protein

Kallikrein-14 Protein, Mouse (His)

HY-P71590

5 μg;10 μg;50 μg

100;170;480 USD

Kallikrein-14 Protein, Mouse (His)

proteins

E. coli

5 μg;10 μg;50 μg

100;170;480 USD

Kallikrein-14 protein is a serine-type endopeptidase with multiple substrate specificities and has trypsin-like and chymotrypsin-like activities. It activates/inactivates protease-activated receptors (F2R, F2RL1, F2RL3) and other kallikreins (KLK1, KLK3, KLK5, KLK11). Kallikrein-14 Protein, Mouse (His) is the recombinant mouse-derived Kallikrein-14 protein, expressed by E. coli , with N-His labeled tag.

Mouse

Kallikrein-14, a serine-type endopeptidase, exhibits a versatile substrate specificity with both trypsin-like and chymotrypsin-like activities. This protease is implicated in the activation or inactivation of various proteinase-activated receptors, including F2R, F2RL1, and F2RL3, as well as other kallikreins such as KLK1, KLK3, KLK5, and KLK11. It plays a crucial role in seminal clot liquefaction through the direct cleavage of semenogelins SEMG1 and SEMG2, leading to the activation of KLK3. Additionally, Kallikrein-14 is involved in epidermal desquamation by cleaving desmoglein DSG1, contributing to the shedding of superficial corneocytes from the skin surface. Its engagement in tumor progression encompasses roles in growth, invasion, and angiogenesis. Notably, Kallikrein-14 is subject to inhibition by various serine protease inhibitors, including SERPINA1, SERPINC1, SERPINE1, and SERPINF2, as well as aprotinin, soybean trypsin inhibitor, and leupeptin. Its autoproteolytic activity may have regulatory implications, and the enzyme's activation is facilitated by citrate while being inhibited by zinc and, to a lesser extent, manganese.

Klk14; Gk14Kallikrein-14; EC 3.4.21.-; Glandular kallikrein KLK14; mGK14; Kallikrein related-peptidase 14

Greater than 90% 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.