Anti-Hsp90 alpha/HSP90AA1 Antibody

At -20°C for one year. After reconstitution, at 4°C for one month. It can also be aliquotted and stored frozen at -20°C for a longer time.Avoid repeated freezing and thawing.

HSP90AA1

Heat shock protein HSP 90-alpha is a protein that in humans is encoded by the HSP90AA1 gene. The gene, HSP90AA1, encodes the human stress-inducible 90-kDa heat shock protein alpha (Hsp90A). Complemented by the constitutively expressed paralog Hsp90B which shares over 85% amino acid sequence identity, Hsp90A expression is initiated when a cell experiences proteotoxic stress. Once expressed Hsp90A dimers operate as molecular chaperones that bind and fold other proteins into their functional 3-dimensional structures. This molecular chaperoning ability of Hsp90A is driven by a cycle of structural rearrangements fueled by ATP hydrolysis. Current research on Hsp90A focuses in its role as a drug target due to its interaction with a large number of tumor promoting proteins and its role in cellular stress adaptation.

Each vial contains 5 mg BSA, 0.9mg NaCl, 0.2mg Na2HPO4, 0.05 mg Thimerosal, 0.05 mg NaN3.

Add 0.2 ml of distilled water will yield a concentration of 500 ug/ml.

|signal transduction|protein trafficking|chaperones|heat shock proteins| cancer|tumor biomarkers

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. Binds bacterial lipopolysaccharide (LPS) et mediates LPS-induced inflammatory response, including TNF secretion by monocytes.