Mouse Heat Shock Protein 90,Hsp-90 ELISA Kit

Code CSB-E08312m
Size 96T,5×96T,10×96T How to order?
Trial Size 24T ELISA kits trial application
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Product Details


CUSABIO's Hsp90 mouse ELISA kit is an in vitro enzyme-linked immunosorbent assay for the quantitative measurement of mouse Hsp90 in serum, plasma, or tissue homogenates. This assay uses an antibody specific to mouse Hsp90 coated on a 96-well plate. Hsp90 present in a sample is bound to the wells by the immobilized antibody after adding the sample to the wells. Biotinylated Hsp90 antibody is added to the wells, forming an antibody-analyte-antibody complex. HRP-conjugated avidin is pipetted to the wells and binds to the complex. A TMB substrate solution is added to the wells and color develops in proportion to the amount of Hsp90 bound. The addition of Stop Solution changes the color from blue to yellow, and the intensity of the color is measured at 450 nm using a microplate reader.

Hsp90 is a highly abundant and ubiquitous molecular chaperone essential for many cellular processes including cell cycle control, cell survival, hormone, and other signaling pathways. Hsp90 takes part in the proper folding and maintenance of its client proteins in eukaryotic cells including protein kinases, transcription factors, and E3 ubiquitin ligases, thus positioning as a central regulator of cellular proteostasis. It is also important for the cell's response to stress and is a key player in maintaining cellular homeostasis.

Target Name heat shock protein 90kDa alpha (cytosolic), class A member 1
Alternative Names Hsp90aa1 ELISA Kit; Hsp86 ELISA Kit; Hsp86-1 ELISA Kit; HspcaHeat shock protein HSP 90-alpha ELISA Kit; Heat shock 86 kDa ELISA Kit; HSP 86 ELISA Kit; HSP86 ELISA Kit; Tumor-specific transplantation 86 kDa antigen ELISA Kit; TSTA ELISA Kit
Abbreviation HSP90AA1
Uniprot No. P07901
Species Mus musculus (Mouse)
Sample Types serum, plasma, tissue homogenates
Detection Range 0.156 ng/mL-10 ng/mL
Sensitivity 0.039 ng/mL
Assay Time 1-5h
Sample Volume 50-100ul
Detection Wavelength 450 nm
Research Area Neuroscience
Assay Principle quantitative
Measurement Sandwich
Intra-assay Precision (Precision within an assay): CV%<8%      
Three samples of known concentration were tested twenty times on one plate to assess.  
Inter-assay Precision (Precision between assays): CV%<10%      
Three samples of known concentration were tested in twenty assays to assess.    
To assess the linearity of the assay, samples were spiked with high concentrations of mouse Hsp-90 in various matrices and diluted with the Sample Diluent to produce samples with values within the dynamic range of the assay.
  Sample Serum(n=4)  
1:5 Average % 93  
Range % 81-101  
1:10 Average % 95  
Range % 86-104  
1:20 Average % 95  
Range % 82-105  
1:40 Average % 93  
Range % 82-101  
The recovery of mouse Hsp-90 spiked to levels throughout the range of the assay in various matrices was evaluated. Samples were diluted prior to assay as directed in the Sample Preparation section.
Sample Type Average % Recovery Range  
Serum (n=5) 95 90-105  
EDTA plasma (n=4) 95 89-110  
Typical Data
These standard curves are provided for demonstration only. A standard curve should be generated for each set of samples assayed.
ng/ml OD1 OD2 Average Corrected  
10 2.773 2.787 2.780 2.665  
5 1.842 1.740 1.791 1.676  
2.5 1.105 1.164 1.135 1.020  
1.25 0.668 0.673 0.671 0.556  
0.625 0.398 0.403 0.401 0.286  
0.312 0.282 0.266 0.274 0.159  
0.156 0.159 0.152 0.156 0.041  
0 0.112 0.118 0.115    
ELISA Data Analysis Watch ELISA data processing video & download Curve Expert if needed
and FAQs
Storage Store at 2-8°C. Please refer to protocol.
Lead Time 3-5 working days

