|Application ||WB, E|
|Other Accession||Q60HH1, NP_000382.3|
|Calculated MW||61248 Da|
|Antigen Region||6-34 aa|
|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|
|Target/Specificity||This TPP1 antibody is generated from rabbits immunized with a KLH conjugated synthetic peptide between 6-34 amino acids from the N-terminal region of human TPP1.|
|Format||Purified polyclonal antibody supplied in PBS with 0.09% (W/V) sodium azide. This antibody is purified through a protein A column, followed by peptide affinity purification.|
|Storage||Maintain refrigerated at 2-8°C for up to 2 weeks. For long term storage store at -20°C in small aliquots to prevent freeze-thaw cycles.|
|Precautions||TPP1 Antibody (N-term) is for research use only and 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 of serine proteases. The protease functions in the lysosome to cleave N-terminal tripeptides from substrates, and has weaker endopeptidase activity. It is synthesized as a catalytically-inactive enzyme which is activated and auto-proteolyzed upon acidification. Mutations in this gene result in late-infantile neuronal ceroid lipofuscinosis, which is associated with the failure to degrade specific neuropeptides and a subunit 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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