Enhanced immuno-detection of shed extracellular domain of HER-2/neu

Chourb, Sinang; Mackness, Brian C.; Farris, Leslie R.; McDonald, Malcolm

doi:10.4236/health.2009.14053

Cited by 6 publications

(6 citation statements)

References 25 publications

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“…The %CV was calculated as described in Table 1; value and SD of blank were consistent with previously published reports [21][22][23][24].…”

Section: Structure Of Extracellular Domain Of Muc1: Potential For Vacsupporting

confidence: 68%

“…Poly (methyl methacrylate) (PMMA) (Sigma) was used to coat polypropylene plates (Corning). The ALYGNSA assay protocol followed previously reported methods [25]. Briefly, the PMMA plates were coated with recombinant Protein G' (1 g/mL at 50 L/well) and incubated overnight at 4˚C.…”

Section: Ca 15-3 Alygnsa Assaymentioning

confidence: 99%

“…The plates were then incubated for 2 hours at room temperature, and then washed. The fluorescently labeled CA 15-3 detector antibody prepared by the DyLight 488 Microscale Antibody Labeling Kit as recently described [25] was diluted to 5 g/mL, and applied at 50 L/well. Following incubation for 1 hour at room temperature and a repeat washing, the plates were read for fluorescence at 485/523 nm on a BioTek Microplate Reader.…”

Section: Ca 15-3 Alygnsa Assaymentioning

confidence: 99%

“…In this present study, an assay was developed for the detection of the breast cancer biomarker CA 15-3 utilizing the ALYGNSA system consisting of a protein biolinker (Protein G') adsorbed onto Poly (methyl methacrylate) (PMMA). The unique interaction of Protein G' with PMMA, a thermoplastic polymer, has been demonstrated to improve human IgG capture antibody align-ment/orientation [20] and deliver greater sensitivity in the detection of several cancer biomarkers [21][22][23][24], including an additional breast cancer biomarker HER-2/ neu [21] and an additional mucin MUC16 (CA 125) [22]. Herein, this same ALYGNSA assay system will be employed to measure CA 15-3 and compare the findings to a commercial control ELISA kit.…”

Section: Introductionmentioning

confidence: 99%

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Improved detection Of the MUC1 cancer antigen CA 15-3 by ALYGNSA fluorimmunoassay

Chourb¹,

Mackness²,

Farris³

et al. 2011

Health

Self Cite

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Breast cancer is the second leading cause of cancerrelated deaths in women worldwide; a prime cancer biomarker to aid in the diagnosis, directed treatment, clinical management, and reoccurrence of this cancer is a MUC1 peptide fragment: cancer antigen 15-3 (CA 15-3). Herein, an immuno-fluorescence assay for CA 15-3 was developed; this ALYGNSA system consists of a protein biolinker (Protein G’) adsorbed onto Poly (methyl methacrylate) (PMMA). The unique interaction of Protein G’ with PMMA, a thermo-plastic polymer has been demonstrated to improve human IgG capture antibody alignment/ orientation and result in greater assay sensitivity. Indeed a previous report (HEALTH 1 325 - 329, 2009) on the shed extracellular domain of HER-2/neu revealed a 10-fold increase in sensitivity of the ALYGSNA assay over a control ELISA assay. Results from this ALYGNSA assay study revealed that a 16-fold increase in detection (≤0.94 U/mL) of CA 15-3 was found in comparison to a commercial control ELISA kit (≤15 U/mL). In conclusion, this enhanced sensitivity of the ALYGNSA assay for CA 15-3, may provide insights into the role/function of this biomarker in normal, as well as, breast cancer and other epithelial cancers

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“…The %CV was calculated as described in Table 1; value and SD of blank were consistent with previously published reports [21][22][23][24].…”

Section: Structure Of Extracellular Domain Of Muc1: Potential For Vacsupporting

confidence: 68%

Section: Ca 15-3 Alygnsa Assaymentioning

confidence: 99%

Section: Ca 15-3 Alygnsa Assaymentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

See 2 more Smart Citations

Improved detection Of the MUC1 cancer antigen CA 15-3 by ALYGNSA fluorimmunoassay

Chourb¹,

Mackness²,

Farris³

et al. 2011

Health

Self Cite

View full text Add to dashboard Cite

show abstract

“…It is urgently needed to develop a high sensitivity and label-free method for early rapid diagnosis of breast cancer. A number of biomarker-based methods have been studied for breast cancer detection [ 18 , 19 , 20 , 21 ], including radioimmunoassay, immunohistochemistry, enzyme-linked immunosorbent assay, and fluoroimmunoassay. However, the biomarker-based methods have some disadvantages include expensive, time-consuming, require complex labeling process and trained people, and often limited in detection sensitivity [ 22 ].…”

Section: Introductionmentioning

confidence: 99%

Microwave Sensors for Breast Cancer Detection

Wang

2018

Sensors

120

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Breast cancer is the leading cause of death among females, early diagnostic methods with suitable treatments improve the 5-year survival rates significantly. Microwave breast imaging has been reported as the most potential to become the alternative or additional tool to the current gold standard X-ray mammography for detecting breast cancer. The microwave breast image quality is affected by the microwave sensor, sensor array, the number of sensors in the array and the size of the sensor. In fact, microwave sensor array and sensor play an important role in the microwave breast imaging system. Numerous microwave biosensors have been developed for biomedical applications, with particular focus on breast tumor detection. Compared to the conventional medical imaging and biosensor techniques, these microwave sensors not only enable better cancer detection and improve the image resolution, but also provide attractive features such as label-free detection. This paper aims to provide an overview of recent important achievements in microwave sensors for biomedical imaging applications, with particular focus on breast cancer detection. The electric properties of biological tissues at microwave spectrum, microwave imaging approaches, microwave biosensors, current challenges and future works are also discussed in the manuscript.

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Serum-based ALYGNSA immunoassay for the prostate cancer biomarker, total prostate-specific antigen (tPSA)

Mackness

McDonald

2010

Anal Bioanal Chem

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Prostate-specific antigen (PSA) is a serum glycoprotein overproduced by the prostate in prostate cancer (> or = 4 ng/mL in the bloodstream). An immunoassay for total PSA (tPSA) was developed using the ALYGNSA method to enhance capture antibody orientation and a limit of detection of 0.63 ng/mL was reported, a limit 15-fold lower than a commercial tPSA ELISA assay. This ALYGNSA assay, however, was performed using only buffer-based proteins and blocking agents (Mackness et al., Anal Bioanal Chem 396:681-686, 2010). To improve the clinical application of this system, a serum-based tPSA ALYGNSA was developed employing human serum. This assay also resulted in a limit of detection of 0.63 ng/mL of tPSA protein. The findings reported here provide support for the clinical application of this assay for diagnosis, progression, treatment, and possible recurrence of prostate cancer.

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Enhanced immuno-detection of shed extracellular domain of HER-2/neu

Cited by 6 publications

References 25 publications

Improved detection Of the MUC1 cancer antigen CA 15-3 by ALYGNSA fluorimmunoassay

Improved detection Of the MUC1 cancer antigen CA 15-3 by ALYGNSA fluorimmunoassay

Microwave Sensors for Breast Cancer Detection

Serum-based ALYGNSA immunoassay for the prostate cancer biomarker, total prostate-specific antigen (tPSA)

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