Human HSP90/HSP90AA1 recombinant protein

Human HSP90/HSP90AA1 recombinant protein

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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.

Epididymis luminal secretory protein 52

RP23-60K23.1; LAP-2; HSPN; HSP90AA1; FLJ31884; EL52; HSP 86; 89KDA; HSPCA; HSP86-1; AL024080; HSP89A; HSPCAL1; HSP4; 86KDA; AL024147; HSPC1; HSP90N; HSP90A; HSP86; HSPCAL4; HSP89; LAP2; HSP90

P07900

EL52; HSP90AA1; hCG_1814169

E. coli

A DNA sequence encoding the human HSP90 isoform 2 (NP_005339.3) C-terminal segment, corresponding to amino acid sequence (Glu 535-Asp 732) was expressed and purified, with two additonal aa (Gly & Pro) at the N terminus.

Human

The recombinant human HSP90 (aa 535-732) consisting of 200 amino acids and has a calculated molecular mass of 22.6 kDa. It migrates as an 24 kDa band in SDS-PAGE under reducing conditions.

> 97 % as determined by SDS-PAGE