|Other Names||Tripeptidyl-peptidase 1, TPP-1, Cell growth-inhibiting gene 1 protein, Lysosomal pepstatin-insensitive protease, LPIC, Tripeptidyl aminopeptidase, Tripeptidyl-peptidase I, TPP-I, TPP1, CLN2|
|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||Lysosomal serine protease with tripeptidyl-peptidase I activity. May act as a non-specific lysosomal peptidase which generates tripeptides from the breakdown products produced by lysosomal proteinases. Requires substrates with an unsubstituted N-terminus (By similarity).|
|Cellular Location||Lysosome. Melanosome. Note=Identified by mass spectrometry in melanosome fractions from stage I to stage IV|
|Tissue Location||Detected in all tissues examined with highest levels in heart and placenta and relatively similar levels in other tissues|
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Provided below are standard protocols that you may find useful for product applications.
This gene encodes a member of the sedolisin family ofserine proteases. The protease functions in the lysosome to cleaveN-terminal tripeptides from substrates, and has weakerendopeptidase activity. It is synthesized as acatalytically-inactive enzyme which is activated andauto-proteolyzed upon acidification. Mutations in this gene resultin late-infantile neuronal ceroid lipofuscinosis, which isassociated with the failure to degrade specific neuropeptides and asubunit of ATP synthase in the lysosome.
Souweidane, M.M., et al. J Neurosurg Pediatr 6(2):115-122(2010)Walus, M., et al. Hum. Mutat. 31(6):710-721(2010)Latrick, C.M., et al. EMBO J. 29(5):924-933(2010)Kuizon, S., et al. PLoS ONE 5 (8), E11929 (2010) :Goldberg-Stern, H., et al. Pediatr. Neurol. 41(4):297-300(2009)
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