A portion of amino acids 346-376 from the human protein were used as the immunogen for the SPAK antibody.
SPAK is a serine/threonine kinase containing an N-terminal series of proline and alanine repeats (PAPA box), followed by a serine/threonine kinase catalytic domain, a nuclear localization signal, a consensus caspase cleavage recognition motif, and a C-terminal region. Northern blot analysis detects ubiquitous expression, most abundantly in brain and pancreas. SPAK can phosphorylate itself and an exogenous substrate in vitro. SPAK immunoprecipitates from transfected mammalian cells in a complex with another serine/threonine kinase that phosphorylates catalytically inactive SPAK. SPAK activates the p38 MAP kinase pathway in cotransfection assays. Full-length SPAK is expressed in the cytoplasm in transfected cells, while a mutant corresponding to caspase-cleaved STK39 localizes predominantly in the nucleus.
Western blot: 1:1000,Immunohistochemistry (FFPE): 1:50-1:100
Application Notes:
The stated application concentrations are suggested starting points. Titration of the SPAK antibody may be required due to differences in protocols and secondary/substrate sensitivity.
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