVEHHHHHH
    • Predicted molecular weight

      53 kDa including tags
    • Amino acids

      1 to 466
    • Tags

      His tag C-Terminus

Specifications

Our Abpromise guarantee covers the use of ab103304 in the following tested applications.

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

  • Applications

    SDS-PAGE

    Mass Spectrometry

  • Mass spectrometry

    MALDI-TOF
  • Form

    Liquid
  • Concentration information loading...

Preparation and Storage

  • Stability and Storage

    Shipped at 4°C. Store at +4°C short term (1-2 weeks). Upon delivery aliquot. Store at -20°C or -80°C. Avoid freeze / thaw cycle.

    pH: 8.00
    Constituents: 0.0308% DTT, 0.316% Tris HCl, 10% Glycerol, 0.58% Sodium chloride

General Info

  • Alternative names

    • ATP dependent DNA helicase VIII
    • ATP-dependent DNA helicase VIII
    • G3BP
    • G3BP stress granule assembly factor 1
    • G3BP-1
    • G3bp1
    • G3BP1_HUMAN
    • GAP binding protein
    • GAP SH3 domain binding protein 1
    • GAP SH3 domain-binding protein 1
    • GTPase activating protein (SH3 domain) binding protein 1
    • hDH VIII
    • Human DNA helicase VIII
    • MGC111040
    • Ras GTPase activating protein binding protein 1
    • Ras GTPase activating protein SH3 domain binding protein
    • Ras GTPase-activating protein-binding protein 1
    • RasGAP associated endoribonuclease G3BP
    see all
  • Function

    May be a regulated effector of stress granule assembly. Phosphorylation-dependent sequence-specific endoribonuclease in vitro. Cleaves exclusively between cytosine and adenine and cleaves MYC mRNA preferentially at the 3'-UTR. ATP- and magnesium-dependent helicase. Unwinds preferentially partial DNA and RNA duplexes having a 17 bp annealed portion and either a hanging 3' tail or hanging tails at both 5'- and 3'-ends. Unwinds DNA/DNA, RNA/DNA, and RNA/RNA substrates with comparable efficiency. Acts unidirectionally by moving in the 5' to 3' direction along the bound single-stranded DNA.
  • Tissue specificity

    Ubiquitous.
  • Sequence similarities

    Contains 1 NTF2 domain.
    Contains 1 RRM (RNA recognition motif) domain.
  • Domain

    The NTF2 domain mediates multimerization.
  • Post-translational
    modifications

    Phosphorylated exclusively on serine residues. Hyperphosphorylated in quiescent fibroblasts. Hypophosphorylation leads to a decrease in endoribonuclease activity (By similarity). RASA1-dependent phosphorylation of Ser-149 induces a conformational change that prevents self-association. Dephosphorylation after HRAS activation is required for stress granule assembly. Ser-149 phosphorylation induces partial nuclear localization.
    Arg-435 is dimethylated, probably to asymmetric dimethylarginine.
  • Cellular localization

    Cytoplasm. Cytoplasm > cytosol. Cell membrane. Nucleus. Cytoplasmic in proliferating cells, can be recruited to the plasma membrane in exponentially growing cells (By similarity). Cytosolic and partially nuclear in resting cells. Recruited to stress granules (SGs) upon either arsenite or high temperature treatment. Recruitment to SGs is influenced by HRAS.
  • Information by UniProt

Images

  • 15% SDS-PAGE analysis of 3µg ab103304.

References

ab103304 has not yet been referenced specifically in any publications.

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