Recombinant Human WW Domain-Binding Protein 2/WBP2 (N-6His)

Recombinant Human WW Domain-Binding Protein 2/WBP2 (N-6His)

Catalog Number:
P001411000ABE
Mfr. No.:
Abe32-8048
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      • Overview
        • MW : 13.38kD. Recombinant Human WW Domain-Binding Protein 2 is produced by our E.coli expression system and the target gene encoding Met1-Ala100 is expressed with a 6His tag at the N-terminus. WW Domain-Binding Protein 2 (WBP2) is a ubiquitous protein that contains one GRAM domain. The WW domain is composed of 38 to 40 semi-conserved AA shared by proteins of diverse functions including structural, regulatory, and signaling proteins. The domain is participated in mediating protein-protein interactions. WBP2 binds to the WW domain of YAP1, WWP1 and WWP2. The WW-binding 1 motif of WBP2 mediates interaction with NEDD4. The function of this protein WBP2 has not been determined. Some researches demonstrate that WBP-2 also interacts with the thyroid-specific transcription factor Pax8.

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      • Properties
        • Source
          E. coli
          Type
          Recombinant Proteins
          Formulation
          Lyophilized from a 0.2 µm filtered solution of 20mM TrisHCl, 1mM DTT, pH 8.0.
          Storage
          Lyophilized protein should be stored at -20°C, though stable at room temperature for 3 weeks. Reconstituted protein solution can be stored at 4-7°C for 2-7 days. Aliquots of reconstituted samples are stable at -20°C for 3 months.
          Endotoxin
          Less than 0.1 ng/µg (1 IEU/µg) as determined by LAL test.

          More Information

          UniProt
          Gene ID
          23558

          * For Research Use Only. Not for use in diagnostic/therapeutics procedures.

      • Applications
        • Application Description
          Always centrifuge tubes before opening. Do not mix by vortex or pipetting. It is not recommended to reconstitute to a concentration less than 100 µg/ml. Dissolve the lyophilized protein in ddH2O. Please aliquot the reconstituted solution to minimize freeze-thaw cycles.

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