HSP90AA1 Antibody (Acetyl-Lys435)

Polyclonal Antibody

ISGylated. S-nitrosylated; negatively regulates the ATPase activity and the activation of eNOS by HSP90AA1.

50/85 kDa

HSP90AA1

Liquid. PBS containing 50% glycerol, 0.5% BSA and 0.02% sodium azide.

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. Apart from its chaperone activity, it also plays a role in the regulation of the transcription machinery.

The antibody was affinity-purified from rabbit antiserum by affinity-chromatography using epitope-specific immunogen.

Acetyl-HSP 90 (K435) Polyclonal Antibody detects endogenous levels of HSP 90 protein only when acetylated at K435.