Kallikrein 4/KLK4 Protein, Human, Recombinant (His)

• Catalog Number: orb1957754
• Category: Proteins
• Description: 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 that 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 principal 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.
• Tag: C-His
• Purity: 98.00%
• MW: 25.8 kDa (predicted); 30-35 kDa (reducing condition, due to glycosylation)
• UniProt ID: Q9Y5K2
• Expression System: HEK293 Cells
• Biological Origin: Human
• Biological Activity: 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 that 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 principal 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.
• Expression Region: A DNA sequence encoding the human KLK4 (NP_004908.3) (Met 1-Ser 254) was expressed, with a polyhistidine tag at the C-terminus. Predicted N terminal: Ser 27
• Storage: -20°C
• Note: For research use only
• Application notes: A Certificate of Analysis (CoA) containing reconstitution instructions is included with the products. Please refer to the CoA for detailed information.
• Expiration Date: 6 months from date of receipt.