We demonstrate an all-optical label and payload separator based on nonlinear polarization rotation in a semiconductor optical amplifier (SOA). The proposed scheme uses a packet format composed of a label and payload information signal combined with a control signal by using polarization division multiplexing. The control signal is employed to separate the label from the payload signal by exploiting nonlinear polarization rotation in a SOA. Experimental results show a label from payload suppression factor of 22 dB. This scheme operates asynchronously and does not need external control signal. Clean and wide open eye diagrams are obtained for both the payload and the label signal operating at bit-rates of 10 Gbit/s and 625 Mbit/s, respectively.
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http://dx.doi.org/10.1364/opex.12.004214 | DOI Listing |
Sensors (Basel)
December 2024
State Key Laboratory of Networking and Switching Technology, Beijing University of Posts and Telecommunications, Beijing 100876, China.
IoT (Internet of Things) networks are vulnerable to network viruses and botnets, while facing serious network security issues. The prediction of payload states in IoT networks can detect network attacks and achieve early warning and rapid response to prevent potential threats. Due to the instability and packet loss of communications between victim network nodes, the constructed protocol state machines of existing state prediction schemes are inaccurate.
View Article and Find Full Text PDFAngew Chem Int Ed Engl
December 2024
Chemical Biology Laboratory, Center for Cancer Research, National Cancer Institute, Frederick, Maryland, 21702, USA.
Targeted payload delivery strategies, such as antibody-drug conjugates (ADCs), have emerged as important therapeutics. Although considerable efforts have been made in the areas of antibody engineering and labeling methodology, improving the overall physicochemical properties of the linker/payload combination remains an important challenge. Here we report an approach to create an intrinsically hydrophilic linker domain.
View Article and Find Full Text PDFCancer Res
December 2024
The University of Texas Health Science Center at Houston, Houston, TX, United States.
As colorectal cancer (CRC) remains a leading cause of cancer-related death, identifying therapeutic targets and approaches is essential to improve patient outcomes. The EGFR ligand epiregulin (EREG) is highly expressed in RAS wildtype and mutant CRC with minimal expression in normal tissues, making it an attractive target for antibody-drug conjugate (ADC) development. In this study, we produced and purified an EREG monoclonal antibody (mAb), H231, that had high specificity and affinity for human and mouse EREG.
View Article and Find Full Text PDFJ Control Release
December 2024
Aiiso Yufeng Li Family Department of Chemical and Nano Engineering, Shu and K.C. Chien and Peter Farrell Collaboratory, University of California San Diego, La Jolla, CA 92093, USA. Electronic address:
The effective delivery of chemotherapeutic drugs to tumor sites is critical for cancer treatment and remains a significant challenge. The advent of nanomedicine has provided additional avenues for altering the in vivo distribution of drug payloads and increasing tumor localization. More recently, cell-derived nanoparticles, with their biocompatibility and unique biointerfacing properties, have demonstrated considerable utility for drug delivery applications.
View Article and Find Full Text PDFbioRxiv
November 2024
Center for Translational Cancer Research, The Brown Foundation Institute of Molecular Medicine, University of Texas Health Science Center at Houston, Houston, TX.
As colorectal cancer (CRC) remains a leading cause of cancer-related death, identifying therapeutic targets and approaches is essential to improve patient outcomes. The EGFR ligand epiregulin (EREG) is highly expressed in RAS wildtype and mutant CRC with minimal expression in normal tissues, making it an attractive target for antibody-drug conjugate (ADC) development. In this study, we produced and purified an EREG monoclonal antibody (mAb), H231, that had high specificity and affinity for human and mouse EREG.
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