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Buckley J.D.,University of South Australia | Thomson R.L.,University of South Australia | Coates A.M.,University of South Australia | Howe P.R.C.,University of South Australia | And 2 more authors.
Journal of Science and Medicine in Sport | Year: 2010

There is evidence that protein hydrolysates can speed tissue repair following damage and may therefore be useful for accelerating recovery from exercise induced muscle damage. The potential for a hydrolysate (WPIHD) of whey protein isolate (WPI) to speed recovery following eccentric exercise was evaluated by assessing effects on recovery of peak isometric torque (PIT). In a double-blind randomised parallel trial, 28 sedentary males had muscle soreness (MS), serum creatine kinase (CK) activity, plasma TNFα, and PIT assessed at baseline and after 100 maximal eccentric contractions (ECC) of their knee extensors. Participants then consumed 250 ml of flavoured water (FW; n = 11), or FW containing 25 g WPI (n = 11) or 25 g WPIHD (n = 6) and the assessments were repeated 1, 2, 6 and 24 h later. PIT decreased ∼23% following ECC, remained suppressed in FW and WPI, but recovered fully in WPIHD by 6 h (P = 0.006, treatment × time interaction). MS increased following ECC (P < 0.001 for time), and remained elevated with no difference between groups (P = 0.61). TNFα and CK did not change (P > 0.45). WPIHD may be a useful supplement for assisting athletes to recover from fatiguing eccentric exercise. © 2008 Sports Medicine Australia.


Osmond R.I.,TGR BioSciences | Crouch M.F.,TGR BioSciences | Dupriez V.J.,Perkin Elmer Corporation
Current Opinion in Molecular Therapeutics | Year: 2010

GPCRs are a large class of cell-surface receptors that are involved in a diverse array of biological processes, including many that are critical to diseases. As a result, GPCRs are a major focus for drug discovery research, and have been highly amenable to therapeutic intervention. However, the successes to date may represent the 'low-hanging fruit' (ie, outcomes that have been easiest to achieve). The signaling of many GPCRs is now recognized to be substantially more complex than initially thought. Thus, the traditional analysis of single GPCR-mediated secondary messengers for early-stage drug discovery, such as the measurement of Ca2+ or the formation of cAMP, may not provide all of the relevant signaling information on a target receptor or information on all of the effects of potential drugs. Given this complexity, the determination of other signaling events, such as the GPCR-mediated activation of major kinase pathways, including PI3K and MAPK, is likely to become increasingly important in the identification of indicators of GPCR function. Furthermore, the advent of highly efficient assays for detecting the GPCR-mediated activation of protein kinase targets allows this target class to be readily amenable to cell-based high-throughput screening programs. © Thomson Reuters (Scientific) Ltd.


Osmond R.I.W.,TGR BioSciences | Das S.,TGR BioSciences | Crouch M.F.,TGR BioSciences
Analytical Biochemistry | Year: 2010

The signal transducers and activators of transcription (STAT) proteins are a small family of signaling proteins that are crucial for cytokine and growth factor receptor-mediated signaling in various blood cell types. Despite their central role in immune and hematopoietic cellular regulation, there are relatively few options for monitoring receptor-mediated JAK/STAT signaling events in a cell-based format, without the need for cellular transfections or labor intensive methodology. Indeed, traditional methods such as the Western blot or ELISA remain a standard method for determining the phosphorylation status of endogenous STAT proteins. Here we present data for the rapid detection of endogenous receptor-mediated phosphorylation of multiple STAT proteins using the bead-based AlphaScreen SureFire technology. With three different cell lines (human acute monocytic leukemia THP-1 cells, human erythroleukemic TF-1 cells, and human T lymphocytic Jurkat cells), we have optimized a rapid and homogeneous methodology for monitoring endogenous, receptor-mediated signaling via STAT 1, STAT 3, or STAT 5 phosphorylation, in response to several agonists. These assays, which can be tailored for both standard research applications or high-throughput drug screening applications, afford quantitative data for receptor-mediated signaling mechanisms in an endogenous, cellular environment. © 2010 Elsevier Inc.


Patent
TGR BioSciences | Date: 2015-03-09

The present disclosure provides methods and/or kits for detecting an analyte in a sample. Some embodiments provide a method for detecting a non-nucleic acid analyte in a sample using a solid substrate comprising a bound immobilisation agent and an antibody capture agent and a detectable agent, which can bind to the analyte. The antibody capture agent comprises, at a plurality of sites, a ligand for the immobilisation agent. A complex between the analyte, the antibody capture agent and a detectable agent is formed and immobilised on the solid substrate by binding between the immobilisation agent and the ligand. In some embodiments, the ligand and the immobilisation agent are a binding pair comprising a peptide tag and an anti-peptide tag antibody.


Patent
TGR BioSciences | Date: 2016-03-17

The present disclosure provides methods and/or kits for detecting an analyte in a sample. Some embodiments provide a method for detecting a non-nucleic acid analyte in a sample using a solid substrate comprising a bound immobilization agent and an capture agent and a detectable agent, which can bind to the analyte. The capture agent comprises, at a plurality of sites, a ligand for the immobilization agent. A complex between the analyte, the capture agent and a detectable agent is formed and immobilized on the solid substrate by binding between the immobilization agent and the ligand. In some embodiments, the ligand and the immobilization agent are a binding pair comprising a peptide tag and an anti-peptide tag antibody.


Patent
TGR BioSciences | Date: 2015-11-13

The present disclosure provides methods and/or kits for detecting an analyte in a sample. Some embodiments provide a method for detecting a non-nucleic acid analyte in a sample using a solid substrate comprising a bound immobilisation agent and an antibody capture agent and a detectable agent, which can bind to the analyte. The antibody capture agent comprises, at a plurality of sites, a ligand for the immobilisation agent. A complex between the analyte, the antibody capture agent and a detectable agent is formed and immobilised on the solid substrate by binding between the immobilisation agent and the ligand. In some embodiments, the ligand and the immobilisation agent are a binding pair comprising a peptide tag and an anti-peptide tag antibody.


Trademark
TGR BioSciences | Date: 2012-03-13

Reagent kits comprising antibodies for conducting immunoassays for medical or veterinary diagnostic purposes.


Trademark
TGR BioSciences | Date: 2012-09-11

diagnostic preparations and reagents for medical use; diagnostic testing kits consisting of diagnostic preparations and reagents for use in measuring proteins in patient samples and for measuring protein levels in human body fluids.


Patent
TGR BioSciences | Date: 2012-03-30

The present disclosure relates to a one-step immunoassay, in which a solid substrate is pre-coated with an immobilisation agent, and whereby the capture agent, the analyte and the detection agent are added to the solid substrate together, followed by a wash step prior to detection. Methods and kits for detecting an analyte in a sample are disclosed. The capture agent can bind the analyte and comprises a ligand for an immobilisation agent. Certain embodiments are directed to antibody capture agents and/or antibody detectable agents. Certain embodiments are directed to a ligand comprising a peptide tag and an immobilisation agent comprising an anti-peptide tag antibody. Certain embodiments are directed to detection of more than one analyte.


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