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40 kDa(Reducing)
40 kDa(Reducing)
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Uniprot E6Y432, with C-His Tag
MIVGGSDSREGAWPWVVALYFDDQQVCGASLVSRDWLVSAAHCVYGRNMEPSKWKAVLGLHMASNLTSPQIETRLIDQIVINPHYNKRRKDNDIAMMHLEMKVNYTDYIQPICLPEENQVFSPGRICSIAGWGTLIYQGSTADVLQEADVPLLSNEKCQQQMPEYNITENMVCAGYEAGGVDSCQGDSGGPLMCQENNRWLLAGVTSFGYQCALPNRPGVYARVPRFTEWIQSFLHHHHHHH
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40 kDa(Reducing)
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Enterokinase (enteropeptidase, EC 3.4.4.8) occupies a key position in the utilization of dietary proteins. The enzyme initiates intraluminar digestion of proteins by the proteolytic conversion of trypsinogen to trypsin, which in turn activates the other pancreatic zymogens (Kunitz, 1939a,b; Hadorn et al., 1969). The proteolytic attack of enterokinase is directed exclusively toward the Lys6-Ile7 peptide bond of trypsinogen leaving all other lysine and arginine bonds in the molecule unaffected (Maroux et al., 1971). The resultant cleavage produces the simultaneous release of active trypsin and of the
amino-terminal hexapeptide Val-(Asp)d-Lys (Rovery et al., 1953; Davie and Neurath, 1955). This unique specificity exhibited by enterokinase is of interest as it relates to both the molecular basis of substrate recognition and the control of the digestive process.
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· 12 months from date of receipt, -20 to -70 °C as supplied.
· 6 months, -20 to -70 °C under sterile conditions after reconstitution.
· 1 week, 2 to 8 °C under sterile conditions after reconstitution.
· Please avoid repeated freeze-thaw cycles.
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参考图片
The substrate of 50 μ g fusion protein was digested by enzyme, and the addition amount of enterokinase in the sample was 0.5IU, 1IU, 1.5IU and 2IU, respectively. The substrate is a fusion protein with a molecular weight of 10 KD and reacted at 25 ℃ for 16 hours, and the target band of 8.4kD is produced after restriction enzyme digestion.