The oligomeric state of the BRD4(1) in solution was analyzed by gel filtration in a buffer containing 20 mM Hepes pH 7.5, 150 mM NaCl using a Superdex 200 10/300GL column (GE Healthcare) calibrated with globular proteins of known molecular weight (GE Healthcare, 28-4038-41/42). Protein (50 µM) and ligands (6S+2S)-PEG1 (25 µM), (6R+2R)-PEG1 (100 µM), JQ1 (100 µM) or DMSO were mixed and incubated at 20°C for 20 min before injection. Eluting peaks were monitored using ultraviolet absorbance at 280 nm. BRD4(1,2) and domain mutants BRD4(1N140A,2) and BRD4(1,2N433A) corresponding to the N140A and N433A mutants respectively were analyzed using the same method but 42 µM of protein was used with a half equivalence of MT1.
Globular proteins
Manufactured by GE Healthcare
Globular proteins are a class of proteins that have a compact, spherical three-dimensional structure. They perform a variety of core functions, including enzymatic catalysis, transport, and structural support within cells.
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Lab products found in correlation
2 protocols using globular proteins
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Oligomeric State Analysis of BRD4(1)
2
Oligomeric State Analysis of BRD4(1)
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The oligomeric state of the BRD4(1) in solution was analyzed by gel filtration in a buffer containing 20 mM Hepes pH 7.5, 150 mM NaCl using a Superdex 200 10/300GL column (GE Healthcare) calibrated with globular proteins of known molecular weight (GE Healthcare, 28-4038-41/42). Protein (50 µM) and ligands (6S+2S)-PEG1 (25 µM), (6R+2R)-PEG1 (100 µM), JQ1 (100 µM) or DMSO were mixed and incubated at 20°C for 20 min before injection. Eluting peaks were monitored using ultraviolet absorbance at 280 nm. BRD4(1,2) and domain mutants BRD4(1N140A,2) and BRD4(1,2N433A) corresponding to the N140A and N433A mutants respectively were analyzed using the same method but 42 µM of protein was used with a half equivalence of MT1.
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