S100A9 protein (Tagged-His Tag) (ab91727)
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 ab91727 in the following tested applications.
The application notes include recommended starting dilutions; optimal dilutions/concentrations should be determined by the end user.
Not yet tested in other applications.
Optimal dilutions/concentrations should be determined by the end user.
- Leukocyte L1 complex heavy chain60B8AGCAGB
- Calgranulin BCalgranulin-BCalprotectin L1H subunitCFAGCGLBL1AGLeukocyte L1 complex heavy chainLIAGMAC387MIFMigration inhibitory factor related protein 14Migration inhibitory factor-related protein 14MRP 14MRP-14MRP14NIFOTTHUMP00000015331P14Protein S100-A9S100 A9S100 calcium binding protein A9S100 calcium binding protein A9 calgranulin BS100 calcium-binding protein A9S100A9S10A9_HUMAN
Contains 2 EF-hand domains.
modificationsPhosphorylated. Phosphorylation inhibits activation of tubulin polymerization.
S100A9 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 S100A9 protein (Tagged-His Tag) (ab91727)
ab91727 has not yet been referenced specifically in any publications.