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

All Hsp90 alpha reagents are produced in house and quality controlled, including 2 Hsp90 alpha Antibody, 45 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 alpha antibodies are validated with different applications, which are WB, ICC/IF, IF, IP, IHC-P.

Hsp90 alpha cDNA 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 (2)

Application Clonality

Anti-Hsp90 alpha Antibody


Specificity: Human

Application: WB,ICC/IF,IF,IP

Clonality: PAb

Human HSP90/HSP90AA1 Western blot (WB) 18180

Anti-Hsp90 alpha Antibody


Specificity: Mouse

Application: IHC-P

Clonality: PAb

Mouse Hsp90 alpha Immunohistochemistry(IHC) 19593

Hsp90 alpha cDNA Clone (45)


Hsp90 alpha qPCR Primer (2)

Heat shock protein 9 (9 kDa heat-shock protein, HSP9) 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. HSP9 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, HSP9 displays a multifaceted ability to influence signal transduction, chromatin remodelling and epigenetic regulation, development and morphological evolution. HSP9 operates as a dimer in a conformational cycle driven by ATP binding and hydrolysis at the N-terminus. Disruption of HSP9 leads to client protein degradation and often cell death. Under stressful conditions, HSP9 stabilizes its client proteins and provides protection to the cell against cellular stressors such as in cancer cells. Especially, several oncoproteins act as HSP9 client proteins and tumor cells require higher HSP9 activity than normal cells to maintain their malignancy. For this reason, Hsp9 has emerged as a promising target for anti-cancer drug development.