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DUSP19 Antibody (N-term) Blocking Peptide
Synthetic peptide
- SPECIFICATION
- CITATIONS
- PROTOCOLS
- BACKGROUND
| Primary Accession | Q8WTR2 |
|---|---|
| Clone Names | 80311161 |
| Gene ID | 142679 |
|---|---|
| Other Names | Dual specificity protein phosphatase 19, Dual specificity phosphatase TS-DSP1, Low molecular weight dual specificity phosphatase 3, LMW-DSP3, Protein phosphatase SKRP1, Stress-activated protein kinase pathway-regulating phosphatase 1, SAPK pathway-regulating phosphatase 1, DUSP19, DUSP17, LMWDSP3, SKRP1 |
| Target/Specificity | The synthetic peptide sequence used to generate the antibody AP9029a was selected from the N-term region of human DUSP19. 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 | DUSP19 (HGNC:18894) |
|---|---|
| Synonyms | DUSP17, LMWDSP3, SKRP1 |
| Function | Has a dual specificity toward Ser/Thr and Tyr-containing proteins. |
| Tissue Location | Expressed in the heart, lung, liver, and pancreas. The expression level in the pancreas is the highest |
Thousands of laboratories across the world have published research that depended on the performance of antibodies from Abcepta to advance their research. Check out links to articles that cite our products in major peer-reviewed journals, organized by research category.
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Provided below are standard protocols that you may find useful for product applications.
Background
Dual-specificity phosphatases (DUSPs) constitute a large heterogeneous subgroup of the type I cysteine-based protein-tyrosine phosphatase superfamily. DUSPs are characterized by their ability to dephosphorylate both tyrosine and serine/threonine residues. They have been implicated as major modulators of critical signaling pathways. DUSP19 contains a variation of the consensus DUSP C-terminal catalytic domain, with the last serine residue replaced by alanine, and lacks the N-terminal CH2 domain found in the MKP (mitogen-activated protein kinase phosphatase) class of DUSPs (see MIM 600714).
References
Cheng,H., et.al., Int. J. Biochem. Cell Biol. 35 (2), 226-234 (2003)
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