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Target Background

(From Uniprot)
Molecular chaperone that promotes the maturation, structural maintenance and proper regulation of specific target proteins involved for instance in cell cycle control and signal transduction. Undergoes a functional cycle that is linked to its ATPase activity which is essential for its chaperone activity. This cycle probably induces conformational changes in the client proteins, thereby causing their activation. Interacts dynamically with various co-chaperones that modulate its substrate recognition, ATPase cycle and chaperone function. Engages with a range of client protein classes via its interaction with various co-chaperone proteins or complexes, that act as adapters, simultaneously able to interact with the specific client and the central chaperone itself. Recruitment of ATP and co-chaperone followed by client protein forms a functional chaperone. After the completion of the chaperoning process, properly folded client protein and co-chaperone leave HSP90 in an ADP-bound partially open conformation and finally, ADP is released from HSP90 which acquires an open conformation for the next cycle. Plays a critical role in mitochondrial import, delivers preproteins to the mitochondrial import receptor TOMM70. Apart from its chaperone activity, it also plays a role in the regulation of the transcription machinery. HSP90 and its co-chaperones modulate transcription at least at three different levels. In the first place, they alter the steady-state levels of certain transcription factors in response to various physiological cues. Second, they modulate the activity of certain epigenetic modifiers, such as histone deacetylases or DNA methyl transferases, and thereby respond to the change in the environment. Third, they participate in the eviction of histones from the promoter region of certain genes and thereby turn on gene expression. Binds bacterial lipopolysaccharide (LPS) and mediates LPS-induced inflammatory response, including TNF secretion by monocytes. Antagonizes STUB1-mediated inhibition of TGF-beta signaling via inhibition of STUB1-mediated SMAD3 ubiquitination and degradation. Mediates the association of TOMM70 with IRF3 or TBK1 in mitochodria outer membrane which promotes host antiviral response.
Gene References into Functions
  1. The study shows that a conserved tryptophan in the middle domain senses the interaction of Hsp90 with a stringent client protein and transfers this information via a cation-pi interaction with a neighboring lysine. PMID: 29662162
  2. Fusion of human SGT1 (hSGT1) to NOD1 LRR significantly enhanced the solubility, and the fusion protein was stabilized by coexpression of mouse Hsp90alpha. PMID: 27591899
  3. The major capsid protein of the mouse polyomavirus VP1 binds microtubules, HSP90, promotes their acetylation and blocks the host cell cycle. PMID: 27885808
  4. Artificially maintaining Hsp90alpha or knocking down Aarsd1L expression interferes with the differentiation of C2C12 myotubes. PMID: 26884463
  5. Immune-mediated destruction of ovarian follicles associated with the presence of HSP90 antibodies. PMID: 25653208
  6. identify that Hsp90alpha at the transition neck region represents a signalling platform on which IRS-1 interacts with intracellular downstream signalling molecules involved in IGF-1 receptor signalling. PMID: 25359884
  7. The study demonstrated that HSP90alpha plays an important role in the biogenesis of fetal PIWI-interacting RNAs (piRNA), which act against the transposon activities, in mouse male germ cells. PMID: 25262350
  8. deficiency does not affect immunoglobulin gene hypermutation and class switch but causes enhanced MHC class II antigen presentation PMID: 22855849
  9. study identified the essential role of Hsp90 in iNOS gene transactivation PMID: 21430289
  10. Hsp90alpha may be required to maintain and to activate these regulators and/or to disassemble the synaptonemal complex that holds homologous chromosomes together PMID: 21209834
  11. extracellular Hsp90alpha promotes angiogenesis in an MMP-2-dependent manner. PMID: 20937816
  12. Hsp90-ovalbumin peptide complexes bind to scavenger receptor expressed by endothelial cells (SREC-I) on the surface of antigen presenting cells. PMID: 20686127
  13. Endogenous HSP90 is essential for cross-presentation of both soluble and cell-associated antigens in dendritic cells. PMID: 20668218
  14. KLF4 inhibition by antisense oligonucleotides markedly decreased the constitutive expression of HSP90 (HSP84 and HSP86). PMID: 19669938
  15. Following exposure to elevated temperatures, higher amounts of Hsp90alpha are inside the nucleus, but not within the nucleoli. PMID: 12713799
  16. Heat shock protein 90 is an endogenous protein enhancer of inducible nitric-oxide synthase PMID: 12855682
  17. by induction of HSP90A c-Myc may control the activity of multiple signal pathways involved in cellular transformation PMID: 14724288
  18. HSPB1 pathway is important during trophoblast stem cell differentiation PMID: 17267699
  19. Hsp90 promotes activation of the Fanconi anemia pathway through regulation of intracellular turnover and trafficking of FANCA PMID: 17327415
  20. Unlike Hsp90beta, Hsp90alpha is not associated with regulation of the antiapoptotic response of immune cells. PMID: 17475835
  21. Blocking Hsp90 disrupts IGF-I and IL-6-induced proangiogenic signaling cascades by targeting IGF-IR and STAT3 in pancreatic cancer PMID: 17975158
  22. These results demonstrate a substantial role for hsp90 in chaperoning of antigenic peptides in direct and indirect presentation. PMID: 18216248
  23. Melusin directly binds to Hsp90, a ubiquitous chaperone involved in regulating several signaling pathways. PMID: 18474241
  24. mammalian Unc45b is a cytosolic protein that forms a stable complex with Hsp90, selectively binds the unfolded conformation of the myosin motor domain, and promotes motor domain folding PMID: 18478096
  25. A possible role of Hsp86 in mouse suprachiasmatic nucleus is association with circadian rhythms. PMID: 18480550
  26. Hsp90 regulates cPLA(2)alpha-mediated arachidonic acid release that involves association of a p54 kinase with cPLA(2)alpha upon okadaic acid stimulation PMID: 18550790
  27. hsp90 facilitates MHC class I antigen processing through epitope production in a complex of the 26 S proteasome PMID: 18703510
  28. the complex role played by Hsp90 in regulating signal transduction pathways in normal tissues as well as in cancer cells. PMID: 18840695

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Subcellular Location Nucleus. Cytoplasm. Melanosome. Cell membrane. Mitochondrion.
Protein Families Heat shock protein 90 family
Database Links

KEGG: mmu:15519

STRING: 10090.ENSMUSP00000021698

UniGene: Mm.1843

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