Recombinant Mouse Tripeptidyl-peptidase 1 (Tpp1)

Product Details

Purity
>85% (SDS-PAGE)
Target Names
Tpp1
Uniprot NO.
Alternative Names
Tpp1; Cln2; Tripeptidyl-peptidase 1; TPP-1; EC 3.4.14.9; Lysosomal pepstatin-insensitive protease; LPIC; Tripeptidyl aminopeptidase; Tripeptidyl-peptidase I; TPP-I
Species
Mus musculus (Mouse)
Source
Yeast
Expression Region
195-562
Target Protein Sequence
LHLGVT PSVLRQRYNL TAKDVGSGTT NNSQACAQFL EQYFHNSDLT EFMRLFGGSF THQASVAKVV GKQGRGRAGI EASLDVEYLM SAGANISTWV YSSPGRHEAQ EPFLQWLLLL SNESSLPHVH TVSYGDDEDS LSSIYIQRVN TEFMKAAARG LTLLFASGDT GAGCWSVSGR HKFRPSFPAS SPYVTTVGGT SFKNPFLITD EVVDYISGGG FSNVFPRPPY QEEAVAQFLK SSSHLPPSSY FNASGRAYPD VAALSDGYWV VSNMVPIPWV SGTSASTPVF GGILSLINEH RILNGRPPLG FLNPRLYQQH GTGLFDVTHG CHESCLNEEV EGQGFCSGPG WDPVTGWGTP NFPALLKTLL NP
Note: The complete sequence may include tag sequence, target protein sequence, linker sequence and extra sequence that is translated with the protein sequence for the purpose(s) of secretion, stability, solubility, etc.
If the exact amino acid sequence of this recombinant protein is critical to your application, please explicitly request the full and complete sequence of this protein before ordering.
Protein Length
Full Length of Mature Protein
Tag Info
N-terminal His-tagged/Tag-Free
The tag type will be determined during production process. If you have specified tag type, please tell us and we will develop the specified tag preferentially.
Storage Condition
Store at -20°C, for extended storage, conserve at -20°C or -80°C.
Shelf Life
The shelf life is related to many factors, storage state, buffer ingredients, storage temperature and the stability of the protein itself.
Generally, the shelf life of liquid form is 6 months at -20°C/-80°C. The shelf life of lyophilized form is 12 months at -20°C/-80°C.
Notes
Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.

Customer Reviews and Q&A

 Customer Reviews

Target Background

Function(From Uniprot)
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.
Gene References into Functions
  1. telomeres are protected from hyper-resection through the repression of the ATM and ATR kinases by TRF2 and TPP1-bound POT1a/b, respectively. PMID:26778124
  2. Rssults suggested that CLN2, CLN3 and CLN5 genes may play an important role in early embryonal neurogenesis. PMID:25303899
  3. demonstrated that cells expressing TIN2DeltaTPP1 instead of wild-type TIN2 phenocopy the POT1a,b knockout setting without showing additional phenotypes PMID:25056954
  4. Gemfibrozil and fenofibrate, Food and Drug Administration-approved lipid-lowering drugs, up-regulate tripeptidyl-peptidase 1 in brain cells via peroxisome proliferator-activated receptor alpha and may have implications in late infantile Batten disease therapy PMID:22989886
  5. TPPI activity becomes crucial for the neuronal functions later in development. PMID:21996941
  6. Telomere protection by TPP1/POT1 requires tethering to TIN2. PMID:22099311
  7. TPP1 protects telomere integrity and regulates telomerase recruitment to telomeres, thereby preventing early occurrence of degenerative skin pathologies. PMID:20493811
  8. TPP1 deletion resulted in the release of POT1a and POT1b from chromatin and loss of these proteins from telomeres, indicating that TPP1 is required for the telomere association of POT1a and POT1b but not for their stability. PMID:19995905
  9. Lysosomal degradation of cholecystokinin-(29-33)-amide in mouse brain is dependent on this enzyme: implications for the degradation and storage of peptides in classical late-infantile neuronal ceroid lipofuscinosis (tripeptidyl peptidase-I) PMID:12038963
  10. TPP-I is the predominant proteolytic enzyme responsible for the intracellular degradation of neuromedin B PMID:15158442
  11. The CLN2-targeted mouse recapitulates much of the pathology and clinical features of classical late-infantile neuronal ceroid lipofuscinosis PMID:15483130
  12. Tpp1 confers telomere end protection by recruiting Pot1a and Pot1b to telomeres. Knockdown of Tpp1 elicits an ataxia telangiectasia mutated protein (ATR)-dependent DNA damage response at telomeres. PMID:17948054
  13. Expression of 6% of normal TPPI activity increased lifespan to that of unaffected mice. PMID:18343701
  14. Results indicate that the loss of TPPI cannot be functionally compensated for by DPPI. PMID:18570628
  15. While all treatment groups show a marked increase in total TPP-I activity over wild-type mice, neonatally treated mice displayed high levels of TPP-I activity in the CNS 1 yr after administration which was spread throughout the brain. PMID:18639872

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Subcellular Location
Lysosome. Melanosome.
Database Links
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