S100A8 (Human) ELISA Kit (DEIA4161)

Regulatory status: For research use only, not for use in diagnostic procedures.

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biological medium, plasma, serum
Species Reactivity
Intended Use
This kit is used for the quantitative measurement of human S100A8/MRP8 in serum, plasma and other biological media.
Contents of Kit
1. Microplate
2. 10X Wash Buffer
3. Dilution Buffer
4. Human S100A8/MRP8 Standard
5. HRP conjugated Detection Antibody
6. Substrate Reagent
7. Stop Solution
All of the reagents included in the S100A7 (Human) ELISA Kit have been tested for stability. Reagents should not be used beyond the stated expiration date. Upon receipt, kit reagents should be stored at 4°C, except the reconstituted human S100A7 Standard must be stored at below -70°C. Coated assay plates should be stored in the original foil bag sealed by the zip lock and containing a desiccant pack. For more detailed information, please download the following document on our website.
Detection Limit
Twenty-one assays were evaluated and the minimum detectable dose (MDD) of human S100A8/MRP8. The MDD (defined as such a concentration of human S100A8/MRP8 giving absorbance higher than mean absorbance of blank plus three standard deviations of the absorbance of blank: A blank + 3SD blank) is better than 43.4 pg/mL of sample.


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Quantitative proteomic analysis of urinary exosomes in kidney stone patients


Authors: Wang, Qing; Sun, Yi; Yang, Yuanyuan; Li, Cong; Zhang, Jiaqiao; Wang, Shaogang

Background: Increased urinary exosomes are associated with kidney stones but how they work is unknown. In this study, we aim to identify dysregulated proteins in urinary exosomes from kidney stone patients and to explore the potential role of exosomal proteins in nephrolithiasis. Methods: First morning voids were collected from participants. Urinary exosomes were isolated via ultracentrifugation. Label free liquid chromatography-tandem mass spectrometry was performed to analyze the proteome of urine exosomes from three kidney stone patients and three age-/sex-matched healthy controls. Bioinformatics analysis was conducted to identify dysregulated proteins associated with stone formation. Results of proteomic analysis were verified by Western blotting in other three kidney stone patients and three healthy controls. Results: Nine hundred and sixty proteins were identified with proteomic analysis, of which 831 were identified in the control group and 879 in the stone group. Sixteen proteins in urinary exosomes were found most significantly different between kidney stone patients and healthy controls. Gene ontology (GO) analysis showed that dysregulated proteins were enriched in innate immune response, defense response to bacterium and calcium-binding. S100A8, S100A9 and S100A12 were common in above three GO terms and were chosen for further study. Western blotting confirmed that the expression of these three S100 proteins was higher in urinary exosomes from kidney stone patients. In addition, S100 proteins were aggregated in urinary exosomes and it was difficult to detect them in urine. Conclusions: Urinary exosomes from kidney stone patients are rich in S100 proteins and play a role in innate immune response, defense response to bacterium and calcium-binding.

Calcium Regulates S100A12 Zinc Sequestration by Limiting Structural Variations


Authors: Wang, Qian; Aleshintsev, Aleksey; Jose, Aneesha N.; Aramini, James M.; Gupta, Rupal

Antimicrobial proteins such as S100A12 and S100A8/A9 are highly expressed and secreted by neutrophils during infection and participate in human immune response by sequestering transition metals. At neutral pH, S100A12 sequesters Zn2+ with nanomolar affinity, which is further enhanced upon calcium binding. We investigated the pH dependence of human S100A12 zinc sequestration by using Co2+ as a surrogate. Apo-S100A12 exhibits strong Co2+ binding between pH 7.0 and 10.0 that progressively diminishes as the pH is decreased to 5.3. Ca2+-S100A12 can retain nanomolar Co2+ binding up to pH 5.7. NMR spectroscopic measurements revealed that calcium binding does not alter the side-chain protonation of the Co2+/Zn2+ binding histidine residues. Instead, the calcium-mediated modulation is achieved by restraining pH-dependent conformational changes to EF loop 1, which contains Co2+/Zn2+ binding Asp25. This calcium-induced enhancement of Co2+/Zn2+ binding might assist in the promotion of antimicrobial activities in humans by S100 proteins during neutrophil activation under subneutral pH conditions.

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