How To Generate And Download Pdf In Pega

To generate a Pega Web Mashup code, create a Mashup channel by using the Channels and Interfaces landing page in either App Studio or Dev Studio, customize the code as necessary, embed that code to a web page, and configure a list of approved sites for the site origin.

When deploying a mashup, copy the generated code to the appropriate location on your web page. At run time, your web page displays Pega Platform content within the IFRAME or DIV element. The default action runs immediately unless the attribute for the action is deferred.

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You may need to control the display size of your mashup to fit inside a defined area. To control the size of a mashup using the DIV tag, set the data-pega-resizetype attribute to customize the mashup width. By using the mashup attribute data-pega-resizetype, the mashup can fit inside a fixed space (data-pega-resizetype = 'fixed') or it can expand to fill the available space on the page (data-pega-resizetype = 'stretch'). By default, the value of the attribute is stretch.

To save time and increase the automation of your business processes, you can now generate case documents by adding a Generate document step to your case types. For example, in a job application review case, you can automatically generate a document that includes information that is provided by a candidate, such as personal details, working experience, and the review process result.

To further demonstrate its commitment to AI, Pegasystems in March launched the AI-Powered Sales Coach within Pega Sales Automation. The software analyzes more than 50 actions sales reps take each day and then proactively alerts managers to underperforming sellers and generates real-time coaching tips.

N2 - Immobilization of proteins onto solid supports is important in the preparation of functional protein microarrays and in the development of bead-based bioassays, biosensors, and industrial biocatalysts. In order to generate the stable, functional, and homogeneous materials required for these applications, attention has focused on methods that enable the efficient and site-specific covalent immobilization of recombinant proteins onto a wide range of platforms. To this end, the phosphopantetheinyl transferase Sfp was employed to catalyze the direct immobilization of recombinant proteins bearing the small, genetically encoded ybbR tag onto surfaces functionalized with CoA. Using mass spectrometry, it was shown that the Sfp catalyzes immobilization of a model acyl carrier protein (ACP) onto CoA-derivatized PEGA resin beads through specific covalent bond formation. Luciferase (Luc) and glutathione-S-transferase (GST) ybbR-fusion proteins were similarly immobilized onto PEGA resin retaining high levels of enzyme activity. This strategy was also successfully applied for the immobilization of the ACP, as well as ybbR-Luc, -GST, and -thioredoxin fusion proteins, on hydrogel microarray slides. Overall, the Sfp-catalyzed surface ligation is mild, quantitative, and rapid, occurring in a single step without prior chemical modification of the target protein. Immobilization of the target proteins directly from a cell lysate mixture was also demonstrated. 2008 American Chemical Society.

AB - Immobilization of proteins onto solid supports is important in the preparation of functional protein microarrays and in the development of bead-based bioassays, biosensors, and industrial biocatalysts. In order to generate the stable, functional, and homogeneous materials required for these applications, attention has focused on methods that enable the efficient and site-specific covalent immobilization of recombinant proteins onto a wide range of platforms. To this end, the phosphopantetheinyl transferase Sfp was employed to catalyze the direct immobilization of recombinant proteins bearing the small, genetically encoded ybbR tag onto surfaces functionalized with CoA. Using mass spectrometry, it was shown that the Sfp catalyzes immobilization of a model acyl carrier protein (ACP) onto CoA-derivatized PEGA resin beads through specific covalent bond formation. Luciferase (Luc) and glutathione-S-transferase (GST) ybbR-fusion proteins were similarly immobilized onto PEGA resin retaining high levels of enzyme activity. This strategy was also successfully applied for the immobilization of the ACP, as well as ybbR-Luc, -GST, and -thioredoxin fusion proteins, on hydrogel microarray slides. Overall, the Sfp-catalyzed surface ligation is mild, quantitative, and rapid, occurring in a single step without prior chemical modification of the target protein. Immobilization of the target proteins directly from a cell lysate mixture was also demonstrated. 2008 American Chemical Society.

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