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Tpp2 encodes a mammalian peptidase that, at neutral pH, removes tripeptides from the N terminus of longer peptides. Additionally we are shipping Tpp2 Proteins (3) and many more products for this protein.
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Novel interactions of TPPII, p53 (show TP53 Antibodies), and SIRT7 (show SIRT7 Antibodies) presented in this study might contribute to the knowledge of the regulatory effects of these proteins on apoptotic pathways and to the understanding mechanisms of aging and lifespan regulation.
TPP2 mediates many important cellular functions by controlling ERK1 (show MAPK3 Antibodies) and ERK2 (show MAPK1 Antibodies) phosphorylation.
Early-onset Evans syndrome, immunodeficiency, and premature immunosenescence associated with TPP2 deficiency have been described in two consanguineous siblings.
Study found that autosomal recessive TPP2 mutations cause recurrent infections, autoimmunity, and neurodevelopmental delay in humans.
TPPII, MYBBP1A (show MYBBP1A Antibodies) and CDK2 (show CDK2 Antibodies) form a protein-protein interaction network.
Previously unknown differences between TPP II orthologues and subtilisin as well as features that might be conserved within the entire family of subtilisin-like serine peptidases.
Study showed that overexpression of Tripeptidyl peptidase II (TPP2) occurs frequently during oral carcinogenesis and might be associated with the progression of Oral Squamous Cell Carcinoma (OSCC) via Spindle Assembly Checkpoint(SAC (show ADCY10 Antibodies)) activation.
obtained a 3D structure of the human TPPII
Current knowledge about TPPII with a focus on structural aspects.
Results suggest an important function of TPPII in the maintenance of viral growth and may have implications for anti-viral therapy.
Data indicate that TPPII can regulate sperm maturation by modulating intracellular Ca(2 (show CA2 Antibodies)+) stores via the type 3 RyR (show RYR1 Antibodies).
Tripeptidyl peptidase II is crucial for nucleoprotein epitope generation during major histocompatibility complex class I complex viral antigen processing both in the presence and absence of lactacystin-sensitive proteasome action.
TPPII is not generally required for the production of major histocompatibility class I-restricted peptides, but presentation of some peptides can be negatively affected by TPPII.
Data show that mice that were homozygous for an insertion in the Tpp2 locus were embryonic lethal and Tpp2 heterozygous mutants were lean compared with wild-type littermates, although food intake was normal.
The data suggest a moderate, predominantly destructive role of TPPII in class I Ag processing.
TPPII is important for maintaining normal cellular and systemic physiology, which may be relevant for potential therapeutic applications of TPPII inhibitors
These results do not support a generally important role of TPPII for viability and proliferation of transformed cells or their p53 (show TP53 Antibodies)-mediated DNA damage response.
These data indicate that while TPPII contributes to the trimming of peptides with very long N-terminal extensions, TPPII is not essential for generating most MHC class I-presented peptides or for stimulating CTL responses to several Ags (show GLA Antibodies) in vivo.
a systematic kinetic analysis of wild type Drosophila melanogaster TPPII and five point mutants of the double-Glu (show SLC2A1 Antibodies)-motif (E312/E343) involving natural substrates were performed.
The structure suggests a model for activation of TPP II involving the relocation of a flexible loop and a repositioning of the active-site serine, coupling it to holocomplex assembly and active-site sequestration.
The 150 kDa subunits of TPPII form a superstructure composed of 2 segmented & twisted (show POMT2 Antibodies) strands. Each strand is 12.5 nm in width & composed of 11 segments that enclose a central channel.
the unique spindle form of the holo-complex of TPP II represents an assembly motif stabilizing a highly active state
The purification and characterization of tripeptidyl peptidase II from Arabidopsis thaliana is reported.
This gene encodes a mammalian peptidase that, at neutral pH, removes tripeptides from the N terminus of longer peptides. The protein has a specialized function that is essential for some MHC class I antigen presentation. The protein is a high molecular mass serine exopeptidase\; the amino acid sequence surrounding the serine residue at the active site is similar to the peptidases of the subtilisin class rather than the trypsin class.
, tripeptidyl aminopeptidase
, tripeptidyl-peptidase 2
, tripeptidyl-peptidase II
, Tripeptidyl-peptidase II
, tripeptidyl peptidase II
, tripeptidylpeptidase II
, tripeptidyl peptidase ii