Human heat shock protein 90α (HSP-90α) ELISA kit

Product Details

Customer Reviews and Q&A

Citations

Target Background

Name: Human heat shock protein 90α (HSP-90α) ELISA kit
Brand: CUSABIO
SKU: CSB-E13462h

Promotion

Code: CSB-E13462h

Rate （N/A）
Review （0）
Citation （4）

Compare

Size:

96T,5×96T,10×96T

Pls inquire

Quantity:

Sample Types: serum, plasma, tissue homogenates

Detect Range: 0.78 ng/mL-50 ng/mL

Sensitivity: 0.195 ng/mL

Trial Size:

24T ELISA Kit Trial Size (Only USD$150/ kit)
* Sample kit cost can be deducted as a $30 credit for each 96-assay kit of the same analyte and brand you subsequently purchase within six months until depleted. More details >>

Interested in a trial size? Please leave a message below.

Send an Inquiry

Start an on-line Chat

Online ordering is currently available for U.S. customers only. For orders outside the U.S., please kindly submit an inquiry or start a chat with us.

Promotion

Product Details
Related Products
Customer Reviews and Q&A
Target Background

Alternative Names

Heat shock 86 kDa ELISA Kit; Heat shock protein 90kDa alpha cytosolic class A member 1 ELISA Kit; Heat shock protein 90kDa alpha cytosolic class B member 1 ELISA Kit; Heat shock protein HSP 90 alpha ELISA Kit; Heat shock protein HSP 90 beta ELISA Kit; Heat shock protein HSP 90-alpha ELISA Kit; HS90A_HUMAN ELISA Kit; HSP 84 ELISA Kit; HSP 86 ELISA Kit; Hsp 90 ELISA Kit; HSP86 ELISA Kit; HSP90A ELISA Kit; HSP90AA1 ELISA Kit; HSP90AB1 ELISA Kit; HSP90B ELISA Kit; HSPC1 ELISA Kit; HSPC2 ELISA Kit; HSPCAL1 ELISA Kit; HSPCAL4 ELISA Kit; Renal carcinoma antigen NY-REN-38 ELISA Kit

Abbreviation

HSP90AA1

Uniprot NO.

P07900

Species

Homo sapiens (Human)

Sample Type

serum, plasma, tissue homogenates

Detection Range

0.78 ng/mL-50 ng/mL

Sensitivity

0.195 ng/mL

Assay Time

1-5h

Sample Loading Volume

50-100ul

Detection Wavelength

450 nm

Research Area

Neuroscience

Assay Principle

quantitative
The tag type will be determined during production process. If you have specified tag type, please tell us and we will develop the specified tag preferentially.

Measurement

Sandwich

Storage

Store at 2-8°C. Please refer to protocol.

Shelf Life

6 months

Lead Time

3-5 working days after you place the order, and it takes another 3-5 days for delivery via DHL or FedEx.
Note: All of our proteins are default shipped with normal blue ice packs, if you request to ship with dry ice, please communicate with us in advance and extra fees will be charged.

Precision

Linearity

To assess the linearity of the assay, samples were spiked with high concentrations of human HSP-90α 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 %	90-95
1:10	Average %	104
	Range %	100-107
1:20	Average %	94
	Range %	89-97
1:40	Average %	99
	Range %	92-103

Recovery

The recovery of human HSP-90α 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)	94	89-97
EDTA plasma (n=4)	94	91-97

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
50	2.712	2.699	2.706	2.569
25	2.013	2.002	2.008	1.871
12.5	1.400	1.422	1.411	1.274
6.25	0.804	0.788	0.796	0.659
3.12	0.424	0.428	0.426	0.289
1.56	0.349	0.341	0.345	0.208
0.78	0.245	0.234	0.240	0.103
0	0.139	0.135	0.137

Troubleshooting and FAQs

ELISA kit FAQs

ELISA Data Analysis

ELISA Standard Curve & Curve Expert software

Description

Heat shock protein 90α (HSP-90α) is a molecular chaperone that plays a key role in protein folding, cellular signaling, and stress response mechanisms. As a member of the HSP90 family, this protein helps fold and stabilize many client proteins, including kinases, transcription factors, and steroid hormone receptors. Cells express HSP-90α constitutively, but levels increase under stress conditions. This makes the protein essential for cellular homeostasis and survival. Its role in cancer progression, neurodegenerative diseases, and inflammatory responses has made it an important target for biomedical research.

