All TPP1 reagents are produced in house and quality controlled, including 1 TPP1 Antibody, 28 TPP1 Gene, 1 TPP1 Lysate, 2 TPP1 Protein, 2 TPP1 qPCR. All TPP1 reagents are ready to use.
Recombinant TPP1 proteins are expressed by Baculovirus-Insect Cells with fusion tags as C-His.
TPP1antibodies are validated with different applications, which are ELISA, IHC-P, ICC/IF, IF.
TPP1cDNA clones are full length sequence confirmed and expression validated. There are 13 kinds of tags for each TPP1 of different species, especially GFP tag, OFP tag, FLAG tag and so on. There are three kinds of vectors for choice, cloning vector, expression vector and lentivrial expression vector.
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 which is associated with the failure to degrade specific neuropeptides and a subunit of ATP synthase in the lysosome. 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.