DPP8 Protein, Human (Sf9)

The DPP8 protein cleaves N-terminal dipeptides from proteins with Pro or Ala at position 2. DPP8 Protein, Human (Sf9) is the recombinant human-derived DPP8 protein, expressed by Sf9 insect cells , with tag free. The total length of DPP8 Protein, Human (Sf9) is 898 a.a., .

DPP8 protein functions as a dipeptidyl peptidase, cleaving N-terminal dipeptides from proteins containing a Pro or Ala residue at position 2. It plays a crucial role as a key inhibitor of caspase-1-dependent monocyte and macrophage pyroptosis in resting cells by preventing the activation of NLRP1 and CARD8. DPP8 achieves this by sequestering the cleaved C-terminal portions of NLRP1 and CARD8, the active components of their respective inflammasomes, in a ternary complex, thereby impeding their oligomerization and subsequent activation. The dipeptidyl peptidase activity of DPP8 is essential for the suppression of NLRP1 and CARD8, although neither of these proteins appears to be a direct substrate of DPP8. This suggests the existence of unidentified substrate(s) required for the inhibition of NLRP1 and CARD8, highlighting the intricate regulatory mechanisms orchestrated by DPP8 in the context of cellular pyroptosis and inflammasome activation.

Human

Sf9 insect cells

Tag Free

Q6V1X1 (M1-I898)

54878

Greater than 90% as determined by reducing SDS-PAGE.

<1 EU/μg, determined by LAL method.