|Datasheet||Specific References||Reviews||Related Products||Protocols|
|Vector Type||Mammalian Expression Vector|
|Expression Method||Constiutive, Stable / Transient|
|Selection In Mammalian Cells||Hygromycin|
A myc tag can be used in many different assays that require recognition by an antibody. If there is no antibody against the studied protein, adding a myc-tag allows one to follow the protein with an antibody against the Myc epitope. Examples are cellular localization studies by immunofluorescence or detection by Western blotting.
The peptide sequence of the myc-tag is: N-EQKLISEEDL-C (1202 Da). It can be fused to the C-terminus and the N-terminus of a protein. It is advisable not to fuse the tag directly behind the signal peptide of a secretory protein, since it can interfere with translocation into the secretory pathway.
|Mouse KLK-4 ORF mammalian expression plasmid, C-GFPSpark tag||MG50993-ACG|
|Mouse KLK-4 ORF mammalian expression plasmid, C-OFPSpark / RFP tag||MG50993-ACR|
|Mouse KLK-4 ORF mammalian expression plasmid, C-Flag tag||MG50993-CF|
|Mouse KLK-4 ORF mammalian expression plasmid, C-His tag||MG50993-CH|
|Mouse KLK-4 ORF mammalian expression plasmid, C-Myc tag||MG50993-CM|
|Mouse KLK-4 ORF mammalian expression plasmid, C-HA tag||MG50993-CY|
|Mouse KLK-4 Gene cDNA clone plasmid||MG50993-G|
|Mouse KLK-4 ORF mammalian expression plasmid, N-Flag tag||MG50993-NF|
|Mouse KLK-4 ORF mammalian expression plasmid, N-His tag||MG50993-NH|
|Mouse KLK-4 ORF mammalian expression plasmid, N-Myc tag||MG50993-NM|
|Mouse KLK-4 ORF mammalian expression plasmid, N-HA tag||MG50993-NY|
|Mouse KLK-4 natural ORF mammalian expression plasmid||MG50993-UT|
|Learn more about expression Vectors|
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.