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TPP1 Antibody (N-term) Blocking Peptide
Synthetic peptide
- SPECIFICATION
- CITATIONS
- PROTOCOLS
- BACKGROUND
| Primary Accession | O14773 |
|---|---|
| Clone Names | 100617267 |
| Gene ID | 1200 |
|---|---|
| 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 | Peptides are lyophilized in a solid powder format. Peptides can be reconstituted in solution using the appropriate buffer as needed. |
| 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. |
| Name | TPP1 |
|---|---|
| Synonyms | CLN2 |
| Function | Lysosomal serine protease with tripeptidyl-peptidase I activity (PubMed:11054422, PubMed:19038966, PubMed:19038967). May act as a non-specific lysosomal peptidase which generates tripeptides from the breakdown products produced by lysosomal proteinases (PubMed:11054422, PubMed:19038966, PubMed:19038967). Requires substrates with an unsubstituted N-terminus (PubMed:19038966). |
| 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 |
Thousands of laboratories across the world have published research that depended on the performance of antibodies from Abcepta to advance their research. Check out links to articles that cite our products in major peer-reviewed journals, organized by research category.
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Provided below are standard protocols that you may find useful for product applications.
Background
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.
References
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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