TAF1C protein (Tagged-His Tag) (ab92121)
This protein was expressed as an N-terminal His-tag fusion protein using Escherichia coli, and purified using Immobilized Metal Ion Affinity Chromatography. In some cases, smaller protein fragments may be present in addition to the intended expression product as a result of premature termination during translation in E. coli and subsequent co-purification via the His-tag. In some cases purified proteins run at a molecular weight different to the theoretically calculated molecular weight. This may be as a result of unequally distributed charges in the amino acid sequence. Alternatively, dimerisation of the expression product can occur under oxygen limitation during expression/cultivation.
Constituents: 0.5% Trehalose, 6M Urea, 100mM Sodium phosphate, 10mM Sodium chloride, pH 4.5
Our Abpromise guarantee covers the use of ab92121 in the following tested applications.
The application notes include recommended starting dilutions; optimal dilutions/concentrations should be determined by the end user.
SDS-PAGE: Use at an assay dependent dilution.
Not yet tested in other applications.
Optimal dilutions/concentrations should be determined by the end user.
- RNA polymerase I-specific TBP-associated factor 110 kDaSL1Taf1c
- TAF1C_HUMANTAFI110TAFI95TATA box binding protein associated factor 1CTATA box-binding protein-associated factor 1CTATA box-binding protein-associated factor RNA polymerase I subunit CTBP associated factor 1CTBP associated factor RNA polymerase I 95 kDaTBP associated factor, RNA polymerase I, 110-KDTBP-associated factor 1CTranscription initiation factor SL1/TIF-IB subunit C
modificationsPhosphorylated upon DNA damage, probably by ATM or ATR.
TAF1C protein (Tagged-His Tag) images
The image shows an electrophoretic assay performed using an Agilent 5100 ALP. In some images coloured control bands can be seen at 15 kDa (green) and/or 240 kDa (purple). The protein-specific band is blue.
References for TAF1C protein (Tagged-His Tag) (ab92121)
ab92121 has not yet been referenced specifically in any publications.