The Human heat shock protein 90α (HSP-90α) ELISA kit (CSB-E13462h) provides quantitative detection of HSP-90α in human samples. This sandwich-based assay works with serum, plasma, and tissue homogenates. The detection range spans 0.78 ng/mL to 50 ng/mL with sensitivity of 0.195 ng/mL. The assay needs 50-100 μL sample volume and takes 1-5 hours to complete. Detection occurs at 450 nm wavelength, giving researchers a reliable tool for measuring HSP-90α levels in various biological specimens.

Application Examples

Note: The following application examples are drawn from a selection of publications citing this product. For additional applications, please refer to the full list of references in the "Citations" section.

This ELISA kit has been used in research studies to quantify heat shock protein levels in human serum samples and cell culture media. The assay allows researchers to study protein expression changes across different experimental conditions and examine how cytotoxic substances affect heat shock protein expression.

• Biomarker profiling - Quantification of heat shock protein levels in serum samples as part of multi-protein expression analysis comparing different experimental groups
• Cell culture studies - Detection of secreted heat shock protein levels in cell culture supernatants to examine cellular protein secretion patterns
• Cytotoxicity research - Evaluation of heat shock protein expression changes in response to cytotoxic substance exposure
• Comparative expression analysis - Measurement of protein level changes between control and experimental conditions in research settings

■ Customer Reviews

Submit a Review here

■ Q&A

Can you please tell me if your kit CSB-E13462h, is specific to HSP-90 alpha only? If so, do you have evidence of this?

Thanks for your inquiry.
CSB-E13462h
This kit is designed according to: https://www.uniprot.org/uniprot/P07900.
It is specific to detect heat shock protein 90α (HSP-90α). The specificity of the raw materials for this kit have been screened and validated strictly. So we can guarantee the specificity of the kit.
Here is the link for the reference of this kit.
http://journals.sagepub.com/doi/abs/10.1177/1073274818804489?cookieSet=1
Pls let me know if you have any further questions. Thank you.

Secreted Heat Shock Protein 90α Attenuated the Effect of Anticancer Drugs in Small-Cell Lung Cancer Cells Through AKT/GSK3β/β-Catenin Signaling Du Y.et al,/,2018
Identification of a Novel Serum Biomarker for Tuberculosis Infection in Chinese HIV Patients by iTRAQ-Based Quantitative Proteomics Chen C,/,2023
Design, synthesis and biological evaluation of new isoxazole derivatives as Hsp90 inhibitors M Abbasi,/,2024
Design, synthesis and biological studies of new isoxazole compounds as potent Hsp90 inhibitors F Keshavarzipour, M Abbasi, Z Khorsandi,/,2024

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.

Function(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(PubMed:25973397). 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

