| 説明 |
HSP 90-alpha 1 Protein, Danio rerio, Recombinant (His & Myc) is expressed in Baculovirus insect cells with N-10xHis and C-Myc tag. The predicted molecular weight is 27.9 kDa and the accession number is Q90474. |
| Species |
Danio rerio (Zebrafish)
|
| Expression Host |
Baculovirus Insect Cells
|
| Tag |
N-10xHis, C-Myc
|
| Accession Number |
Q90474
|
| Amino Acid |
HNDDEQYIWESAAGGSFTVKPDFGESIGRGTKVILHLKEDQSEYVEEKRIKEVVKKHSQFIGYPITLYIEKQREKEVDLEEGEKQEEEEVAAGEDKDKPKIEDLGADEDEDSKDGKNKRKKKVKEKYIDAQELNKTKPIWTRNPDDITNEEYGEFYKSLSNDWEDHLAVKHFSVEGQLEFRALLFVPRRAAFDLFENKKKRNNIK
|
| Construction |
151-355 aa
|
| Protein Purity |
> 85% as determined by SDS-PAGE.
|
| 分子量 |
27.9 kDa (predicted)
|
| Formulation |
Tris-based buffer, 50% glycerol
|
| 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 proteinsolutions, 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 |
Molecular chaperone that promotes the maturation, structural maintenance and proper regulation of specific target proteins involved for instance in cell cycle control and signal transduction. Undergoes a functional cycle that is linked to its ATPase activity which is essential for its chaperone activity. This cycle probably induces conformational changes in the client proteins, thereby causing their activation. Interacts dynamically with various co-chaperones that modulate its substrate recognition, ATPase cycle and chaperone function. Engages with a range of client protein classes via its interaction with various co-chaperone proteins or complexes, that act as adapters, simultaneously able to interact with the specific client and the central chaperone itself. Recruitment of ATP and co-chaperone followed by client protein forms a functional chaperone. After the completion of the chaperoning process, properly folded client protein and co-chaperone leave HSP90 in an ADP-bound partially open conformation and finally, ADP is released from HSP90 which acquires an open conformation for the next cycle. Plays a key role in slow and fast muscle development in the embryo. Plays a role in myosin expression and assembly.
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