Adenylate Kinase 1 protein (Tagged-His Tag) (ab91894)
Overview
Properties
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
Concentration information loading...Applications
Our Abpromise guarantee covers the use of ab91894 in the following tested applications.
The application notes include recommended starting dilutions; optimal dilutions/concentrations should be determined by the end user.
| Application | Notes |
|---|---|
| SDS-PAGE | |
| MS |
SDS-PAGE: Use at an assay dependent dilution.
Not yet tested in other applications.
Optimal dilutions/concentrations should be determined by the end user.
Protein info
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Alternative names
- Adenylate kinase 1Adenylate kinase isoenzyme 1Adenylate kinase soluble
- AK 1AK1ATP AMP transphosphorylaseATP-AMP transphosphorylase 1KAD1_HUMANMyokinase
see all
Target information above from: UniProt accession
P00568
The UniProt Consortium
The Universal Protein Resource (UniProt) in 2010
Nucleic Acids Res. 38:D142-D148 (2010)
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Adenylate Kinase 1 protein (Tagged-His Tag) images
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The image shows an electrophoretic assay performed using an Agilent 5100 ALP. In some images colored control bands can be seen at 15 kDa (green) and/or 240 kDa (purple). The protein-specific band is blue.
References for Adenylate Kinase 1 protein (Tagged-His Tag) (ab91894)
ab91894 has not yet been referenced specifically in any publications.
