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A Universal Method For Quantifying Proteins, Small Molecules, Lipids, And Electrolytes

UCLA scientists in the Departments of Psychiatry & Biobehavioral Sciences and Human Genetics have developed a novel method for the simultaneous quantification of proteins, small molecules, lipids, and electrolytes.

Phenotypic Profiling Of Hepatocellular Carcinoma Circulating Tumor Cells For Treatment Selection

Researchers in the UCLA Departments of Surgery and Molecular and Medical Pharmacology have developed a novel blood-based assay that can capture and characterize circulating tumor cells indicative of both early- and late-staged hepatocellular carcinoma (HCC).

Lipid Bilayer Formation Using Sessile Droplets

UCLA researchers in the Department of Bioengineering have developed a method to form a biologically functional lipid bilayer in a high-throughput and automated fashion.

Surfaceome Profiling Of Advanced Prostate Cancer To Identify Target Antigens For Immune-Based Therapy

Dr. Witte and colleagues at UCLA have developed a novel approach to identify surface biomarkers and targetable antigens in prostate cancer by combining multiple omics analyses across different cell lines.

Development Of A Method For Endocrine Network Discovery Uncovers Peptide Therapeutic Targets

UCLA researchers in the Division of Cardiology at the Geffen School of Medicine have developed a bioinformatics methodology to identify and functionally annotate novel endocrine pathways.

Tissue Projection Electrophoretic Separation Of Protein

A range of related immunoblotting methods have enabled the identification and semi-quantitative characterization of e.g., DNA (Southern blot), RNA (northern blot), proteins (Western blot), and protein-protein interactions (far-western blot); by coupling biomolecule separations and assays.  However, there are a wide number of alternative splicing events, post-translational modifications, and co-translational modifications (e.g., phosphorylation, glycosylation, and protein cleavage) that give rise to proteoforms and protein complexes with distinct function and subsequent cell behavior that cannot be analyzed with conventional methods such as immunohistochemistry (IHC). Analytical variability (lack of isoform- or complex-specific antibody probes), biological variability (small cell subpopulations diluted in bulk analysis), and lack of multiplexing (measurement of multiple proteins from the same tissues) can all render proteoforms and protein complexes undetectable by current technologies.     UC Berkeley researchers have created electrophoretic separation platform that is capable of measuring proteoforms and protein complexes lacking specific antibodies alongside spatial information, at the cellular level.  This platform maintains the architecture of 2D tissue slices while projecting a protein separation in the 3rd dimension. The platform mitigates artifacts induced by tissue dissociation processes, as the intact tissue is lysed and subject to a protein separation. The platform is also compatible with differential detergent fractionation methods for further separation of proteins (e.g. separation by localization within the cell, by cell type, by protein complex formation, or by cellular vs. matrix proteins), opening the door for a novel, refined classification taxonomy using enhanced biomarker signatures for diagnostics and treatment selection in oncology among a wide range of additional future applications.  

Protein-Coated Microparticles For Protein Standardization In Single-Cell Assays

Single-cell analysis offers powerful capabilities of identification of rare sub-populations of cells, understanding heterogeneity of cancerous tumors, and tracking cell differentiation and reprogramming. Despite great potentials for uncovering new biological systems and targeting diseases with precision medicine, single-cell approaches are composed of complex device processes that can cause bias in measurement.  In deep sequencing, technical variation in single cell expression data occurs during capture and pre-amplification steps. Similarly, in single-cell protein assays, technical variability can obscure functionally relevant variance.    To better control protein measurement quality in single-cell assays, researchers at the University of California, Berkeley developed a novel method to loading and release protein standard. This method utilizes the surface of modified and functionalized microparticles as vehicles to capture target proteins with desired concentrations. Chelation-assisted click chemistry is applied to demonstrate that protein standards with different molecular masses can be loaded and bounded in a single-cell protein assay. Microparticles are introduced into single-cell devices by either passive gravity, magnetic attraction, or other physicochemical forces. These protein standards from microparticles provide a reference to measure protein mass sizes from individual cells and a quality control for any biases in device fabrication, cell lysis, protein solubility, protein capture, and protein readouts (i.e. antibody probing).   

Living Bioreactor for Stoichiometric Protein Production

Living bioreactors are powerful systems for producing a variety of valuable compounds. The versatility of such bioreactors is one of the more useful aspects of the system. Large quantities of compounds or cellular components can be produced efficiently, with minimal cost. Alternately, these systems can be used to produce pathway components that are necessary in the production of secondary products. A common problem with such systems is that they are limited by non-uniform production of pathway components, or require an isolation process to ensure the components are in the appropriate quantity and sequence in the process. Inventors at Texas A&M and UC San Francisco have developed a novel technique to address these issues. The technology effectively results in a stoichiometric production of protein components that are produced in an array, ready for secondary production.

Rapid Screening and Identification of Antigenic Components in Tissues and Organs

Researchers at the University of California, Davis have developed an approach to rapidly screen and identify antigenic components in tissues and organs.

Versatile Labeling of Protein N-Termini for Site-specific Bioconjugation

Improved subtiligase variants allow broad and versatile site-specific chemical modification or conjugation of proteins on their N-termini.

