Recombinant Zebrafish Heat Shock Protein Hsp 90-Alpha 1 (HSP90A.1) Protein (His&Myc)
Beta LifeScience
SKU/CAT #: BLC-05089P
Greater than 85% as determined by SDS-PAGE.
Recombinant Zebrafish Heat Shock Protein Hsp 90-Alpha 1 (HSP90A.1) Protein (His&Myc)
Beta LifeScience
SKU/CAT #: BLC-05089P
Our products are highly customizable to meet your specific needs. You can choose options such as endotoxin removal, liquid or lyophilized forms, preferred tags, and the desired functional sequence range for proteins. Submitting a written inquiry expedites the quoting process.
Product Overview
| Description | Recombinant Zebrafish Heat Shock Protein Hsp 90-Alpha 1 (HSP90A.1) Protein (His&Myc) is produced by our Baculovirus expression system. This is a protein fragment. |
| Purity | Greater than 85% as determined by SDS-PAGE. |
| Uniprotkb | Q90474 |
| Target Symbol | HSP90A.1 |
| Synonyms | hsp90a.1; hsp90; hsp90a; hsp90aa1; zgc:86652Heat shock protein HSP 90-alpha 1 |
| Species | Danio rerio (Zebrafish) (Brachydanio rerio) |
| Expression System | Baculovirus |
| Tag | N-10His&C-Myc |
| Target Protein Sequence | HNDDEQYIWESAAGGSFTVKPDFGESIGRGTKVILHLKEDQSEYVEEKRIKEVVKKHSQFIGYPITLYIEKQREKEVDLEEGEKQEEEEVAAGEDKDKPKIEDLGADEDEDSKDGKNKRKKKVKEKYIDAQELNKTKPIWTRNPDDITNEEYGEFYKSLSNDWEDHLAVKHFSVEGQLEFRALLFVPRRAAFDLFENKKKRNNIK |
| Expression Range | 151-355aa |
| Protein Length | Partial |
| Mol. Weight | 27.9 kDa |
| Research Area | Others |
| Form | Liquid or Lyophilized powder |
| Buffer | Liquid form: default storage buffer is Tris/PBS-based buffer, 5%-50% glycerol. Lyophilized powder form: the buffer before lyophilization is Tris/PBS-based buffer, 6% Trehalose, pH 8.0. |
| Storage | 1. Store at -20°C/-80°C upon receipt, aliquoting is necessary for mutiple use. 2. Avoid repeated freeze-thaw cycles. 3. Store working aliquots at 4°C for up to one week. 4. In general, protein in liquid form is stable for up to 6 months at -20°C/-80°C. Protein in lyophilized powder form is stable for up to 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. |
Target Details
| Target Function | 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. |
| Subcellular Location | Melanosome. Cytoplasm, myofibril, sarcomere, Z line. Cytoplasm, myofibril, sarcomere, A band. Cytoplasm, perinuclear region. Note=Expressed at the Z line and in the perinuclear region of myofibrils. Shuttles between the Z line and A band in response to stress conditions and fibril damage. |
| Protein Families | Heat shock protein 90 family |
| Database References | KEGG: dre:30591 STRING: 7955.ENSDARP00000022302 UniGene: PMID: 29662162 |
