DUSP13-L184 Antibody (C-term)
Purified Rabbit Polyclonal Antibody (Pab)
- SPECIFICATION
- CITATIONS: 1
- PROTOCOLS
- BACKGROUND
Application ![]()
| IHC-P, WB, E |
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Primary Accession | Q9UII6 |
Reactivity | Human |
Host | Rabbit |
Clonality | Polyclonal |
Isotype | Rabbit IgG |
Calculated MW | 22149 Da |
Antigen Region | 169-198 aa |
Gene ID | 51207 |
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Other Names | Dual specificity protein phosphatase 13 isoform B, DUSP13B, Dual specificity phosphatase SKRP4, Testis- and skeletal-muscle-specific DSP, DUSP13, DUSP13B, TMDP |
Target/Specificity | This DUSP13-L184 antibody is generated from rabbits immunized with a KLH conjugated synthetic peptide between 169-198 amino acids from the C-terminal region of human DUSP13-L184. |
Dilution | WB~~1:1000 IHC-P~~1:50~100 |
Format | Purified polyclonal antibody supplied in PBS with 0.09% (W/V) sodium azide. This antibody is prepared by Saturated Ammonium Sulfate (SAS) precipitation followed by dialysis against PBS. |
Storage | Maintain refrigerated at 2-8°C for up to 2 weeks. For long term storage store at -20°C in small aliquots to prevent freeze-thaw cycles. |
Precautions | DUSP13-L184 Antibody (C-term) is for research use only and not for use in diagnostic or therapeutic procedures. |
Name | DUSP13B (HGNC:19681) |
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Synonyms | DUSP13, SKRP4, TMDP |
Function | Dual specificity phosphatase that dephosphorylates MAPK8/JNK and MAPK14/p38, but not MAPK1/ERK2, in vitro (PubMed:21360282). Exhibits intrinsic phosphatase activity towards both phospho- seryl/threonyl and -tyrosyl residues, with similar specific activities in vitro (PubMed:10585869). |
Tissue Location | Highly expressed in the testis (at protein level) (PubMed:10585869, PubMed:15252030). Also found in the skeletal muscle (PubMed:15252030). |

Provided below are standard protocols that you may find useful for product applications.
Background
Dual-specificity phosphatases, a subfamily of protein-tyrosine phosphatases, play important roles in signal transduction, cell cycle progression, and tumor suppression. The cDNA encoding a novel phosphatase, PIR1, phosphatase that interacts with RNA/RNP complex 1. Sequence analysis revealed that the predicted 329-amino acid protein has homology to several dual-specificity phosphatases and contains 2 stretches of arginine-rich sequence similar to those found in some RNA-binding proteins. In vitro, recombinant protein displays protein-tyrosine phosphatase activity and binds directly to RNA.
References
Nakamura K., Shima H., Watanabe M., Haneji T., Kikuchi K.Biochem. J. 344:819-825(1999). Deloukas et al. Nature 429:375-381(2004). Strausberg et al. Proc. Natl. Acad. Sci. U.S.A. 99:16899-16903(2002).

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