Recombinant Human Hsp90 alpha

Nucleus , Cytoplasm , Melanosome , Cell membrane , Mitochondrion , Note=Identified by mass spectrometry in melanosome fractions from stage I to stage IV.

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 rPubMed:11274138, PubMed:11276205, PubMed:12526792, PubMed:15577939, PubMed:15937123, PubMed:20628368, PubMed:24613385, PubMed:25609812, PubMed:27353360, PubMed:29127155, PubMed:25973397, PubMed:26991466, PubMed:27295069}.

Store at 4°C if entire vial will be used within 2-4 weeks of receipt. Store at or below -20°C for longer periods of time. Addition of a carrier protein (such as 0.1% HSA or BSA) is recommended for long term-storage.

Hsp90, a mammalian heat shock protein, is a molecular chaperone that helps to keep a target protein in a folding- competent state. It has been found in cell cytosol, nucleus, and endoplasmic reticulum of many different tissues. Hsp90 functions as a dimer. It has an ATP-binding site and low ATPase activity. Its chaperone activity is enhanced at high temperatures, and its function is sensitive to bivalent cation concentrations.