Recombinant Human E2F2 protein (His tag)
SKU: PDEH100410-100
To better serve you, we would like to discuss your specific requirement.
Please Contact Us for a quote.
Recombinant Human E2F2 protein (His tag)
SKU # | PDEH100410 |
Expression Host | E. coli |
Description
Synonyms | Transcription factor E2F2;E2F2; |
Species | Human |
Expression_host | E.coli |
Sequence | Ala 65-Asn 437 |
Accession | Q14209 |
Mol_Mass | 40.9 kDa |
AP_Mol_Mass | 55 kDa |
Tag | N-His |
Bio_Activity | Not validated for activity |
Propertie
Purity | > 95 % as determined by reducing SDS-PAGE. |
Endotoxin level | Please contact us for more information. |
Storage | Generally, lyophilized proteins are stable for up to 12 months when stored at -20 to -80℃. Reconstituted protein solution can be stored at 4-8℃ for 2-7 days. Aliquots of reconstituted samples are stable at < -20℃ for 3 months. |
Shipping | This product is provided as lyophilized powder which is shipped with ice packs. |
Formulation | Lyophilized from sterile PBS, pH 7.4. Normally 5 % - 8 % trehalose, mannitol and 0.01% Tween80 are added as protectants before lyophilization. Please refer to the specific buffer information in the printed manual. |
Reconstitution | It is recommended that sterile water be added to the vial to prepare a stock solution of 0.5 mg/mL. Concentration is measured by UV-Vis |
Background
The protein encoded by this gene is a member of the E2F family of transcription factors. The E2F family plays a crucial role in the control of cell cycle and action of tumor suppressor proteins and is also a target of the transforming proteins of small DNA tumor viruses. The E2F proteins contain several evolutionally conserved domains found in most members of the family. These domains include a DNA binding domain, a dimerization domain which determines interaction with the differentiation regulated transcription factor proteins (DP), a transactivation domain enriched in acidic amino acids, and a tumor suppressor protein association domain which is embedded within the transactivation domain. This protein and another 2 members, E2F1 and E2F3, have an additional cyclin binding domain. This protein binds specifically to retinoblastoma protein pRB in a cell-cycle dependent manner, and it exhibits overall 46% amino acid identity to E2F1.