RPAP3 provides a flexible scaffold for coupling HSP90 to the human R2TP co-chaperone complex. PMID:29662061
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
While activation in c-Src is strictly controlled by ATP-binding and phosphorylation, the authors find that activating conformational transitions are spontaneously sampled in Hsp90-dependent Src mutants. PMID:28290541
chemotherapy agents can induce HSP90AA1 expression in osteosarcoma cells. And HSP90AA1, acting as an important regulator of autophagy, is a critical factor in the development of osteosarcoma chemoresistance both in vitro and in vivo. HSP90AA1 provides a novel therapeutic target for improving osteosarcoma treatment. PMID:30153855
We confirm that miR-628-3p promotes apoptosis and inhibits migration in A549 cells by negatively regulating HSP90. Our results may reveal a novel strategy for lung cancer treatment PMID:29888262
Data recognize HSP90 as a novel binding partner of PKM2 in hepatocellular carcinoma (HCC) cells. HSP90 potentiates the glycolysis and proliferation, reduces the apoptosis and thus enhances the growth of HCC cells through PKM2 Thr-328 phosphorylation maintaining its stability. PMID:29262861
EGFR expression stratified most pronounced among HSP90low tumours, where the EGFRhigh phenotype was associated with longer survival PMID:28765916
the SGT1-HSP90 complex contributes to the E3 ligase activity of the CUL4A complex that is necessary for CENP-A ubiquitylation and CENP-A deposition at the centromere. PMID:28816574
our data suggested that Hsp90alpha could positively regulate the self-renewal of BCSCs by facilitating the nuclear translocation of c-Myc and EZH2 to maintain BMI1 expression. PMID:28914785
HSP90 contributes to cutaneous vasodilation via NOS-dependent mechanisms in young habitually active men during exercise in the heat. PMID:28751373
The association between the MEEVD C-terminal peptide from the heat shock protein 90 (Hsp90) and tetratricopeptide repeat A (TPR2A) domain of the heat shock organizing protein (Hop) is a useful prototype to study the fundamental molecular details about the Hop-Hsp90 interaction. Observed are conformational changes of the peptide and the protein receptor induced by binding. The binding free energy is 8.4 kcal/mol. PMID:28723223
Our findings demonstrate Hsp90 blockade leads to ICN1 destabilization, providing an alternative strategy to antagonize oncogenic Notch1 signaling with Hsp90-selective inhibitors PMID:28143869
Generated multiple mutant KRAS-driven cancer cell lines with acquired resistance to the purine-scaffold HSP90 inhibitor PU-H71. Report a Y142N missense mutation in the ATP-binding domain of HSP90alpha that co-occurred with amplification of the HSP90AA1 locus in resistant cells. PMID:28032595
ATM is the primary kinase responsible for phosphorylation of Hsp90alpha after exposure ionizing radiation. PMID:27738310
molecular modeling was employed to incorporate experimental data using partial constructs of the Hsp90 C-terminal domain. PMID:27771574
findings suggested that this mechanism may be exploited by the Hsp90-Cdc37 chaperone to recruit and protect intrinsically dynamic kinase clients from degradation PMID:29267381
The findings establish an active role for Tsc1 as a facilitator of Hsp90-mediated folding of kinase and non-kinase clients-including Tsc2-thereby preventing their ubiquitination and proteasomal degradation. PMID:29127155
Data indicate HSP90 inhibitors as a class of preferred drugs for treatment combination with immunotherapy. PMID:28878208
Data suggest that SOCS3 is an important signaling protein in CLL, and Hsp90 inhibitors represent an approach to target transcriptional repression in B cell lymphoproliferative disorders. PMID:27107422
FKBP51 is primarily localized in mitochondria and hTERT is totally nuclear, upon the onset of oxidative stress, FKBP51 (but not FKBP52) becomes mostly nuclear colocalizing with hTERT, and longer exposure times to peroxide favors hTERT export to mitochondria. PMID:27233944
High HSP90 expression is associated with Colorectal Cancers. PMID:28870917
High HSP90 expression is associated with prostate cancer. PMID:28038472
Data suggest HSP90AA1-dependent regulation of ATM-NBN-CHK2 and ATR-CHK1 axes influences cells capability to repair double-stranded DNA damage; mechanisms include phosphorylation, polyubiquitination, and proteasomal degradation/proteolysis. (HSP90AA1 = heat shock protein 90kDa alpha; ATM = ataxia telangiectasia mutated protein; NBN = nibrin; CHK = checkpoint kinase; ATR = ataxia telangiectasia and Rad3 related kinase) PMID:28631426
Data show that pyruvate kinase M2 (PKM2) directly interacted with mutant growth factor receptor (EGFR) and heat-shock protein 90 (HSP90), and thus stabilized EGFR by maintaining its binding with HSP90 and co-chaperones. PMID:26500058
Binding of FM807 to the N-terminus of Hsp90 disrupted Hsp90/client complexes, resulting in degradation of the Hsp90 client protein EGFR and inhibition of the downstream pathway. PMID:28157708
