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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.

Monoclonal Antibodies Against Chk2 (Clone 4B8)

Mouse monoclonal antibody (clone 4B8) against the human Serine/threonine-protein kinase Chk2. This antibody has been tested for use in immunoprecipitation and western blot.

Monoclonal Antibodies Against Mtpap (Clone 1D3)

Mouse monoclonal antibody against the human Poly (A) RNA polymerase, mitochondrial (mtPAP). This antibody has been tested for use in immunocytochemistry/immunofluorescence, immunoprecipitation, and western blot.

Novel Target For Contraceptives And Painkillers

The steroid progesterone (P4) is a major component of follicular fluid and is released by ovaries and cumulus cells surrounding the oocyte.  P4 is known to cause rapid and robust elevation of sperm cytoplasmic calcium levels through binding to a non-genomic receptor.  This rise in intracellular calcium leads to changes in sperm motility and primes the cell for acrosomal exocytosis, which is required for fertilization.     UC Berkeley researchers have identified an enzyme as a P4 non-genomic receptor.  The enzyme was found to possess progesterone-stimulated endocannabinoid hydrolase activity, and regulate human sperm activation.  The technology includes methods of modulating the level and/or activity of the enzyme in a cell in an individual. 

A Method For Predicting Glycosylation On Secreted Proteins

Glycosylation is a key post-translational modification that can affect critical properties of proteins produced in biopharmaceutical manufacturing, such as stability, therapeutic efficacy, or immunogenicity. However, unlike a protein's amino acid sequence, glycosylation is hard to engineer since it does not follow any direct equivalent of a genetic code. Despite various attempts to computationally model the process of glycosylation, industrial glycoengineering is still largely carried out using costly and time-consuming trial-and-error strategies and could greatly benefit from computational models that would better meet the requirements for industrial utilization.

Determine Molecular Interaction Dissociation Constant By Quantitative FRET Assay

Background: FRET (Foster Resonance Energy Transfer) assay measures binding affinities of proteins to visualize their interaction with one another. SUMOs (Small Ubiquitin-related Modifiers) are post-translational modification proteins that are involved in many cellular processes with a distinguished role in transcription inhibition when attached to other proteins. SUMO signaling pathways in conjunction with pathogenesis are vigorously investigated to discover the underlying etiological causes for disease. Currently, biopharmaceutical companies spend $1B to find suitable drug targets. Knowledge of protein-protein interactions will help expedite the drug discovery stage and develop new therapeutic drugs that are more efficacious and cheaper.  Description: UCR Researchers have developed a novel, quantitative version of the FRET assay to determine dissociation constants. They were able to achieve this methodology with the SUMO protein and its various interactions with other proteins. This new FRET assay produces consistent results in less than an hour compared to those of traditional methods that take 12 hours for the same experiment.

Monoclonal Antibody Against mtPAP (Clone 3D2)

Mouse monoclonal antibody against the human Poly (A) RNA polymerase, mitochondrial (mtPAP). This antibody has been tested for use in immunocytochemistry/immunofluorescence, immunoprecipitation, and western blot. .

Monoclonal Antibody Against PNPase (Clone 3H5)

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.

Rapid In Vivo Quantitative Imaging for Clinical Diagnosis of Blood Clot Formation

This advanced quantitative real-time in vivo imaging technology provides fast and highly specific non-invasive diagnosis of thrombotic diseases such as stoke and cancer.

Low-Cost Chromatin Assembly Kit

Brief description not available

Mobile Molecular Diagnostics System

There is a growing interest in point-of-care testing (POCT) where testing is done at or near the site of patient care, since POCT has a short therapeutic turnaround time, decreased process steps where errors can occur and only a small sample volume is required to perform a test.    UC Berkeley researchers have developed a mobile molecular diagnostics system that leverages efficient and dependable blood sampling, automated sample preparation, rapid optical detection of multi-analyte nucleic acids and proteins, and user-friendly systems integration with wireless communication.  The system includes a hand-held automated device with an adaptive sample control module, an optical signal transduction module, and an interface to a smartphone making this a reliable and field-applicable system for point-of-care and on-demand diagnostics. 

On-Chip Platform For Single-Molecule Electrical Conductance Measurements

A microchip capable of detecting bacteria and viruses by using nanotechnology to electrically detect RNA-based interactions for identification of plant-associated microbes that cause plant and human diseases.

High Throughput Method to Identify Mutations that Increase or Decrease Protein Stability

UCLA researchers in the Department of Molecular and Medical Pharmacology have developed a novel method for identifying amino acid mutations that affect protein stability with higher accuracy than computational modeling.

A Photobacterium Sp. Alpha2-6-Sialytransferase 9Psp2.6St) A366g Mutant With Increased Expression Level And Improved Activity In Sialylating Tn Antigen

Researchers at the University of California, Davis have developed an improved sialyltransferase that can be used for the preparation of tumor-associated carbohydrate antigens. 

