DPP10 Antibody (Center) Blocking Peptide
Synthetic peptide
- SPECIFICATION
- CITATIONS
- PROTOCOLS
- BACKGROUND
Primary Accession | Q8N608 |
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Clone Names | 90921134 |
Gene ID | 57628 |
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Other Names | Inactive dipeptidyl peptidase 10, Dipeptidyl peptidase IV-related protein 3, DPRP-3, Dipeptidyl peptidase X, DPP X, Dipeptidyl peptidase-like protein 2, DPL2, DPP10, DPRP3, KIAA1492 |
Target/Specificity | The synthetic peptide sequence used to generate the antibody AP9000c was selected from the Center region of human DPP10. 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 | DPP10 |
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Synonyms | DPRP3, KIAA1492 |
Function | Promotes cell surface expression of the potassium channel KCND2 (PubMed:15454437). Modulates the activity and gating characteristics of the potassium channel KCND2 (PubMed:15454437). Has no dipeptidyl aminopeptidase activity (PubMed:12662155). |
Cellular Location | Cell membrane {ECO:0000250|UniProtKB:Q6NXK7, ECO:0000269|PubMed:14566338}; Single-pass type II membrane protein {ECO:0000250|UniProtKB:P42658} |
Tissue Location | Found in serum, T-cells and brain (at protein level). Expressed in brain, pancreas, spinal cord and adrenal glands |
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Provided below are standard protocols that you may find useful for product applications.
Background
DPP10 is a single-pass type II membrane protein that is a member of the S9B family in clan SC of the serine proteases. This protein has no detectable protease activity, most likely due to the absence of the conserved serine residue normally present in the catalytic domain of serine proteases. However, it does bind specific voltage-gated potassium channels and alters their expression and biophysical properties.
References
Blakey J.D., et.al., Thorax 64:381-387(2009).
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