KLK-4 / Kallikrein-4 Protein (His tag) (recombinant human)

Activity: Measured by its ability to cleave the fluorogenic peptide substrate Boc-VPR-AMC. (R&D Systems, Catalog # ES011). The specific activity is >250 pmoles/min/µg.(Activation description: The proenzyme needs to be activated by Thermolysin for an activated form) Protein Construction: A DNA sequence encoding the human KLK4 (NP_004908.3) (Met 1-Ser 254) was expressed, with a polyhistidine tag at the C-terminus. Sequence: Met 1-Ser 254. Fusion tag: C-His Endotoxin: < 1.0 EU per µg as determined by the LAL method. Apparent Molecular Mass: 30-35 kDa. Protein function: Kallikrein-4, also known as Enamel matrix serine proteinase 1, Kallikrein-like protein 1, KLK-L1, Serine protease 17, KLK4, PRSS17 and EMSP1, is a secreted protein which belongs to the peptidase S1 family and Kallikrein subfamily. Kallikrein-4 / KLK4 is a serine protease expressed during enamel maturation, and proteolytic processing of the enamel matrix by KLK4 is critical for proper enamel formation. Kallikrein-4 / KLK4 contains one peptidase S1 domain. Kallikrein-4 / KLK4 is secreted by transition- and maturation-stage ameloblasts. KLK4 aggressively degrades the retained organic matrix following the termination of enamel protein secretion. Two proteases are secreted into the enamel matrix of developing teeth. The early protease is enamelysin (MMP-20). The late protease is kallikrein 4 (KLK4). The principle functions of MMP-20 and KLK4 in dental enamel formation are to facilitate the orderly replacement of organic matrix with mineral, generating an enamel layer that is harder, less po Protein function: Has a major role in enamel formation (PubMed:15235027). Required during the maturation stage of tooth development for clearance of enamel proteins and normal structural patterning of the crystalline matrix. [The UniProt Consortium]