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Application notes
(see key)
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Recommended dilutions
WB: 1/1000 - 1/5000. Predicted molecular weight: 100 kDa. Use at 1/1000 when using colourimetric substrates, use at 1/5000 when using chemiluminescent substrates. Dilution optimised using Chromogenic detection. Not yet tested in other applications. Optimal dilutions/concentrations should be determined by the end user.
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Relevance
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DPP-8 (Dipeptidyl Peptidase-8) is a serine proteinase of the clan SC. The clan SC proteinases have a catalytic triad of Ser-Asp-His, and like other Serine proteinases, the active site serine is in a Gly-Xaa-Ser-Xaa -Gly orientation. DPP-8 is a member of a broader family of dipeptidyl peptidases including DPP-2, DPP-4, FAP/Seprase, DPP-6, DPP-9, DPP-10, which have differing substrate specificity and tissue localizations. DPP-8 is most closely related to DPP-9, with which it shares 58% identical residues. DPP-8 has only 27% identity with DPP-4, but seems to have similar substrate specificity. Although DPP-4 and FAP-a form a surface-bound heterodimer in some cells, and homodimers in others, DPP-8 seems to be a cytoplasmic protein. The original publication determined that DPP-8 was a monomer, active at neutral pH, and later publications suggest DPP-8 is a homodimer. Substrates include glucagon-like peptide-1, glucagon-like peptide-2, neuropeptide-Y, but with different efficacy relative to DPP-4. DPP-8 has been found in highest abundance in the testis and placenta, but is found in most tissues. Several different splice variants of DPP-8 were seen in the different tissues, with some tissue-specific expression. Four different human sequences are reported to date; 898, 882, 847 and 782 amino acids in length. The longest sequence of human DPP-8 has a predicted mass of 103.4 kDa, and pI of 5.42. The 882, 847 and 782 amino acid forms are predicted at 101.4, 97.5 and 89.9 kDa respectively, with pIs of 5.26, 5.55 and 5.07. Another three partial sequences that are alternatively spliced have deletions in the catalytic domain, and may not be catalytically active. Over expression of DPP-8 caused decreased viability in cells, but a catalytically dead mutant of DPP-8 had the same results, thus some of the DPP-8 activity may be non-enzymatic. Two of the splice variants have longer aminotermini (16 AA insert), and this may affect localization in the cell.
This antibody recognizes all four forms of DPP8
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