Description
Human DTX4 Recombinant Protein (N-His)
Human DTX4 Recombinant Protein (N-His) is a recombinant protein expressed in E. coli, spanning Gly387-Asp619, with an N-terminal His tag. Predicted molecular weight: 28.03 kDa. Purity: >90% as determined by SDS-PAGE. Supplied lyophilized from a solution in PBS pH 7.4, 0.02% NLS, 1 mM EDTA, 4% Trehalose, 1% Mannitol. Applications: ELISA, immunogen, SDS-PAGE and Western blot. E3 ubiquitin-protein ligase DTX4 is a ~67 kDa protein. Regulator of Notch signaling, a signaling pathway involved in cell-cell communications that regulates a broad spectrum of cell-fate determinations. For research use only.
Functions as a ubiquitin ligase protein in vivo, mediating 'Lys48'-linked polyubiquitination and promoting degradation of TBK1, targeting to TBK1 requires interaction with NLRP4.
| Product Name: | Human DTX4 Recombinant Protein (N-His) |
| SKU: | GXRP04644 |
| Size: | 50 µg, 100 µg, 1 mg |
| Species: | Human |
| Synonyms: | RING finger protein 155, Protein deltex-4, RNF155, KIAA0937, RING-type E3 ubiquitin transferase DTX4, E3 ubiquitin-protein ligase DTX4, DTX4, Deltex4 |
| Tag: | N-His |
| Expression Host: | E. coli |
| Protein Length: | Gly387-Asp619 |
| Calculated MW: | 28.03 kDa |
| UniProt: | Q9Y2E6 |
| Applications: | ELISA, Immunogen, SDS-PAGE, WB |
| Purity: | >90% as determined by SDS-PAGE. |
| Form: | Lyophilized |
| Formulation: | Lyophilized from a solution in PBS pH 7.4, 0.02% NLS, 1 mM EDTA, 4% Trehalose, 1% Mannitol. |
| Reconstitution: | Reconstitute in sterile water for a stock solution. Adjust the volume of sterile water so that, after reconstitution, the final stock concentration matches the value indicated on the product label or datasheet. |
| Storage: | Store at 2 to 8°C for frequent use. Store at -20 to -80°C for twelve months from the date of receipt. |
| Shipping: | In general, proteins are provided as lyophilized powder/frozen liquid. They are shipped out with dry ice/blue ice unless customers require otherwise. |
| Note: | For research use only. |