Hsp90 alpha (Protein|Antibody|cDNA Clone|ELISA Kit)

All Hsp90 alpha reagents are produced in house and quality controlled, including 1 Hsp90 alpha Antibody, 42 Hsp90 alpha Gene, 1 Hsp90 alpha Protein, 2 Hsp90 alpha qPCR. All Hsp90 alpha reagents are ready to use.

Recombinant Hsp90 alpha proteins are expressed by E. coli with fusion tags as N-cleavage.

Hsp90 alphaantibodies are validated with different applications, which are WB, ICC/IF, IF, IP.

Hsp90 alphacDNA clones are full length sequence confirmed and expression validated. There are 13 kinds of tags for each Hsp90 alpha of different species, especially GFP tag, OFP tag, FLAG tag and so on. There are three kinds of vectors for choice, cloning vector, expression vector and lentivrial expression vector.

Hsp90 alpha Protein (1)


Hsp90 alpha Protein, Human, Recombinant


Expression host: E. coli

Human HSP90/HSP90AA1 Protein 9577

Hsp90 alpha Antibody (1)

Application Clonality

Anti-Hsp90 alpha Antibody


Application: WB,ICC/IF,IF,IP

Clonality: PAb

Human HSP90/HSP90AA1 Western blot (WB) 18180

Hsp90 alpha cDNA Clone (42)


Hsp90 alpha qPCR Primer (2)

Heat shock protein 90 (90 kDa heat-shock protein, HSP90) is a molecular chaperone involved in the trafficking of proteins in the cell. It is a remarkably versatile protein involved in the stress response and in normal homoeostatic control mechanisms. HSP90 interacts with 'client proteins', including protein kinases, transcription factors and others, and either facilitates their stabilization and activation or directs them for proteasomal degradation. By this means, HSP90 displays a multifaceted ability to influence signal transduction, chromatin remodelling and epigenetic regulation, development and morphological evolution. HSP90 operates as a dimer in a conformational cycle driven by ATP binding and hydrolysis at the N-terminus. Disruption of HSP90 leads to client protein degradation and often cell death. Under stressful conditions, HSP90 stabilizes its client proteins and provides protection to the cell against cellular stressors such as in cancer cells. Especially, several oncoproteins act as HSP90 client proteins and tumor cells require higher HSP90 activity than normal cells to maintain their malignancy. For this reason, Hsp90 has emerged as a promising target for anti-cancer drug development.