Recombinant Human Kallikrein 4/KLK4 Protein (His Tag)(Active) | PKSH030981

Recombinant Human Kallikrein 4/KLK4 Protein (His Tag)(Active) | PKSH030981 | Gentaur US, UK & Europe Disrtribition

Synonyms: Kallikrein-4; Enamel Matrix Serine Proteinase 1; Kallikrein-Like Protein 1; KLK-L1; Prostase; Serine Protease 17; KLK4; EMSP1; PRSS17; PSTS;AI2A1;ARM1;EMSP;kallikrein;KLK-L1

Active Protein: Active protein

Activity: A DNA sequence encoding the human KLK4 (NP_004908.3) (Met 1-Ser 254) was expressed, with a polyhistidine tag at the C-terminus.

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.

Fusion Tag: C-His

Species: Human

Expressed Host: HEK293 Cells

Shipping: This product is provided as lyophilized powder which is shipped with ice packs.

Purity: > 94 % as determined by reducing SDS-PAGE.

Endotoxin: < 1.0 EU per µg as determined by the LAL method.

Stability and Storage: Generally, lyophilized proteins are stable for up to 12 months when stored at -20 to -80℃. Reconstituted protein solution can be stored at 4-8℃ for 2-7 days. Aliquots of reconstituted samples are stable at < -20℃ for 3 months.

Molecular Mass: 25.8 kDa

Formulation: Lyophilized from sterile PBS, pH 7.4

Reconstitution: Please refer to the printed manual for detailed information.

Background: 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 porous, and unstained by retained enamel proteins. Defects in Kallikrein-4 / KLK4 are the cause of amelogenesis imperfecta hypomaturation type 2A1 (AI2A1) which is an autosomal recessive defect of enamel formation. The disorder involves both primary and secondary dentitions.

Research Area: N/A