DUSP8 (Dual Specificity Protein Phosphatase 8, Dual Specificity Protein Phosphatase hVH-5, VH5)

Ser/ Thr and Tyr dual specificity phosphatases comprise a group of enzymes with both Ser/Thr and tyrosine specific protein phosphatase activity which are capable of removing both the serine/threonine or tyrosine-bound phosphate groups from a wide range of phosphoproteins, which have been phosphorylated under the action of a kinase. Dual specificity protein phosphatases (DSPs) are implicated in the roles of mitogenic signal transduction regulation as well as cell cycle control. The expression of DUSP1 gene is induced in human skin fibroblasts by oxidative:heat stress as well as growth factors and specifies a protein with structural features similar to members of the non-receptor-type protein-tyrosine phosphatase family. It has significant amino-acid sequence similarity to a Tyr/Ser-protein phosphatase encoded by the late gene H1 of vaccinia virus. Purified DUSP1 protein has intrinsic phosphatase activity, and specifically inactivates mitogen-activated protein (MAP) kinase in vitro by the concomitant dephosphorylation of both its phosphothreonine and phosphotyrosine residues. Additionally, it suppresses the activation of MAP kinase by oncogenic ras in extracts of Xenopus oocytes. Thus, DUSP1 may play an important role in the human cellular response to environmental stress as well as in the negative regulation of cellular proliferation. The Dual specificity protein phosphatase motif is found in 5 isoforms from this gene. 45 other genes in the database also contain this motif. Applications: Suitable for use in ELISA. Other applications not tested. Recommended Dilution: ELISA: 1:100-1:1000 Optimal dilutions to be determined by the researcher. 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. Aliquots are stable for at least 12 months. For maximum recovery of product, centrifuge the original vial after thawing and prior to removing the cap.