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Tripeptidyl Peptidase I (TPP1)

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CLN2; GIG1; LPIC; Tripeptidyl aminopeptidase; Lysosomal pepstatin-insensitive protease; Ceroid-Lipofuscinosis,Neuronal 2,Late Infantile; Cell growth-inhibiting gene 1 protein

Tripeptidyl Peptidase I (TPP1)
CCC C828
HGNC 2073
MGI 1336194
PubMed 24513288
RGD 621296
UniProt O14773
Wiki TPP1
Tripeptidyl-peptidase 1 is 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.Detected in all tissues examined with highest levels in heart and placenta and relatively similar levels in other tissues.

Organism species: Homo sapiens (Human)

CATALOG NO. PRODUCT NAME APPLICATIONS
Proteins RPC828Hu01 Recombinant Tripeptidyl Peptidase I (TPP1) Positive Control; Immunogen; SDS-PAGE; WB.
Antibodies PAC828Hu01 Polyclonal Antibody to Tripeptidyl Peptidase I (TPP1) WB; IHC; ICC; IP.
MAC828Hu22 Monoclonal Antibody to Tripeptidyl Peptidase I (TPP1) WB; IHC; ICC; IP.
Assay Kits SEC828Hu ELISA Kit for Tripeptidyl Peptidase I (TPP1) Enzyme-linked immunosorbent assay for Antigen Detection.

Organism species: Mus musculus (Mouse)

CATALOG NO. PRODUCT NAME APPLICATIONS
Proteins RPC828Mu01 Recombinant Tripeptidyl Peptidase I (TPP1) Positive Control; Immunogen; SDS-PAGE; WB.
RPC828Mu02 Recombinant Tripeptidyl Peptidase I (TPP1) Positive Control; Immunogen; SDS-PAGE; WB.
Antibodies PAC828Mu01 Polyclonal Antibody to Tripeptidyl Peptidase I (TPP1) WB; IHC; ICC; IP.
PAC828Mu02 Polyclonal Antibody to Tripeptidyl Peptidase I (TPP1) WB; IHC; ICC; IP.
Assay Kits SEC828Mu ELISA Kit for Tripeptidyl Peptidase I (TPP1) Enzyme-linked immunosorbent assay for Antigen Detection.

Organism species: Rattus norvegicus (Rat)

CATALOG NO. PRODUCT NAME APPLICATIONS
Proteins n/a Recombinant Tripeptidyl Peptidase I (TPP1) Recombinant Protein Customized Service Offer
Antibodies n/a Monoclonal Antibody to Tripeptidyl Peptidase I (TPP1) Monoclonal Antibody Customized Service Offer
n/a Polyclonal Antibody to Tripeptidyl Peptidase I (TPP1) Polyclonal Antibody Customized Service Offer
Assay Kits n/a CLIA Kit for Tripeptidyl Peptidase I (TPP1) CLIA Kit Customized Service Offer
n/a ELISA Kit for Tripeptidyl Peptidase I (TPP1) ELISA Kit Customized Service Offer
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  14. "Crystal structure and autoactivation pathway of the precursor form of human tripeptidyl-peptidase 1, the enzyme deficient in late infantile ceroid lipofuscinosis."J. Biol. Chem. 284:3985-3997(2009) [PubMed] [Europe PMC] [Abstract]
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  16. "Prenatal testing for late infantile neuronal ceroid lipofuscinosis."Ann. Neurol. 47:254-257(2000) [PubMed] [Europe PMC] [Abstract]
  17. "Heterogeneity of late-infantile neuronal ceroid lipofuscinosis."Genet. Med. 2:312-318(2000) [PubMed] [Europe PMC] [Abstract]
  18. "Two novel CLN2 gene mutations in a Chinese patient with classical late-infantile neuronal ceroid lipofuscinosis."Am. J. Med. Genet. 99:161-163(2001) [PubMed] [Europe PMC] [Abstract]
  19. "New mutations in the neuronal ceroid lipofuscinosis genes."Eur. J. Paediatr. Neurol. 5:7-10(2001) [PubMed] [Europe PMC] [Abstract]
  20. "Expression and analysis of CLN2 variants in CHO cells: Q100R represents a polymorphism, and G389E and R447H represent loss-of-function mutations."Hum. Mutat. 18:165-165(2001) [PubMed] [Europe PMC] [Abstract]
  21. "Late infantile neuronal ceroid lipofuscinosis: quantitative description of the clinical course in patients with CLN2 mutations."Am. J. Med. Genet. 112:347-354(2002) [PubMed] [Europe PMC] [Abstract]
  22. "Identification of novel CLN2 mutations shows Canadian specific NCL2 alleles."J. Med. Genet. 39:822-825(2002) [PubMed] [Europe PMC] [Abstract]
  23. "Tripeptidyl peptidase 1 deficiency in neuronal ceroid lipofuscinosis. A novel mutation."Vopr. Med. Khim. 48:594-598(2002) [PubMed] [Europe PMC] [Abstract]
  24. "Mutation of the glycosylated asparagine residue 286 in human CLN2 protein results in loss of enzymatic activity."Glycobiology 14:1C-5C(2004) [PubMed] [Europe PMC] [Abstract]
  25. "Mutations in CLN7/MFSD8 are a common cause of variant late-infantile neuronal ceroid lipofuscinosis."Brain 132:810-819(2009) [PubMed] [Europe PMC] [Abstract]
  26. "Functional consequences and rescue potential of pathogenic missense mutations in tripeptidyl peptidase I."Hum. Mutat. 31:710-721(2010) [PubMed] [Europe PMC] [Abstract]
  27. "Targeted next generation sequencing as a diagnostic tool in epileptic disorders." Epilepsia 53:1387-1398(2012) [PubMed] [Europe PMC] [Abstract]
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  29. "Autosomal recessive spinocerebellar ataxia 7 (SCAR7) is caused by variants in TPP1, the gene involved in classic late-infantile neuronal ceroid lipofuscinosis 2 disease (CLN2 disease)."Hum. Mutat. 34:706-713(2013) [PubMed] [Europe PMC] [Abstract]