To avoid genomic DNA amplification, at least one primer is designed crosses the junction of exons according to the conserved region of a specific gene with all variants.

Confirmed in positive organizations; screened the primer with high specificity and high sensitivity.

AI2A1 qPCR Primer Pairs, Human;ARM1 qPCR Primer Pairs, Human;EMSP qPCR Primer Pairs, Human;EMSP1 qPCR Primer Pairs, Human;kallikrein qPCR Primer Pairs, Human;KLK-L1 qPCR Primer Pairs, Human;PRSS17 qPCR Primer Pairs, Human;PSTS qPCR Primer Pairs, Human

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-2). The late protease is kallikrein 4 (KLK4). The principle functions of MMP-2 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.