Human Kallikrein 8 / KLK-8 Protein (Human Kallikrein 8, His Tag) Gln 29 - Gly 260 (Accession # AAH40887) was produced in human 293 cells (HEK293) at ACROBiosystems.
Human Kallikrein 8, His Tag is fused with a polyhistidine tag at the C-terminus, and has a calculated MW of 25.8 kDa. The predicted N-terminus is Gln 29. The reducing (R) protein migrates as 38 kDa in SDS-PAGE due to glycosylation.
Pre-activation is required for enzymatic assays. Please dilute Human Kallikrein 8 to 200 µg/mL in activation buffer (50 mM Tris, pH 8.0), and then dilute Lysyl-Endopeptidase to a final concentration of 0.4 mU/mL in activation buffer. Combine equal volume of diluted KLK8 and Lysyl-Endopeptidase together and incubate at 37 ℃ for 30 minutes. Please note that the optimal treatment time may need to be determined empirically.
Less than 1.0 EU per μg by the LAL method.
>95% as determined by SDS-PAGE.
Lyophilized from 0.22 μm filtered solution in 50 mM Tris, 150 mM NaCl, pH 8.0. Normally Mannitol or Trehalose are added as protectants before lyophilization.
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See Certificate of Analysis for reconstitution instructions and specific concentrations.
Avoid repeated freeze-thaw cycles.
No activity loss was observed after storage at:
In lyophilized state for 1 year (4°C); After reconstitution under sterile conditions for 3 months (-70°C).
Human Kallikrein 8, His Tag on SDS-PAGE under reducing (R) condition. The gel was stained overnight with Coomassie Blue. The purity of the protein is greater than 95%.
Kallikrein-8 (KLK8) is also known as Neuropsin (NP or NRPN), Ovasin, Serine protease 19 (PRSS19), Tumor-associated differentially expressed gene 14 protein (TADG-14), which belongs to the peptidase S1 family and Kallikrein subfamily. KLK8 contains 1 peptidase S1 domain. KLK8 is pH dependence protein and the optimum pH is 8.5, and the protein is active from pH 7-10. KLK8 is expressed at high levels in serum, ascites fluid and tumor cytosol of advanced stage ovarian cancer patients and may serve as a marker of ovarian cancer. KLK8 cleavage of amide substrates following the basic amino acids Arg or Lys at the P1 position, with a preference for Arg over Lys, and the catalytic activity of KLK8 is inhibited by a range of serine protease inhibitors including antipain, aprotinin, leupeptin, benzamidine and soybean trypsin inhibitor.
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