ELISA/assay

HSP90 alpha ELISA Kit

SKT-107

96 well

HSP90 alpha ELISA Kit

Colorimetric detection of HSP90 alpha

96 well

Cancer Heat Shock Cell Signaling Protein Trafficking Chaperone Proteins Cancer Tumor Biomarkers

HSP86, HSP89A, HSP90A, HSP90AA1, HSP90alpha, HSPC1, HSPCA, HsoCAL3

ELISA Kits

Colorimetric Assay

Sandwich ELISA (Enzyme-linked Immunosorbent Assay)

Sandwich

ELISA kit used to quantitate HSP90 alpha concentration in samples.

1. Prepare Standard and samples in Standard and Sample Diluent. 2. Add 100 µL of Standard or sample to appropriate wells. 3. Cover plate with Plate Sealer and incubate at 37°C for 1 hour. 4. Wash plate four times with 1X Wash Buffer. 5. Add 100 µL of Biotinylated Antibody Working Solution to each well. 6. Cover plate with Plate Sealer and incubate at room temperature, 20-25 °C for 1 hour. 7. Wash plate four times with 1X Wash Buffer. 8. Add 100 µL of Streptavidin-HRP Working Solution to each well. 9. Cover plate with Plate Sealer and incubate at room temperature for 30 minutes. 10. Wash plate four times with 1X Wash Buffer. 11. Add 100 µL of TMB Substrate to each well. 12. Develop the plate in the dark at room temperature for 30 minutes. 13. Stop reaction by adding 100 µL of Stop Solution to each well. 14. Measure absorbance on a plate reader at 450 nm.

Human Goat Avian

Cell Lysates Tissue Serum Whole Blood

40 samples in duplicate

30 minutes

0.117 ng/ml

0.44 - 28 ng/ml

Heat Shock Protein 90 (HSP90) is a highly conserved molecular chaperone essential for maintaining protein homeostasis across all eukaryotic cells. Although classified as a stress protein, HSP90 is abundantly expressed even under non-stress conditions, comprising up to 2% of cytosolic protein. Its core functions include the folding, maturation, stabilization, and trafficking of a wide range of client proteins. HSP90 plays a pivotal role in regulating key signaling molecules such as kinases (v-Src, Wee1, c-Raf), transcription factors (p53), steroid receptors, and enzymes like telomerase and viral polymerases. These interactions are mediated through ATP-dependent conformational changes and co-chaperone complexes involving Cdc37, p23, and immunophilin-like proteins, which protect client proteins from proteasomal degradation. In neuroscience, HSP90 is increasingly recognized for its role in modulating protein misfolding and aggregation—central features of neurodegenerative diseases such as Alzheimer’s, Parkinson’s, and Huntington’s. Alterations in HSP90 expression or function can disrupt neuronal signaling and impair the activity of neuroprotective proteins, contributing to disease progression. Pharmacological inhibitors of HSP90, including geldanamycin and radicicol, are being explored as therapeutic agents to restore proteostasis and reduce toxic protein accumulation in neurodegenerative models.

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