The 90 kDa molecular chaperone family includes 90 kDa heat shock protein Hsp90 and 94 kDa glucose-regulated protein grp94, both major molecular chaperones of the cytosol and the endoplasmic reticulum. Mammalian cells contain isoforms Hsp90 alpha and Hsp90 beta, encoded by separate genes. The amino acid sequences of human and yeast Hsp90 alpha are 85% and 90% homologous to those of Hsp90 beta, respectively. All known members of the Hsp90 protein family are highly conserved, especially in the N -terminal and C-terminal regions containing independent chaperone sites with different substrate specificity. These ubiquitous and highly conserved proteins account for 1-2% of all cellular proteins in most cells. Hsp90 functions as part of the cell

• For Western Blot

Recognizes human and chicken HSP90alpha. Detects a band of ~90kDa by Western blot.

Type: Primary
Antigen: HSP90A
Clonality: Monoclonal
Clone:
Conjugation: HRP (Horseradish Peroxidase)
Epitope:
Host: Rat
Isotype: IgG2a
Reactivity: Human