Human CellExp Kallikrein-1, human recombinant protein
KLK1, Kallikrein-1, KLKR, Klk6, hK1
- SPECIFICATION
- CITATIONS
- PROTOCOLS
- BACKGROUND
Primary Accession | P06870 |
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Calculated MW | This protein is fused with polyhistidine tag at the C-terminus, has a calculated MW of 27.9 kDa. The predicted N-terminus is Pro 19. DTT-reduced Protein migrates as 40-45 kDa due to glycosylation. |
Gene ID | 3816 |
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Gene Symbol | KLK1 |
Other Names | KLK1, Kallikrein-1, KLKR, Klk6, hK1 |
Gene Source | Human |
Source | HEK293 cells |
Assay&Purity | SDS-PAGE; ≥95% |
Assay2&Purity2 | N/A; |
Recombinant | Yes |
Results | Measured by its ability to cleave a fluorogenic peptide substrate Pro – Phe – Arg – 7 – amido – 4 - methylcoumarin (PFR-AMC). The specific activity is >1200 pmol/min/ µg. |
Target/Specificity | Kallikrein-1 |
Application Notes | Centrifuge the vial prior to opening. Reconstitute in sterile PBS, pH 7.4 to a concentration of 50 µg/ml. Do not vortex. This solution can be stored at 2-8°C for up to 1 month. For extended storage, it is recommended to store at -20°C. |
Format | Lyophilized |
Storage | -20°C; Lyophilized from 0.22 µm filtered solution in 50 mM Tris, 2 mM CaCl2, 150 mM NaCl, pH 7.5. Normally Mannitol or Trehalose is added as protectants before lyophilization. |
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Provided below are standard protocols that you may find useful for product applications.
Background
Kallikrein-1 (KLK1) belongs to the peptidase S1 family and Kallikrein subfamily. KLK1 contains one peptidase S1 domain. KLK-1 preferential cleavage of Arg-|-Xaa bonds in small molecule substrates and also has highly selective action to release kallidin (lysyl-bradykinin) from kininogen involves hydrolysis of Met-|-Xaa or Leu-|-Xaa. Glandular Kallikreins cleave Met-Lys and Arg-Ser bonds in kininogen to release Lys-bradykinin.
References
Fukushima D.,et al.Biochemistry 24:8037-8043(1985).
Evans B.A.,et al.Biochemistry 27:3124-3129(1988).
Angermann A.,et al.Biochem. J. 262:787-793(1989).
Chen L.-M.,et al.Braz. J. Med. Biol. Res. 27:1829-1838(1994).
Yousef G.M.,et al.Biochem. Biophys. Res. Commun. 276:125-133(2000).
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