Background

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.

Images

Western blotting analysis using anti-Tripeptidyl peptidase 2 antibody (Cat#62643). Total cell lysates (30 μg) from various cell lines were loaded and separated by SDS-PAGE. The blot was incubated with anti-Tripeptidyl peptidase 2 antibody (Cat#62643, 1:5,000) and HRP-conjugated goat anti-rabbit secondary antibody (Cat#201, 1:20,000) respectively. Image was developed using FeQ™ ECL Substrate Kit (Cat#226).

Western blotting analysis using anti-Tripeptidyl peptidase 2 antibody (Cat#62643). Tripeptidyl peptidase 2 expression in wild type (WT) and Tripeptidyl peptidase 2 shRNA knockdown (KD) HeLa cells with 20 μg of total cell lysates . β-Tubulin serves as a loading control. The blot was incubated with anti-Tripeptidyl peptidase 2 antibody (Cat#62643, 1:5,000) and HRP-conjugated goat anti-rabbit secondary antibody (Cat#201, 1:20,000) respectively. Image was developed using NaQ™ ECL Substrate Kit (Cat#716).

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