Kallikreins are a subgroup of serine proteases having diverse physiological functions. Growing evidence suggests that many Kallikreins are implicated in carcinogenesis and some have potential as novel cancer and other disease biomarkers. This gene is one of the fifteen members of the Kallikrein subfamily located in a cluster on chromosome 19. Its encoded protein is secreted and may play a role in suppression of tumorigenesis in breast and prostate cancers. Alternate splicing of this gene results in multiple transcript variants encoding the same protein.
Product Name:
Human Kallikrein 4/KLK4 Recombinant Protein (RPES2848)
Recombinant Human Kallikrein 4 is produced by our Mammalian expression system and the target gene encoding Ser27-Ser254 is expressed with a 6His tag at the C-terminus.
Purity:
> 95 % as determined by reducing SDS-PAGE.
Mol Mass:
25.4 kDa
AP Mol Mass:
30 kDa
Formulation:
Lyophilized from a 0.2 µm filtered solution of 20mM TrisHCl, 150mM NaCl, pH 8.0.
Shipping:
This product is provided as lyophilized powder which is shipped with ice packs.
Stability and Storage:
Lyophilized proteins are stable for up to 12 months when stored at -20 to -80°C. Reconstituted protein solution can be stored at 4-8°C for 2-7 days. Aliquots of reconstituted samples are stable at < -20°C for 3 months.
system_update_altDatasheetHuman Kallikrein 4/KLK4 Recombinant Protein Kallikrein-4, also known as Enamel matrix serine proteinase 1, Kallikrein-like protein 1, KLK-L1, Serine protease 17, KLK4,
system_update_altDatasheetHuman Kallikrein 1/KLK1 Recombinant Protein Kallikrein-1 (KLK1) is a member of human tissue Kallikrein family. Human KLK1 precursor contains a singal peptide (residues 1
system_update_altDatasheetHuman Kallikrein 7/KLK7 Recombinant Protein Human Kallikrein 7 is a member of the tissue kallikrein family of extracellular serine proteases that is made up of 15 member
system_update_altDatasheetHuman Kallikrein 1/KLK1 Recombinant Protein Human tissue kallikrein (KLK1) is a serine protease, component of the KKS that has been demonstrated to exert pleiotropic ben