Conventional as well as scaled molecular dynamics simulations further demonstrate that citrullination of selected Arg residues leads to progressive disruption of HSP90 tertiary structure, promoting exposure of R502/R510 to PAD modification and subsequent autoantibody binding. PMID:27448590
SYK is an HSP90 client protein, and B-cell receptor signaling-dependent phosphorylation of HSP90 on Y197 is required for this interaction. HSP90 promotes Burkitt lymphoma cell survival by maintaining tonic B-cell receptor signaling. PMID:28064214
Data indicate a chaperone function of nicotinamide mononucleotide adenylyl transferase 2 (NMNAT2), independent from its enzymatic activity, and NMNAT2 complexes with heat shock protein 90 (HSP90) to refold aggregated protein substrates. PMID:27254664
In the bound state, the Hsp90 dimer predominantly populates an open conformation, and transthyretin retains its globular structure. PMID:28218749
CD30 facilitates phosphorylation of heat shock factor 1, activates heat shock promoter element, and induces heat shock protein (HSP) 90. PMID:27870927
However, once the mumps virus L protein formed a mature polymerase complex with the P protein, Hsp90 activity was no longer required for the stability and activity of the L protein. PMID:28053100
HSP90 may be essential for stabilization and function of P2X7Rs through an action on the cysteine-rich domain of the cytoplasmic the C-terminus. PMID:27301716
HSP90AA1 and AB1 genes exhibit low expression in breast cancers highly sensitive to chemotherapy and may indicate the patients with higher probability of pathological complete response. PMID:28051275
the effect of HSP90 inhibition on IL-17-mediated cytokine and antimicrobial peptide expression in keratinocytes following heat treatment, was examined. PMID:27279135
epididymis secretory protein 4 had better specificity than CA125 in discriminating ovarian cancer, and endometrial cancer from benign gynecological diseases in southern China population PMID:27302312
Hsp90 has roles in the regulation of autophagy, such as toll-like receptor (TLR)-mediated autophagy, Ulk1-mediated mitophagy, and chaperone-mediated autophagy (CMA) [review] PMID:26432328
this study identified HSP90AA1 as a new potential biomarker for Behcet's disease by comparing highly ranked genes from all the built network-derived gene lists, which was confirmed the with real-world clinical samples PMID:27226232
Data show that heat shock protein 90 (HSP90) inhibitor 17-DMAG caused loss of ret proto-oncogene protein (RET) and proto-oncogene protein erbB-3 (ERBB3) phosphorylation and lead to rapid cell death. PMID:26595521
Hsp103 associates with cochaperone proteins, such as Hop, Cdc37 and Aha1, similar to Hsp90. The extra domain reduces the ATP hydrolysis when compared to Hsp90 thereby acting as a negative regulator of the chaperones intrinsic ATPase activity. PMID:23951259
Data suggest that synergistic mechanism between heat shock protein 90 (Hsp90) inhibitor SNX-7081 and fludarabine nucleoside (2-FaraA) may provide an alternative treatment for chronic lymphocytic leukemia (CLL) patients with p53 protein mutations. PMID:26556860
The expression of HSP90A was increased in the HCC cells, serum, and tissues. Immunohistochemistry analysis on 76 clinical tissue samples also suggested the relevance between HSP90A expression and HCC metastatic behavior. PMID:26704341
Aarsd1 inhibits the activity of a paradigmatic Hsp90 client protein. PMID:26884463
study confirmed Hsp90 as an influenza virus A PB2 polymerase interacting protein, and established that Hsp90 interacts with both the E627 and 627K variants, but has established this interaction is species independent, and both mammalian and avian Hsp90 can bind to the PB2 protein PMID:26616658
Data show that high-affinity heat shock protein 90 (HSP90) binding conferred by the inhibitor backbone could be exploited for conjugate accumulation within tumor cells. PMID:26271675
In conjunction with HSP90, the cytoplasmic USP19 may play a key role in triage decision for the disease-related polyQ-expanded substrates, suggesting a function of USP19 in quality control of misfolded proteins by regulating their protein levels PMID:26808260
The region of aa 250-295 of BGLF4 is essential for the BGLF4/Hsp90 interaction. PMID:26982469
The thermodynamics of binding of Cyp-40 to Hsp90 shows remarkable temperature sensitivity in the physiological temperature range. PMID:26330616
HSP90 overexpression is a prognostic marker for cholangiocarcinoma. HSP90-targeted therapy may be an option for a subset of cholangiocarcinoma. PMID:26141945
From our screening methodology, we identified HCAb2 as a breast tumor specific heavy chain antibody targeting cell surface heat shock protein 90. PMID:26334999
Heat shock protein 90 is required for ex vivo neutrophil-driven autoantibody-induced tissue damage in experimental epidermolysis bullosa acquisita. PMID:25739426