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DUSP12 Antibody (Center) Blocking Peptide

Synthetic peptide

     
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Product Information
Primary Accession Q9UNI6
Clone Names 100525016
Additional Information
Gene ID 11266
Other Names Dual specificity protein phosphatase 12, Dual specificity tyrosine phosphatase YVH1, DUSP12
Format Peptides are lyophilized in a solid powder format. Peptides can be reconstituted in solution using the appropriate buffer as needed.
StorageMaintain refrigerated at 2-8°C for up to 6 months. For long term storage store at -20°C.
PrecautionsThis product is for research use only. Not for use in diagnostic or therapeutic procedures.
Protein Information
Name DUSP12
Function Dual specificity phosphatase; can dephosphorylate both phosphotyrosine and phosphoserine or phosphothreonine residues. Can dephosphorylate glucokinase (in vitro) (By similarity). Has phosphatase activity with the synthetic substrate 6,8-difluoro-4-methylumbelliferyl phosphate and other in vitro substrates (PubMed:10446167, PubMed:24531476).
Cellular Location Nucleus. Cytoplasm, cytosol. Note=Primarily nuclear. Detected in a mesh-like pattern in the cytosol.
Tissue Location Ubiquitous, highest expression in spleen, testis, ovary, and peripheral blood leukocytes and lower expression in liver and lung
Research Areas
Citations (0)
citation

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Background

The protein encoded by this gene is a member of the dualspecificity protein phosphatase subfamily. These phosphatasesinactivate their target kinases by dephosphorylating both thephosphoserine/threonine and phosphotyrosine residues. Theynegatively regulate members of the mitogen-activated protein (MAP)kinase superfamily (MAPK/ERK, SAPK/JNK, p38), which is associatedwith cellular proliferation and differentiation. Different membersof the family of dual specificity phosphatases show distinctsubstrate specificities for various MAP kinases, different tissuedistribution and subcellular localization, and different modes ofinducibility of their expression by extracellular stimuli. Thisgene product is the human ortholog of the Saccharomyces cerevisiaeYVH1 protein tyrosine phosphatase. It is localized predominantly inthe nucleus, and is novel in that it contains, and is regulated bya zinc finger domain.

References

Biernacki, M.A., et al. Cancer Res. 70(3):906-915(2010)Bonham, C.A., et al. J. Biol. Chem. 284(34):22853-22864(2009)Sharda, P.R., et al. Biochem. J. 418(2):391-401(2009)Gao, F., et al. Zhonghua Yi Xue Za Zhi 88(32):2250-2253(2008)Hasstedt, S.J., et al. Ann. Hum. Genet. 72 (PT 2), 163-169 (2008) :

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$ 277.78
Cat# BP16903c
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