protein

Cathepsin C/DPPI Protein, Mouse (Inactive, His-Myc)

HY-P701247

20 μg;50 μg

200;440 USD

Cathepsin C/DPPI Protein, Mouse (Inactive, His-Myc)

proteins

E. coli

20 μg;50 μg

200;440 USD

The cathepsin C/DPPI protein is a thiol protease that acts as a dipeptidyl peptidase with multiple substrate specificities, excluding proline at the P1 position and arginine at the P2 position. It has both exopeptidase and endopeptidase functions and can activate serine proteases such as elastase, cathepsin G, and granzymes A and B. Cathepsin C/DPPI Protein, Mouse (Inactive, His-Myc) is the recombinant mouse-derived Cathepsin C/DPPI protein, expressed by E. coli , with N-10*His, C-Myc labeled tag. The accession of Cathepsin C/DPPI Protein, Mouse (Inactive, His-Myc) is P97821 (D25-W134).

Mouse

Cathepsin C/DPPI Protein, functioning as a thiol protease, exhibits dipeptidylpeptidase activity with efficacy against a diverse spectrum of dipeptide substrates comprising polar and hydrophobic amino acids. Notably, the P1 position cannot accommodate proline, and the P2 position cannot accommodate arginine in the substrate. This thiol protease displays versatility as both an exopeptidase and an endopeptidase. Its functional repertoire extends to the activation of serine proteases, including elastase, cathepsin G, and granzymes A and B. The broad substrate specificity and multifunctional roles of Cathepsin C/DPPI highlight its significance in the intricate network of proteolytic processes, implicating its involvement in diverse cellular functions and regulatory pathways.

Cathepsin C; cathepsin CEC 3.4.14.1; Cathepsin J; CPPIHMS; CTSC; dipeptidyl peptidase 1; Dipeptidyl peptidase I; Dipeptidyl transferase; dipeptidyl-peptidase I; DPP1; DPPI; DPP-I; JP; JPD; PALS; PLS

Greater than 95% as determined by reducing SDS-PAGE.

Lyophilized from a 0.22 μm filtered solution of 10 mM Tris-HCl, 1 mM EDTA, 6% Trehalose, pH 8.0.

Room temperature in continental US; may vary elsewhere.