Product Overview
Blocking/Immunizing peptide for anti-CLN2/TPP1 antibody
Tag/Conjugate
Unconjugated
Application Notes
For in vitro research use only. Not intended for any diagnostic or therapeutic purpose. Not for human or animal consumption.
Format
Lyophilized powder
Storage
Shipped at ambient temperature, store at -20°C.
Antigen Description
This gene encodes 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. [provided by RefSeq, Jul 2008]
Function
endopeptidase activity; endopeptidase activity; metal ion binding; peptidase activity; peptide binding; protein binding; serine-type endopeptidase activity; serine-type peptidase activity; tripeptidyl-peptidase activity; tripeptidyl-peptidase activity;
Synonyms
TPP1; tripeptidyl peptidase I; ceroid lipofuscinosis, neuronal 2, late infantile (Jansky Bielschowsky disease) , CLN2; tripeptidyl-peptidase 1; TPP I; tripeptidyl aminopeptidase; growth-inhibiting protein 1; cell growth-inhibiting gene 1 protein; lysosomal pepstatin insensitive protease; CLN2; GIG1; LPIC; TPP-1; MGC21297;
Citations
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Elleder, M; Dvorakova, L; et al. Atypical CLN2 with later onset and prolonged course: a neuropathologic study showing different sensitivity of neuronal subpopulations to TPP1 deficiency. ACTA NEUROPATHOLOGICA 116:119-124(2008).
Qing, YF; Zhou, JG; et al. Altered expression of TPP1 in fibroblast-like synovial cells might be involved in the pathogenesis of rheumatoid arthritis. RHEUMATOLOGY INTERNATIONAL 32:2503-2510(2012).