Recombinant Human Bruton tyrosine kinase/BTK Protein was resolved with SDS-PAGE under reducing (Lane 1) and non-reducing (Lane 2) conditions.
The activity of BTK is based on the MSA technology, and the content and ratio of the substrate and the product are directly separated and detected in real time and dynamically by the different migration rates of the substrate and the product after the enzymatic reaction.
Bruton's tyrosine kinase (BTK) is a tyrosine kinase and contains five different protein interaction domains, including an amino terminal pleckstrin homology (PH) domain, a proline-rich TEC homology (TH) domain, SRC homology (SH) domains SH2 and SH3, as well as a protein kinase domain with tyrosine phosphorylation activity. BTK plays a crucial role in B cell development as it is required for transmitting signals from the pre-B cell receptor that forms after successful immunoglobulin heavy chain rearrangement. It also has a role in mast cell activation through the high-affinity IgE receptor.
