|Other Names||Dipeptidase 1, Dehydropeptidase-I, Microsomal dipeptidase, Renal dipeptidase, hRDP, DPEP1, MDP, RDP|
|Format||Synthetic peptide was lyophilized with 100% acetonitrile and is supplied as a powder. Reconstitute with 0.1 ml DI water for a final concentration of 1 mg/ml.|
|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.|
|Function||Hydrolyzes a wide range of dipeptides. Implicated in the renal metabolism of glutathione and its conjugates. Converts leukotriene D4 to leukotriene E4; it may play an important role in the regulation of leukotriene activity.|
|Cellular Location||Apical cell membrane; Lipid-anchor, GPI- anchor. Cell projection, microvillus membrane; Lipid-anchor, GPI- anchor. Note=Brush border membrane|
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Provided below are standard protocols that you may find useful for product applications.
DPEP1 (EC 220.127.116.11) is a kidney membrane enzyme thathydrolyzes a variety of dipeptides and is implicated in renalmetabolism of glutathione and its conjugates, e.g., leukotriene D4(Kozak and Tate, 1982 [PubMed 6122685]). DPEP1 is responsible forhydrolysis of the beta-lactam ring of antibiotics, such as penemand carbapenem (Campbell et al., 1984 [PubMed 6334084]). Earlier,beta-lactamase enzymes were thought to occur only in bacteria,where their probable function was in protecting the organismsagainst the action of beta-lactam antibiotics. These antibioticsexhibit selective toxicity against bacteria but virtual inertnessagainst many eukaryotic cells (Adachi et al., 1990 [PubMed2303490]).
Nan, H., et al. J. Invest. Dermatol. 129(9):2250-2257(2009)Pare, G., et al. Circ Cardiovasc Genet 2(2):142-150(2009)Nitanai, Y., et al. J. Mol. Biol. 321(2):177-184(2002)Kera, Y., et al. Comp. Biochem. Physiol. B, Biochem. Mol. Biol. 123(1):53-58(1999)Satoh, S., et al. Biotechnol. Prog. 10(2):134-140(1994)
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