Agilent Technologies

About: Agilent Technologies is a company organization based out in Santa Clara, California, United States. It is known for research contribution in the topics: Signal & Mass spectrometry. The organization has 7398 authors who have published 11518 publications receiving 262410 citations. The organization is also known as: Agilent Technologies, Inc..

Theoretical and practical aspects of fast gas chromatography and method translation

Abstract: Interest in the development and implementation of fast gas chromatography (GC) methods continues to increase. Fast GC method development and validation can be simplified and more successful if a few key theoretical and practical concepts are kept in mind. Key concepts such as speed-optimized flow rate, optimal temperature-program rate, sample capacity, “cut the column”, and principles of method translation are discussed.

The Effect of Perimeter Geometry on FBAR Resonator Electrical Performance

Abstract: We describe the first four Lamb-Rayleigh modes seen in an FBAR resonator. We also describe the effect of apodization (non parallel edges) have on the kx-ky space as compared to square resonators.

Two-stage Off-Gel isoelectric focusing: protein followed by peptide fractionation and application to proteome analysis of human plasma.

Abstract: This paper presents the recently introduced Off-Gel™ electrophoresis (OGE) technology as a versatile tool to reproducibly fractionate intact proteins and peptides into discrete liquid fractions. The coupling of two stages of OGE, i.e., the separation of intact proteins in a first-stage followed by fractionation of peptides derived from each protein fraction after proteolysis in a second stage, results in an array of 15×15 fractions that are directly amenable to additional peptide fractionation like reverse-phase liquid chromatography (RPC). The analysis of all second-stage peptide fractions from only the first-stage protein fraction representing pH 5.0 –5.15 by on-line reverse-phase LC-tandem mass spectrometry resulted in the identification of 53 proteins (337 peptides), of which 10 were on different immunoglobulin (Ig) chains, with an input of only 1.5 mg human blood plasma proteins. Increasing the protein load to approximately 12 mg increased the number of identified proteins in the same protein fraction to 73 proteins (449 peptides), of which 15 were Ig-related. Immunodepletion of six of the most abundant proteins (albumin, transferrin, haptoglobin, IgG, IgA, and α-1-antitrypsin) prior to first-stage OGE with an input of 1.5 mg of protein (equivalent to approximately 10 mg nondepleted plasma) resulted in the identification of 81 proteins (660 peptides), of which three were still Ig fragments. The pI-based separation of peptides appears to be nonuniform based on the theoretically determined pI values of identified peptides. This observation specifically accounts for the neutral zone (pI 5–8) and can be accounted for by the physicochemical properties of the peptides given by their amino acid composition. The power of OGE separation of proteins and peptides is discussed with a focus on the use of the knowledge about the pI of proteins and peptides that assist the validation of correct identifications together with the retention time of peptides on RPC.

Identifying services provided via IP and similar packet networks, and service usage records for such services

Abstract: A service key is assembled from information in data packets traversing a communications link, to enable identification of services implemented via the data packets.