Aptamer functionalized shrink-induced high surface area electrochemical sensors

A low-cost method of manufacturing a, rough high surface area electrodes with a dissolvable polymer coating to improve surface wettability and electrochemical sensing.

Assay for Inhibitors of Nonsense-Mediated RNA Decay

Prof. Sika Zheng at UCR has developed a new endogenous NMD assay that is both sensitive and quantitative. The assay can be used on its own to assess changes in cellular NMD activity with high specificity and sensitivity. It can facilitate analysis of NMD controls by cellular pathways in response to stimuli or during development and is particularly suitable for unbiased screening of NMD modulators. The assay is designed to distinguish NMD regulation from transcriptional regulation and alternative splicing control.

Process For Sorting Dispersed Colloidal Structures

Researchers from the Chemistry and Biochemistry department at UCLA have developed method of separating and/or sorting specific target structures from other non-target structures in a complex mixture using custom-made target-specific colloidal particles.

Drop-Carrier Particles For Digital Assays

UCLA researchers in the Department of Bioengineering have developed a novel drop-carrier particle for single cell or single molecule assays.

Low Cost Wireless Spirometer Using Acoustic Modulation

The present invention relates to portable Spirometry system that uses sound to transmit pulmonary airflow information to a receiver.

Metal-free affinity media/agents for the selective capture of histidine-rich peptide sequences

The present invention utilizes metal-free synthetic polymer-based materials for the purification of peptides and proteins containing or being fused with histidine-rich sequences, which does not damage the function of the target protein and is less costly.

Improved Cell-Free Protein Synthesis For Protein Microarray

Researchers at UC Irvine have developed a cell-free (CF) protein synthesis system to solubilize and synthesize highly hydrophobic membrane proteins that would typically aggregate using current CF synthesis systems. With such high amounts of synthesized proteins, researchers intend to build protein microarrays for diagnostic purposes.

Enhanced Cell/Bead Encapsulation Via Acoustic Focusing

The invention consists of a multi-channel, droplet-generating microfluidic device with a strategically placed feature. The feature vibrates in order to counteract particle-trapping micro-vortices formed in the device. Counteracting these vortices allows for single particle encapsulation in the droplets formed by the device and makes this technology a good candidate for use in single cell diagnostics and drug delivery systems.

A Protein Domain That Protects Ubiquitinated Forms Of Proteins From Degradation In Cis And In Trans

Ubiquitylation affects proteins in many ways, such as activation or inactivation, and signaling for their degradation. It is not fully understood how ubiquitin effects all proteins or how researchers may use it to control cellular processes. This invention describes novel fusion proteins that protect ubiquitylated forms of the target proteins from degradation.

Functionally Selective Ligands for Study and Inhibition of Inflammation

Background: Due to the complexity of the complement system cascade, biological roles of many signaling receptors are unknown. Additionally, biased ligand binding to cell-bound receptors may lead to selective intracellular effector binding and ligand-specific pathway activation and function. Mechanistic knowledge forms the basis for assay development to explore pharmacology against complement-mediated inflammatory diseases.   Brief Description: A multidisciplinary team of researchers from UCR, Texas A&M, Sheffield, and Queensland have discovered the first functionally selective peptide ligands for a complement system receptor that is involved in inflammation. The peptides are functionally selective ligands of C5aR2 but not C5aR1 or C3aR, and they have been characterized in vitro and in vivo. These peptides are novel tools that can modulate the activity of the receptor in vitro and in vivo, and interrogate the function of the receptor and its implication in inflammatory diseases.

Pyrite Shrink-Wrap Laminate As A Hydroxyl Radical Generator

The invention is a diagnostic technology, as well as a research and development tool. It is a simple, easy to operate, and effective platform for the analysis of pharmaceuticals and biological species. Specifically, this platform generates hydroxyl radicals for oxidative footprinting – a technique commonly employed in protein mapping and analysis. The platform itself is inexpenisve to fabricate, scalable, and requires nothing more than an ordinary pipet to use. In addition, it is highly amenable to scale-up, multiplexing, and automation, and so it holds promise as a high-throughput method for mapping protein structure in support of product development, validation, and regulatory approval in the protein-based therapeutics industry.

Monoclonal Antibody Against PNPase (Clone 4C11)

Mouse monoclonal antibody against the human mitochondrial polyribonucleotide nucleotidyltransferase 1 (PNPase). This antibody has been tested for use in immunocytochemistry/immunofluorescence, immunoprecipitation, and western blot.

Monoclonal Antibody against ATR-IP (Clone 11)

Mouse monoclonal antibody against the human ATR-interacting protein (ATR-IP). This antibody has been tested for use in immunocytochemistry/immunofluorescence, immunoprecipitation, and western blot.

Monoclonal Antibody Against CEP164 (Clone 13)

Mouse monoclonal antibody against the human centrosomal protein 164kDa (Cep164). This antibody binds to the phosphorylation site of Cep164 and has been tested for use in immunocytochemistry/immunofluorescence, immunoprecipitation, and western blot.

Monoclonal Antibody Against CEP164 (Clone 17)

Mouse monoclonal antibody against the human centrosomal protein 164kDa (Cep164). This antibody binds to the phosphorylation site of Cep164 and has been tested for use in immunoprecipitation and western blot.

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