Application Note
IHC-P: Use at an assay dependent dilution. IP: Use at an assay dependent dilution. Detects both free and complexed Hsp90 and also picks up both hsp90 alpha and beta equally well (detects 100ng of each). WB: Use at a concentration of 2 μg/ml. Detects a band of approximately 90 kDa (predicted molecular weight: 83.2 kDa (beta) & 84.5 kDa (alpha)). Optimal dilutions/concentrations should be determined by the end user.
Positive Control
Heat-shocked HeLa cell lysate and Hsp90 protein
Product Note
Detects both the alpha and beta isoforms of Hsp90
Form
Liquid
Buffer
PBS, 50% Glycerol, 0.1mM PMSF
Preservative
No preservative
Storage
Store as concentrated solution. Centrifuge briefly prior to opening vial. For short-term storage (1-2 weeks), store at 4ºC. For long-term storage, aliquot and store at -20ºC or below. Avoid multiple freeze-thaw cycles.
Concentration
1 mg/ml (Please refer to the vial label for the specific concentration.)
Antigen Species
Human
Immunogen
Human Hsp90 purified from therapeutic orchiectomy specimens.
Purification
Protein G affinity purified
Conjugation
Unconjugated
RRID
AB_370555
Note
For laboratory research use only. Not for any clinical, therapeutic, or diagnostic use in humans or animals. Not for animal or human consumption.
Purchasers shall not, and agree not to enable third parties to, analyze, copy, reverse engineer or otherwise attempt to determine the structure or sequence of the product.
Synonyms
FLJ31884 heat shock 90kDa protein 1 alpha Heat shock protein HSP 90 alpha HSP86 Hsp89 HSP90A HSPC1 HSPCAL1 HSPN LAP2 Lipopolysaccharide associated protein2 LPS associated protein 2
Cellular Localization
Cytoplasmic
Background
The 90kDa molecular chaperone family comprises several proteins including the 90kDa heat shock protein, Hsp90 and the 94kDa glucose regulated protein, grp94 which are major molecular chaperones of the cytosol and of the endoplasmic reticulum. In mammalian cells there are at least two Hsp90 isoforms, Hsp90a and hsp90s which are encoded by separate genes. The amino acid sequence of human and yeast Hsp90a is 85% and 90% homologous to that of Hsp90s respectively. All known members of the Hsp90 protein family are highly conserved, especially in the N terminal and C terminal regions which have been shown to contain 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 is part of the cell's powerful network of chaperones to fight the deleterious consequences of protein unfolding caused by nonphysiological conditions. However, in the absence of stress, Hsp90 is a necessary component of fundamental cellular processes such as hormone signaling and cell cycle control. In this context several key regulatory proteins such as steriod receptors, cell cycle kinases involved in signal transduction and p53 have been identified as substrates of Hsp90. It has been suggested that Hsp90 acts as a capacitor for morphological evolution by buffering widespread variation, which may affect morphogenic pathways.
Research Area