Newsroom

New web-site launched

11 Oct 2009: Badrilla publishes a new web-site providing clear and comprehensive technical information on its products. This is designed to assist the selection of products, and to display the suitability of individual products for individual experimental systems.

New phospho-antibodies to RYR2 and L-type Ca2+-channel released

11 Oct 2009: Badrilla announces the release of new phospho-specific antibodies Ryanodine Receptor 2 and L-type Ca2+-channel (DHPR/Cav 1.2). Three rabbit polyclonal antibodies specific for RYR2-phosphoSer2030 (cAMP kinase site), RYR2-phosphoSer2814 (CaMKII site), and Cav1.2-phosphoSer1928 (cAMP kinase site) are now available. The antibodies can be used in western blotting and/or immunofluorescence microscopy experimental formats to explore the phosphorylation status of these proteins in cardiac myocytes, and define their role in health and disease.

New phospho-specific antibodies released

9th December 2006: Badrilla announces the release of two new phospho-specific antibodies to SERCA2 phosphorylated on Ser-38 and CaMkinase II phosphorylated on Thr-286 or -287 (depending on the isoform in question). These antibodies are both rabbit polyclonal antibodies, and have the same high standard of specificity which is enjoyed throughout our product range. Antibodies are provided in pack sizes capable of performing numerous Western blots (100mL), approximately 20 mini-gel blots in our experience. The antibody to phospho-SERCA is accompanied by a positive control sample, as we have not to date identified conditions which provoke phosphorylation of this protein in biological specimens.

Calibration Tools for Quantitative Biology: a vital step forward

26th July 2005: Badrilla announces the publication of a simple calibration technology capable of providing wholly quantitative data from immunoassays, including western blots. This will permit description of the number of moles of each component of interest in a biological specimen, bringing new clarity to molecular descriptions of biological and biomedical processes.

Modern biological research seeks to describe the molecular events underlying important natural phenomena, which requires quantitative information regarding all parameters in a system. This includes definition of the concentration of components (proteins) in a system and their activity, which is often regulated by their state of phosphorylation. At present these simple parameters are unknown, as the data generated relate to the intensity of the immunosignal observed, rather than the concentration of component of interest. The relationship between these two parameters (signal intensity and antigen concentration) is unknown, which prevents the quantitative description of the system under study. To overcome this limitation, Badrilla has created a calibration technology, which will be delivered to scientists as a simple accessory reagent, to calibrate the signals generated from their most popular techniques (Western blot, ELISA). This will permit calculation of the concentration of each component (protein, phosphoprotein) in a specimen, and will take biological research to a new, wholly quantitative level.

The technology presents a defined concentration of epitope features (the feature recognised by an antibody) fused to a presentation molecule of known molecular weight and pI, which ensures that the product is homogeneous in character, and possesses physical characteristics suited to the experimental procedure of the researcher (Rodriguez et al. (2004) J. Biol. Chem. 279, 17111; Colyer (2005) patent PCT/GB05/000015). A serial dilution of this product defines the relationship between antibody signal intensity and the concentration of the molecule of interest, thereby calibrating all experimental data.

Enquiries and requests for further information should be directed to John Colyer at info62972@badrilla.com

New anti-phospho-PLB (Thr-17) antibody

7th June 2003: Badrilla launches new antibody to Thr-17 phosphorylated PLB with the same quality as the previous serum, but with greater apparent sensitivity. As the stocks of the original anti-phospho-PLB (Thr-17) reduced, we have explored the properties of sera obtained from the immunisation of other rabbits. One such serum displayed outstanding results, with greater stability than the original serum and greater sensitivity, whilst retaining the quality of discrimination between phosphorylation sites which all researchers require. This serum has now replaced the original antiserum and is distributed under catalogue A010-13.

It should be noted that a non-specific interaction between antibodies in this serum (0503-01) and a protein of ~30kDa is observed in rat cardiac homogenates. The interaction is not affected by epitope peptide and thus is unrelated to PLB. We recommend, as always, that specific interactions are identified through the use of epitope peptides in all experiments performed. An example of such an experiment is shown in our data sheet. Epitope peptides are available to all antibodies distributed by Badrilla.