84-2147-63　［取扱停止］Trypsin 1ml　171794

特徴

• Trypsinogen (EC 3.4.23.18/20/21/23/24/26) is the precursor form or zymogen of the pancreatic enzyme trypsin.
• It is found in pancreatic juice, along with amylase, lipase, and chymotrypsinogen.
• It is activated by enteropeptidase, which is found in the intestinal mucosa, to form trypsin.
• Once activated, the trypsin can activate more trypsinogen into trypsin.
• Trypsin cleaves the peptide bond on the carboxyl side of basic amino acids such as arginine and lysine.
• Trypsinogen, as a precursor of trypsin, functions as storage of an inactive form of trypsin so that it may be kept in pancreas and released in significant amount when required for protein digestion.
• Trypsinogen is activated by enterokinase.
• Enterokinase is produced by the mucosa of duodenum and it cleaves the peptide bond of trypsinogen after residue 15 which is a lysine.
• The N-terminal peptide is discarded, and a slight rearrangement of the folded protein occurs.
• The newly-formed N-terminal residue (residue 16) insert into a cleft where its α-amino group forms an ion pair with the aspartate near the active site serine, and results in the conformational rearrangement of other residues.
• The amino group of Gly 193 orientates itself into the correct position which completes the oxyanion hole in active site, thereby activating the protein.[1] Since trypsin also cleaves the peptide bond after an arginine or a lysine, it can cleave other trypsinogen, and the activation process therefore becomes autocatalytic.
• Applications:Suitable for use in ELISA.
• Other applications not tested.
• Recommended Dilution:Optimal dilutions to be determined by the researcher.
• Storage and Stability:May be stored at 4°C for short-term only.
• Aliquot to avoid repeated freezing and thawing.
• Store at -20°C.
• Aliquots are stable for 12 months.
• For maximum recovery of product, centrifuge the original vial after thawing and prior to removing the cap.