Description
Human CCT8 Recombinant Protein (N-His)
Human CCT8 Recombinant Protein (N-His) is a recombinant protein expressed in E. coli, spanning Glu26-Asp522, with an N-terminal His tag. Predicted molecular weight: 56.48 kDa. Purity: >90% as determined by SDS-PAGE. Supplied lyophilized from a solution in PBS pH 7.4, 1 mM EDTA, 4% Trehalose, 1% Mannitol. Applications: ELISA, immunogen, SDS-PAGE and Western blot. T-complex protein 1 subunit theta is a ~59 kDa protein. Component of the chaperonin-containing T-complex (TRiC), a molecular chaperone complex that assists the folding of actin, tubulin and other proteins upon ATP hydrolysis. For research use only.
The TRiC complex mediates the folding of WRAP53/TCAB1, thereby regulating telomere maintenance. As part of the TRiC complex may play a role in the assembly of BBSome, a complex involved in ciliogenesis regulating transports vesicles to the cilia.
| Product Name: | Human CCT8 Recombinant Protein (N-His) |
| SKU: | GXRP10788 |
| Size: | 50 µg, 100 µg, 1 mg |
| Species: | Human |
| Synonyms: | C21orf112, CCT-theta, CCT8, CCTQ, Chaperonin containing T-complex polypeptide 1 subunit 8, EC:3.6.1.-, KIAA0002, Renal carcinoma antigen NY-REN-15, T-complex protein 1 subunit theta, TCP-1-theta |
| Tag: | N-His |
| Expression Host: | E. coli |
| Protein Length: | Glu26-Asp522 |
| Calculated MW: | 56.48 kDa |
| UniProt: | P50990 |
| 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, 1 mM EDTA, 4% Trehalose, 1% Mannitol. |
| Reconstitution: | Reconstitute in sterile water for a stock solution. A copy of datasheet will be provided with the products, please refer to it for details. |
| 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 |