|Other Names||Dual specificity protein phosphatase 7, Dual specificity protein phosphatase PYST2, DUSP7, PYST2|
|Target/Specificity||The synthetic peptide sequence used to generate the antibody AP8450a was selected from the N-term region of human DUSP7. A 10 to 100 fold molar excess to antibody is recommended. Precise conditions should be optimized for a particular assay.|
|Format||The synthetic peptide was lyophilized with 100% acetonitrile and is supplied as a powder. Reconstitute with 0.1 ml deionized water for a final concentration of 1 mg/ml.|
|Storage||Maintain refrigerated at 2-8°C for up to 6 months. For long term storage store at -20°C.|
|Precautions||This product is for research use only. Not for use in diagnostic or therapeutic procedures.|
|Function||Regulates the activity of the MAP kinase family in response to changes in the cellular environment. PYST2-S may act as a negative regulator of PYST2-L although it is unclear whether this is by competing for transcription, translation or activation factors.|
|Tissue Location||Expressed at significantly higher levels in malignant hematopoietic cells than in corresponding non-malignant cells.|
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Provided below are standard protocols that you may find useful for product applications.
DUSP7 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 (MAP)kinase superfamily (MAPK/ERK, SAPK/JNK, p38), which are associatedwith cellular proliferation and differentiation. Different members of the family of dual specificity phosphatases show distinct substrate specificities for various MAP kinases, different tissue distribution and subcellular localization, and different modes of inducibility of their expression by extracellular stimuli.
Immunol. Lett. 92 (1-2), 149-156 (2004)Oncogene 22 (48), 7649-7660 (2003)Meth. Enzymol. 366, 103-113 (2003)J. Cell. Sci. 111 (PT 22), 3389-3399 (1998)EMBO J. 15 (14), 3621-3632 (1996)
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