Human Kallikrein 7, His Tag (KL7-H5228) is expressed from human 293 cells (HEK293). It contains AA Glu 23 - Arg 253 (Accession # P49862-1).
Predicted N-terminus: Glu 23
This protein carries a polyhistidine tag at the C-terminus.
The protein has a calculated MW of 26.2 kDa. The protein migrates as 29-33 kDa under reducing (R) condition (SDS-PAGE) due to glycosylation.
Pre-activation is required for enzymatic assays. Please dilute Human Kallikrein 7 to 200 µg/mL in TCNB buffer (50 mM Tris, 10 mM CaCl2, 150 mM NaCl, 0.05% Brij-35 (w/v), pH 7.5), and then dilute Thermolysin to a final concentration of 20 μg/mL in TCNB buffer. Combine equal volume of diluted KLK7 and Thermolysin together and incubate at 37 ℃ for 2 hours. Then stop reaction with equal volume of 100 mM EDTA diluted in 50 mM Tris, 150 mM NaCl, pH 8.5. 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 7.5. Normally trehalose is added as protectant before lyophilization.
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Please see Certificate of Analysis for specific instructions.
For best performance, we strongly recommend you to follow the reconstitution protocol provided in the CoA.
For long term storage, the product should be stored at lyophilized state at -20°C or lower.
Please avoid repeated freeze-thaw cycles.
No activity loss is observed after storage at:
- 4-8°C for 12 months in lyophilized state;
- -70°C for 3 months under sterile conditions after reconstitution.
Human Kallikrein 7, 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-7 (KLK7) is also known as kallikrein-related peptidase 7, Stratum corneum chymotryptic enzyme, Serine protease 6, KLK7, and PRSS6, is a secreted protein which belongs to the peptidase S1 family and Kallikrein subfamily. KLK7 is secreted as an inactive zymogen in the stratum granulosum layer of the epidermis, requiring proteolytic cleavage of the short N-terminal pro-region to liberate activated enzyme. This may be performed by KLK5 or matriptase, which are in vitro activators of KLK7. Once active, KLK7 is able to cleave desmocollin and corneodesmosin. KLK7 activity is regulated by a number of endogenous protein inhibitors including LEKTI, SPINK6, elafin and alpha-2-Macroglobulin-like 1. Both Zn2+ and Cu2+ ions are also able to inhibit KLK7. Dysregulation of KLK7 has been linked to several skin disorders, and overexpression of KLK7 may provide a route for metastasis in several cancers.
- (1) Katiuchia Uzzun Sales, et al., 2010, Nat. Genet. 42 (8): 676–683.
- (2) Brattsand, M., et al., 2005, J Invest Dermatol, 124(1):198-203.
- (3) Caubet C, et al., 2004, J. Invest. Dermatol. 122 (5): 1235–44.
- (4) Deraison, C., et al., 2007, Mol Biol Cell, 18(9):3607-3619.
- (5) Franzke CW, et al., 2003, J Biol Chem. 271 (36): 21886–90.
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