Human Papilloma Virus type 11 (HPV 11) Regulatory Protein E1 (His) is expressed in E. coli expression system with N-6xHis tag. The predicted molecular weight is 23.1 kDa and the accession number is P04014.
| 説明 |
Human Papilloma Virus type 11 (HPV 11) Regulatory Protein E1 (His) is expressed in E. coli expression system with N-6xHis tag. The predicted molecular weight is 23.1 kDa and the accession number is P04014. |
| Species |
HPV 11
|
| Expression Host |
E. coli
|
| Tag |
N-6xHis
|
| Accession Number |
P04014
|
| Amino Acid |
IEFIPFLSKLKLWLHGTPKKNCIAIVGPPDTGKSCFCMSLIKFLGGTVISYVNSCSHFWLQPLTDAKVALLDDATQPCWTYMDTYMRNLLDGNPMSIDRKHRALTLIKCPPLLVTSNIDISKEEKYKYLHSRVTTFTFPNPFPFDRNGNAV
|
| Construction |
452-602 aa
|
| Protein Purity |
> 85% as determined by SDS-PAGE.
|
| 分子量 |
23.1 kDa (predicted)
|
| Formulation |
If the delivery form is liquid, the default storage buffer is Tris/PBS-based buffer, 5%-50% glycerol. If the delivery form is lyophilized powder, the buffer before lyophilization is Tris/PBS-based buffer, 6% Trehalose, pH 8.0.
|
| Reconstitution |
A Certificate of Analysis (CoA) containing reconstitution instructions is included with the products. Please refer to the CoA for detailed information.
|
| Stability & Storage |
Lyophilized powders can be stably stored for over 12 months, while liquid products can be stored for 6-12 months at-80℃. For reconstituted protein solutions, the solution can be stored at -20°c to -80'c for at least 3 months. Please avoid multiple freeze-thaw cycles and store products in aliquots.
|
| Shipping |
In general, Lyophilized powders are shipping with blue ice. Solutions are shipping with dry ice.
|
| Research Background |
ATP-dependent DNA helicase required for initiation of viral DNA replication. It forms a complex with the viral E2 protein. The E1-E2 complex binds to the replication origin which contains binding sites for both proteins. During the initial step, a dimer of E1 interacts with a dimer of protein E2 leading to a complex that binds the viral origin of replication with high specificity. Then, a second dimer of E1 displaces the E2 dimer in an ATP-dependent manner to form the E1 tetramer. Following this, two E1 monomers are added to each half of the site, which results in the formation of two E1 trimers on the viral ori. Subsequently, two hexamers will be created. The double hexamer acts as a bi-directional helicase machinery and unwinds the viral DNA and then recruits the host DNA polymerase to start replication.
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