DUSP3 is a member of the dual specificity protein phosphatase subfamily. These phosphatases inactivate their target kinases by dephosphorylating both the phosphoserine/threonine and phosphotyrosine residues. They negatively regulate members of the mitogen-activated protein kinase superfamily, which are associated with cellular proliferation and differentiation. DUSP3 is expressed in both breast and ovarian tissues. DUSP3 Shows activity both for tyrosine-protein phosphate and serine-protein phosphate, but displays a strong preference toward phosphotyrosines. Specifically dephosphorylates and inactivates ERK1 and ERK2.
Source:
Recombinant corresponding to aa1-185 from human DUSP, fused to His-tag at N-terminal expressed in E.coli.
AA Sequence:
MGSSHHHHHH SSGLVPRGSH MSGSFELSVQ DLNDLLSDGS GCYSLPSQPC NEVTPRIYVG NASVAQDIPK LQKLGITHVL NAAEGRSFMH VNTNANFYKD SGITYLGIKA NDTQEFNLSA YFERAADFID QALAQKNGRV LVHCREGYSR SPTLVIAYLM MRQKMDVKSA LSIVRQNREI GPNDGFLAQL CQLNDRLAKE GKLKP
Molecular Weight:
~22.6kD (MALDI-TOF)
Biological Activity:
Determined by measuring the amount of enzyme hydrolyzing 1nm of p-nitrophenyl phosphate (pNPP) per minute at 37C, pH 7.5 using 10mM of substrate, corresponding to a specific activity of >1750IU/mg.
Storage and Stability:
May be stored at 4 degrees C for short-term only. Aliquot to avoid repeated freezing and thawing. Store at -20 degrees C. For maximum recovery of product, centrifuge the original vial after thawing and prior to removing the cap. Further dilutions can be made in assay buffer.
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