The kit is designed to allow maximal recovery of immunoprecipitates. It provides all the necessary reagents to perform immunoprecipitation from cell extracts of any protein to which a suitable antibody is available. Based on protein G, the kit binds to most commonly used antibodies. In addition, spin columns are provided to enable quick washes without the loss of protein G resin and thus protein yield is maximized.
Features and Benefits
Minimal loss of antigen-antibody bound beads during washing.
Minimal or no non-specific signals by increasing the stringency of the washing step.
Preparation Note
When preparing reagents, use ultrapure water (17M -cm)
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The BamA protein of Escherichia coli plays a central role in the assembly of β-barrel outer membrane proteins (OMPs). The C-terminal domain of BamA folds into an integral outer membrane β-barrel, and the N terminus forms a periplasmic polypeptide transport-associated
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In Escherichia coli, YaeT, together with four lipoproteins, YfgL, YfiO, NlpB, and SmpA, forms a complex that is essential for beta-barrel outer membrane protein biogenesis. Data suggest that YfgL and YfiO make direct but independent physical contacts with YaeT. Whereas
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Talaromyces (Penicillium) marneffei is one of the leading causes of systemic mycosis in immunosuppressed or AIDS patients in Southeast Asia. How this intracellular pathogen evades the host immune defense remains unclear. We provide evidence that T. marneffei depletes levels of a
The Journal of biological chemistry, 282(48), 35104-35112 (2007-10-04)
During apoptosis, the pro-apoptotic protein Bax relocalizes from the cytosol to the mitochondrial outer membrane. This relocalization is associated to major conformational changes, namely at the N- and C-terminal ends of the protein. Substitution of residues located at critical positions
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Bcl-2 homologues (such as Bcl-x(L)) promote survival in part through sequestration of "activator" BH3-only proteins (such as Puma), preventing them from directly activating Bax. It is thus assumed that inhibition of interactions between activators and Bcl-x(L) is a prerequisite for
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