TPP1 / CLN2 Protein (His Tag)

Tripeptidyl peptidase I Protein Datasheet

TPP1 / CLN2 Protein Product Information

• Synonym: GIG1, CLN2, LPIC, TPP-1
• Protein Construction: A DNA sequence encoding the pro form of human TPP1 (AAH14863.1) (Met 1- Pro 563) was fused with a polyhistidine tag at the C-terminus.
• Source: Human
• Expression Host: Baculovirus-Insect cells

TPP1 / CLN2 Protein QC Testing

• Purity: > 95 % as determined by SDS-PAGE
• Endotoxin: < 1.0 EU per μg of the protein as determined by the LAL method
• Stability: Samples are stable for up to twelve months from date of receipt at -70℃
• Predicted N terminal: Ser 20
• Molecular Mass: The secreted recombinant human TPP1 (pro form) comprises 554 amino acids and has a predicted molecular mass of 60.7 kDa. The apparent molecular mass of rhTPP1 is approximately 60 kDa in SDS-PAGE under reducing conditions.
• Formulation: Lyophilized from sterile 20mM, Tris 500mM NaCl ,PH7.4,10%gly.
  1. Normally 5 % - 8 % trehalose and mannitol are added as protectants before lyophilization. Specific concentrations are included in the hardcopy of COA.
  2. Please contact us for any concerns or special requirements.
• SDS-PAGE: TPP1 / CLN2 protein

TPP1 / CLN2 Protein Usage Guide

• Storage: Store it under sterile conditions at -70℃. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.
• Reconstitution: A hardcopy of COA with reconstitution instruction is sent along with the products. Please refer to it for detailed information.

TPP1 / CLN2 Protein Description

Tripeptidyl-peptidase 1 (TPP1 / CLN2) 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. TPP1 / CLN2 May act as a non-specific lysosomal peptidase which generates tripeptides from the breakdown products produced by lysosomal proteinases. Defects in TPP1 / CLN2 are the cause of neuronal ceroid lipofuscinosis type 2 (CLN2), a form of neuronal ceroid lipofuscinosis. Neuronal ceroid lipofuscinoses are progressive neurodegenerative, lysosomal storage diseases characterized by intracellular accumulation of autofluorescent liposomal material, and clinically by seizures, dementia, visual loss, and/or cerebral atrophy. Experiments have found that TIN2-anchored TPP1 plays a major role in the recruitment of telomerase to telomeres in human cells and that recruitment does not depend on POT1 or interaction of the shelterin complex with the single-stranded region of the telomere.

References

1. Xin H. et al., 2007, Nature. 445 (7127): 559-62.
2. O'Connor MS. et al., 2006, Proc Natl Acad Sci. 103 (32): 11874-9.
3. Abreu E. et al., 2010, Mol Cell Biol. 30 (12): 2971-82.