Designed for immunoprecipitation applications. This product is blocked with BSA to reduce non-specific binding and cannot be used for purification; best for bovine, goat, human, and rat IgG and for mouse IgG1.
Protein G PLUS agarose suspension specifically formulated for immunoprecipitation.
Other Notes
Agarose solution is supplied ready to use. Protein G Plus agrarose is blocked with BSA and should not be used for immunoglobulin purification or covalent cross-linking. For immunoprecipitation reactions 15 µl/µg primary antibody is recommended. Preclearing will minimize extra bands resulting from nonspecific precipitation. To preclear, add to the sample 20 µl agarose conjugate and 1 µg normal IgG from the same species as the immunoprecipitating antibody. When immunoblotting is used for detection, some secondary antibodies can react nonspecifically with BSA or other proteins present at high concentrations in the sample. This can be eliminated by reducing the concentration of secondary antibody.
Legal Information
CALBIOCHEM is a registered trademark of Merck KGaA, Darmstadt, Germany
Search for Certificates of Analysis (COA) by entering the products Lot/Batch Number. Lot and Batch Numbers can be found on a product’s label following the words ‘Lot’ or ‘Batch’.
Already Own This Product?
Find documentation for the products that you have recently purchased in the Document Library.
Journal of proteome research, 9(6), 3135-3145 (2010-05-05)
Type 1 diabetes, in human patients and NOD mice, results from an immune attack on insulin-producing beta-cells of the pancreas by autoreactive T lymphocytes. In NOD mice, genetically controlled perturbations in the signaling pathways downstream of the antigen-specific T cell
Stem cells and development, 25(10), 774-787 (2016-03-17)
The remarkable functional plasticity of professional antigen-presenting cells (APCs) allows the adaptive immune system to respond specifically to an incredibly diverse array of potential pathogenic insults; nonetheless, the specific molecular effectors and mechanisms that underpin this plasticity remain poorly characterized.
American journal of physiology. Cell physiology, 302(1), C27-C45 (2011-09-24)
Although extensive phosphoproteomic information is available for renal epithelial cells, previous emphasis has been on phosphorylation of serines and threonines with little focus on tyrosine phosphorylation. Here we have carried out large-scale identification of phosphotyrosine sites in pervanadate-treated native inner