Rabbit Antibody to DPP-10 (Dipeptidyl Peptidase-10, DPP-Y, DPL2); Stalk region

RP1-DPP-10 is a rabbit polyclonal antibody made to the serine protease DPP-10. The antibody is made to a synthetic peptide based on stalk region of human DPP-10.  RP1-DPP-10 reacts with human, mouse and rat DPP-10, and does not recognize other DPP family members. The antibody has been peptide-affinity purified, concentrated to 1.0 mg/ml, with the addition of 0.05% sodium azide as preservative and 50% glycerol as cryoprotectant.

DPP-10 (Dipeptidyl Peptidase-9) is a Type-II transmembraneserine 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.  In DPP-10, the catalytic serine is missing, as is the case for DPP-6, and both proteins are considered catalytically incompetent.  DPP-10 is a member of a broader family of dipeptidyl peptidases including DPP-2, DPP-4, FAP/Seprase, DPP-6, DPP-8, DPP-9, which have differing substrate specificity and tissue localizations.  DPP-10 shares 51% sequence identity with DPP-6, 32% identity with DPP-4, and 29% identity with FAP-α. DPP-4 and FAP-α form a surface-bound heterodimer in some cells, and homodimers in others, and DPP-10 may play a similar role if partnered with another DPP enzyme. DPP-10 has been identified as an asthma-associated protease, similar to ADAM-33, and linkage analysis studies are attempting to dissect out the role these enzymes play in the disease. DPP-10 has been found in highest abundance in the brain and pancreas, but different splice variants can be found in many tissues. Four different splice variants of DPP-10 are reported to date; 800, 796, 792 and 789 amino acids in length. The differences are entirely in the cytoplasmic domain of DPP-10. The 800 amino acid sequence of human DPP-10 has a predicted mass of 91.2 kDa, and pI of 5.87, but several glycosylation sites make DPP-10 run at larger sizes on SDS PAGE gels. The 796, 792 and 789 amino acid forms are predicted at 90.9, 90.3 and 90.2 kDa respectively (although all three are likely glycosylated), with pIs of 6.1, 5.7 and 5.9. DPP-10 is thought to be shed from the cell surface by proteolytic cleavage of the linker regions, and is shed from the cells, like the other transmembrane serine proteases. DPP-10 is thought to regulate voltage-gated potassium channels, similar to the role DPP-6 is thought to play. A ternary complex of DPP-10, Kv4 and KChIP3 forms a pore. Interestingly, the potassium channel accessory activity seems to reside in the cytoplasmic and transmembrane domains, not the catalytic domain. RP1-DPP-10 recognizes all four forms of DPP-10. A recommended starting concentration for Western blots is 1:1,000 when using colorimetric substrates such as BCIP/NBT, and 1:5,000 for chemiluminescent substrates.  Higher concentrations of antibody may be needed for samples from more distantly related species.  

FOR RESEARCH USE ONLY. NOT FOR USE IN HUMANS.

The undiluted antibody solution is stable for approximately 12 months at -20°C.

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