Recombinant Heat shock protein HSP 90-beta (hsp90ab1), partial - CD BioSciences

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Recombinant Heat shock protein HSP 90-beta (hsp90ab1), partial

Recombinant Heat shock protein HSP 90-beta (hsp90ab1), partial

SPP-02450

Size Price
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100 μg Online Inquiry
500 μg Online Inquiry
Target Information
Species Danio rerio
Target Name HSP90
UniProt No. O57521
Subcellular Location Cytoplasm
Tissue Specificity Detected throughout the embryo and in low levels in the musculature. Expressed predominantly in the developing brain, tail bud and cells surrounding the posterior margin of the yolk tube.
Gene Abbr. HSP90AB1
Full Name heat shock protein 90 alpha family class B member 1
Introduction 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. 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 (By similarity). Not required for myofibril formation in skeletal muscles.
Product Details
Product Type Recombinant Protein
Storage & Handling
Storage Temp. Store at -20 °C upon receipt unless otherwise instructed.
Handling Aliquoting is necessary for mutiple use. Avoid repeated freeze-thaw cycles.

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