DUSP24 Antibody (Center) Blocking Peptide
Synthetic peptide
- SPECIFICATION
- CITATIONS
- PROTOCOLS
- BACKGROUND
Primary Accession | Q9Y6J8 |
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Clone Names | 80311170 |
Gene ID | 51657 |
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Other Names | Serine/threonine/tyrosine-interacting-like protein 1, Dual specificity phosphatase inhibitor MK-STYX, Dual specificity protein phosphatase 24, Map kinase phosphatase-like protein MK-STYX, STYXL1, DUSP24, MKSTYX |
Target/Specificity | The synthetic peptide sequence used to generate the antibody AP8875c was selected from the Center region of human DUSP24. A 10 to 100 fold molar excess to antibody is recommended. Precise conditions should be optimized for a particular assay. |
Format | Peptides are lyophilized in a solid powder format. Peptides can be reconstituted in solution using the appropriate buffer as needed. |
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. |
Name | STYXL1 |
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Synonyms | DUSP24, MKSTYX |
Function | Catalytically inactive phosphatase (PubMed:20180778, PubMed:23163895). By binding to G3BP1, inhibits the formation of G3BP1- induced stress granules (PubMed:20180778, PubMed:23163895). Does not act by protecting the dephosphorylation of G3BP1 at 'Ser-149' (PubMed:23163895). Inhibits PTPMT1 phosphatase activity (PubMed:24709986). By inhibiting PTPMT1, positively regulates intrinsic apoptosis (PubMed:21262771). May play a role in the formation of neurites during neuronal development (PubMed:29250526). |
Cellular Location | Mitochondrion matrix |
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Provided below are standard protocols that you may find useful for product applications.
Background
DUSP24 is probable pseudophosphatase. It contains a Ser residue instead of a conserved Cys residue in the dsPTPase catalytic loop which probably renders it catalytically inactive as a phosphatase. The binding pocket may be however sufficiently preserved to bind phosphorylated substrates, and maybe protect them from phosphatases.
References
Ewing,R.M., et.al., Mol. Syst. Biol. 3, 89 (2007)
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