Heat shock protein HSP 90-alpha 1 (hsp90a.1), partial, Danio rerio, recombinant

Organism: Danio rerio (Zebrafish) (Brachydanio rerio). Source: Baculovirus. Expression Region: 151-355aa. Protein Length: Partial. Tag Info: N-terminal 10xHis-tagged and C-terminal Myc-tagged. Target Protein Sequence: HNDDEQYIWE SAAGGSFTVK PDFGESIGRG TKVILHLKED QSEYVEEKRI KEVVKKHSQF IGYPITLYIE KQREKEVDLE EGEKQEEEEV AAGEDKDKPK IEDLGADEDE DSKDGKNKRK KKVKEKYIDA QELNKTKPIW TRNPDDITNE EYGEFYKSLS NDWEDHLAVK HFSVEGQLEF RALLFVPRRA AFDLFENKKK RNNIK. Purity: Greater than 85% as determined by SDS-PAGE. Endotoxin: Not test. Biological Activity: n/a. Form: Liquid or Lyophilized powder. Buffer: 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: We recommend that this vial be briefly centrifuged prior to opening to bring the contents to the bottom. Please reconstitute protein in deionized sterile water to a concentration of 0.1-1.0 mg/mL.We recommend to add 5-50% of glycerol (final concentration) and aliquot for long-term storage at -20 °C/-80 °C. Our default final concentration of glycerol is 50%. Customers could use it as reference. Storage: The shelf life is related to many factors, storage state, buffer ingredients, storage temperature and the stability of the protein itself. Generally, the shelf life of liquid form is 6 months at -20 °C/-80 °C. The shelf life of lyophilized form is 12 months at -20 °C/-80 °C. Notes: Repeated freezing and thawing is not recommended. Store working aliquots at 4 °C for up to one week. Relevance: 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. Reference: "HSP 90 alpha and HSP 90 beta genes are present in the zebrafish and are differentially regulated in developing embryos." Krone P.H., Sass J.B. Biochem. Biophys. Res. Commun. 204:746-752(1994). Function: nan