Product Pathways - Protein Stability
TPP2 Antibody #14981
|14981S||100 µl ( 10 western blots )||￥3,250.00||现货查询 购买询价 防伪查询|
|14981||carrier free & custom formulation / quantity||email request|
Species cross-reactivity is determined by western blot.
Applications Key: W=Western Blotting, IP=Immunoprecipitation,
Specificity / Sensitivity
TPP2 Antibody recognizes endogenous levels of total TPP2 protein. This antibody cross-reacts with a 35 kDa protein of unknown identity in some lysates.
Source / Purification
Polyclonal antibodies are produced by immunizing animals with a synthetic peptide corresponding to residues near the carboxy terminus of human TPP2 protein. Antibodies are purified by protein A and peptide affinity chromatography.
Western blot analysis of extracts from 293T cells, mock transfected (-) or transfected with a construct expressing Myc/DDK-tagged full-length human TPP2 protein (hTPP2-Myc/DDK; +), using TPP2 Antibody.
Tripeptidyl-peptidase 2 (TPP2) is a well-conserved subtilisin-like amino peptidase that is expressed predominantly in the cytoplasmic compartment (1,2). The amino-terminal region of TPP2 harbors a catalytic triad that is characteristic of serine proteases and allows for TPP2 cleavage of tripeptides from the free amino terminus of oligopeptide substrates (3). TPP2 is a large (>5MDa) homooligomeric protease in which proteolytic activity is regulated by subunit oligomerization (4,5). While TPP2 plays a general role in amino acid homeostasis, research studies demonstrate that TPP2 is involved in MHC class I antigen presentation (6,7) and DNA-damage repair (8). TPP2 activity is required for the survival of Burkitt's lymphoma cells, suggesting a possible role for TPP2 in oncogenesis (9). Additional research studies show that TPP2 proteolytic activity is important for regulating lysosome abundance and glycolytic metabolism and that TPP2 deficiency leads to defects in adaptive immunity, innate immunity, and nervous system development (10).
- Tomkinson, B. (1999) Trends Biochem Sci 24, 355-9.
- Tomkinson, B. and Lindås, A.C. (2005) Int J Biochem Cell Biol 37, 1933-7.
- Hilbi, H. et al. (2002) Biochim Biophys Acta 1601, 149-54.
- Seyit, G. et al. (2006) J Biol Chem 281, 25723-33.
- Tomkinson, B. (2000) Arch Biochem Biophys 376, 275-80.
- Seifert, U. et al. (2003) Nat Immunol 4, 375-9.
- York, I.A. et al. (2006) J Immunol 177, 1434-43.
- Preta, G. et al. (2009) Biochem Biophys Res Commun 389, 575-9.
- Gavioli, R. et al. (2001) Nat Cell Biol 3, 283-8.
- Lu, W. et al. (2014) Cell 159, 1578-90.
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