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P 300-Ch1 302-531
The His-tag recombinant protein is purified by affinity chromatography in combination with FPLC columns.
The purified P300-Ch1 is greater than 90% homogeneous based on SDS-PAGE analysis.
1 unit equals 1 nanogram of purified protein. 1-5 units are sufficient for a gel mobility shift assay in a 20µl reaction; 50-100 units are sufficient for reconstituted transcription assay and 100-200 units are sufficient for a protein-protein interaction assay or an acetylation assay.
Recombinant p300-Ch1 can be used for: 1) protein-protein interaction assay; 2) in vitro transcription assay; 3) in vitro acetylation assay; and 4) cell growth assay. For Research Use Only.
The protein is in 20mM Tris-HCl pH7.9,100mM NaCl, 0.2mM EDTA, 1mM DTT and 20% glycerol. Stored at -70°C before use. Avoid repeated freeze thaw cycles.
Homo sapiens E1A binding protein p300 (EP300), KAT3B; p300 and RSTS2.
MGQQPAPQVQ QPGLVTPVAQ GMGSGAHTAD PEKRKLIQQQ LVLLLHAHKC QRREQANGEV
RQCNLPHCRT MKNVLNHMTH CQSGKSCQVA HCASSRQIIS HWKNCTRHDC PVCLPLKNAG
DKRNQQPILT GAPVGLGNPS SLGVGQQSAP NLSTVSQIDP SSIERAYAAL GLPYQVNQMP
TQPQVQAKNQ QNQQPGQSPQ GMRPMSNMSA SPMGVNGGVG VQTPSLLSDS
Human p300 and CBP (CREB binding protein) are highly related transcriptional coactivators. Both proteins have been identified through protein interaction assays (1-3). In addition to interacting with a variety of cellular factors and onco-proteins, loss of the wild type CBP alleles in isolated tumors suggests that CBP/p300 might serve as tumor suppressors (4). The ability of p300 to acetylate many transcription factors, including p53, E2F, TFIIE, and TFIIF etc. demonstrated a novel mechanism of targeted p300 regulation of gene expression (5-7). The Zn(2+)-binding cysteine/histidine-rich 1 (CH1) domain of p300/CBP binds many of these transcription factors.
This products is recommended For RESEARCH USE ONLY and is Not qualified for Use in Diagnostic or Therapeutic Procedures.
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