enzyme substrate Based on these findings we have proposed

Based on these findings we have proposed a working model that Dsg3 competes with inactive Src for binding to the scaffolding domain of caveolin-1, and thus causes Src to release from binding to caveolin-1, that leading to its auto-activation (Fig. 5B). This working model opens up a new avenue for future research.
Experimental design, materials and methods
Acknowledgments This work was supported by an MRC funded studentship to Barts and London School of Medicine and Dentistry that was awarded to HW.
Data In order to identify the TF responsible for the activation of IRS-2 promoter activity downstream FSH, all TFBS in the IRS-2 promoter region [3] were explored using the Genomatix MatInspector software (Fig. 1) followed by a search for TFs that are reported to be transcriptional activators of FSH (Table 1, Supplementary material). The data also shows SP1 as a potential key TF downstream of FSH in human GCs as it has SP1 enzyme substrate with a very high similarity (Core similarity=1) (Table 2). The increased binding of SP1 to IRS-2 promoter by FSH in human GCs was validated by ChIP assay (Fig. 2). Here, we have identified putative TFBS in the IRS-2 promoter region and data thereof was subjected to IRS-2–protein interaction analysis to emphasize the importance of this data. Unweighted binary interactions were analyzed for TF regulatory genes in IRS-2 network using Cytoscape software tool and R-code (Supplementary material)Fig. 3.
Experimental design-materials and methods
Acknowledgments We are thankful to Avijit Podder and Dr. N. Lata for the analysis of IRS-2-protein interactions. This work was supported by research Grant (Ref. no. BT/PR5379/MED/14/631/2004; BT/PR8330/AAQ/01/313/2006) from the Department of Biotechnology (DBT), Government of India, New Delhi, India to RS.
Data, experimental design, materials and methods
Acknowledgments Funding was provided by: Academy of Finland (Contract no. 1252183). The authors of this article also thank A. Kankaanpää and H. Li (Aalto University) for technical assistance.
Specifications table
Description of the actual data
Experimental design
Calculation The rate constant of a first-order reaction (k) equation is used to determine catalase activity: t: time. S°: absorbance of standard tube. S: absorbance of test tube. M: absorbance of control test (correction factor).
Data The method is modified from that elucidated previously by Goth [1] and Korolyuk et al. [2] in which the consumption of hydrogen peroxide is measured spectrophotometrically by a complex reaction with ammonium molybdate at 405nm or 410nm. The present method has properties that distinguish them from other assays. The first characteristic includes measurement of absorbance at a wavelength equal to λmax (374nm) which produces results with high accuracy and precision. In an earlier study, Goth [1] measured the absorbance at 405nm. Goth attributed the reason for this choice to the accessibility of spectrophotometers and filter photometers. Possibly, that choice was good two decades ago. Presently, with the huge progress in spectrophotometric techniques, chemical analysts cannot agree with this explanation [3]. The choice of wavelengths other than 374nm (such as 405nm) produces significant disadvantages. It produces unreliable results because of the interference of measurements with each other. It is rare to find a spectroscopic method that uses a wavelength other than λmax for chemical analysis. The choice of λmax is necessary for various causes. This wavelength distinguishes each compound and gives a description of the electronic structure of the produced complex. It is also used to achieve the highest sensitivity and to decrease deviations from Beer׳s Law [4]. λmax will provide the largest possible accuracy of the measurements because a small change in concentration can provide a greater change in absorbance than other wavelengths. This means that the quantitative analyses are more accurate. Fig. 1 elucidates the difference in accuracy when the absorbance was measured in the λmax compared with when it is measured at other wavelengths. Fig. 1(A) represents the wavelength that is used in Goth method, which shows the inappropriate interference between closely spaced levels of the enzyme at wavelength 405nm, which causes the inability of the Goth method to differentiate between them. In the spectra of Fig. 1(B), we note that the space between curves 1 (20mM H2O2), curves 2 (10mM H2O2) and curves 3 (5mM H2O2) is at a maximum at 374nm, and at this wavelength the change in absorbance is highest for a given change in concentration. This means that the measurement of concentration as a function of the absorbance is most sensitive at λmax wavelength. For these reasons, analysts usually select the wavelength of maximum absorbance for a given solution and use it in the absorbance measurements.