Novel Multivalent Bioassay Reagents

The guiding principle for the creation of biomolecular recognition agents has been that affinity is essential for both strength and specificity.  Monoclonal antibodies, the dominant workhorse of affinity reagents, have mono-valent affinities in the uM-nM range with apparent affinities that can be sub nM with the bi-valency intrinsic in intact immunoglobulin structure.  The avidin-biotin interaction used ubiquitously for biomolecular assembly is femto-molar and both highly specific and essentially irreversible.  High affinity has been proclaimed the essential goal for the selection of useful specific aptamers, though there has been disagreement about a tight coupling of affinity and specificity.  

Self-Assembled Modified Beta Solenoid Protein Scaffolds for Devices And Materials

Available for licensing are patent rights in novel and versatile beta solenoid proteins that are useful as scaffolds for nanoparticle assembly, photocatalytic devices, thermoelectric devices, passive absorption of small atoms or molecules, cement additive, heavy element remediation, heavy element absorption, and as biological catalysts.

Stimuli-Sensitive Intrinsically Disordered Protein Brushes

Recent advances in biomedicine and biotechnology are driving the demand for novel surface functionalization platforms for biologically active molecules. Polymer brush coatings form when macromolecular chains are end-tethered to surfaces at high grafting densities. While there have been notable successes integrating polymer brush coatings with proteins to control biological function, such strategies require covalent conjugation of the protein to the polymer, which can be inefficient and can compromise biological function. Moreover, these polymer brushes almost universally feature synthetic polymers, which are often heterogeneous and do not readily allow incorporation of chemical functionalities at precise sites along the constituent chains. To address these challenges, Researchers at the University of California, Berkeley (UCB) conducted experiments with polymer brushes based on nerve cell neurofilaments as the intrinsically disordered protein (IDP). By cloning a portion of a gene that encodes one of the neurofilament bristles, and re-engineering it such that they could attach the resulting protein to surfaces, UCB investigators have developed a biomimetic, recombinant IDP that can assemble into an environment-sensitive protein brush that swells and collapses dramatically with environmental changes in solution pH and ionic strength. Their research demonstrates that stimuli-responsive brushes can be efficiently integrated with proteins without compromising biological function, which could have broad commercial appeal as a new class of smart biomaterial building blocks.

Suppression Of Allergic Lung Inflammation And Hyperactivity

Phosphorylated Myrisolyated Alanine-rich C Kinase Substrate (MARCKS) is elevated in human and animal asthmatic tissues. In addition, unphosphorylated MARCKS is also the key molecule to trap PIP2 and to interact with PI3K and Src at cell membrane. Researchers at the University of California, Davis have developed a novel, non-toxic, and water soluble peptide, targeting MARCKS’ phosphorylation site domain, that inhibits MARCKS activity and retains PIP2 pool to suppress PIP3 production.  As a result, the peptide treatment is capable of suppression of allergic lung inflammation and hyper-reactivity.

Single-Molecular Homogenous Amplified Detection in Confined Volumes

This novel method detects the concentration of molecules of interest without washing steps or any solid-phase reaction.

Devices and Methods for Subcellular Western Blotting Of Single Cells

The nuclear membrane divides the eukaryotic cell into two compartments between which there is a major interchange of proteins, nucleic acids and small molecules. The physical separation of the nucleoplasm and cytoplasm provides an added level of spatial regulation of protein activity.  Protein subcellular localization is intrinsically linked to function, with aberrant localization linked to numerous diseases such as cancer.  However, existing subcellular analytic devices and methods are slow, offer low multiplexing (about 5 proteins) and are not quantitative.    Scientists at UC Berkeley have designed a microfluidic device for analysis of subcellular compartments (e.g., cytosol, nucleus).  The device and methods differentially lyse specific subcellular compartments in single cells, performs single cell Western blotting solely on proteins in those targeted compartments (5+ proteins per compartment) and serially assays multiple subcellular compartments in the same single cells. 

Shrink-Induced, Self-Driven Microfluidic Devices

The addition of novel surface modifications and use of shrink-wrap film to create devices will yield self-driven, shrink-induced microfluidic detection for samples such as bodily fluids. Novel fabrications and surfaces will have a profound impact on the creation of point of care diagnostics.

Microfluidic Tumor Tissue Dissociation Device

The microfluidic device will be able to dissociate tumor tissue obtained by a needle biopsy from solid tumors into single cells without cell damage. The resulting cells can be used for subsequent molecular analysis to determine cancer diagnosis and help guide treatment. This research tool will improve and standardize tumor sample preparation thereby advancing cancer diagnosis and treatment.

Modified FC Polypeptides and Methods of Use

Chemically based protein modification methods could provide useful strategies for the generation of antibody mimics. However, the highly complex structures of antibody domains make it exceptionally difficult to modify these proteins in a single or small number of locations. This complexity includes the presence of multiple polypeptide chains, extensive disulfide networks, and critically important glycosylation patterns, all of which must remain intact to obtain biological function.   To address these problems, UC Berkeley investigators have developed novel antibody mimics by installing synthetic molecules at the N-termini of crystallizable fragment domains (Fc's) via chemical modification approaches.  The synthesis leads to the production of Fc-synthetic molecule hybrids, where the Fc domains serve as building blocks to improve the pharmacokinetic properties of synthetic agents and provide them with immunological activating properties. 

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