Trypsinogen

Trypsin is produced, stored and released as the inactive trypsiongen to ensure that the protein is only activated in the appropriate location. Premature trypsin activation can be destructive and may trigger a series of events that lead to pancreatic self-digestion. In normal pancreas, around 5% of trypsinogens are thought to get activated, therefore there are a number of defenses against such inappropriate activation. Trypsinogen is stored in intracellular vesicles in the pancreas called zymogen granules whose membranous walls are thought to be resistant to enzymatic degradation. A further safeguard against inappropriate trypsin activation is the presence of inhibitors such as bovine pancreatic trypsin inhibitor (BPTI) and serine protease inhibitor Kazal-type 1 (SPINK1) which binds to any trypsin formed. Trypsin autocatalytic activation of trypsinogen is also a slow process due to the presence of a large negative charge on the conserved N-terminal hexapeptide of trypsinogen which repels the aspartate on the back of trypsin's specificity pocket. Trypsin may also inactivate other trypsin by cleavage.\n\nApplications:\nSuitable for use in ELISA, Immunoprecipitation and Western Blot. Other applications not tested.\n\nRecommended Dilutions:\nELISA: 1:2000-1:10,000\nOptimal dilutions to be determined by the researcher. \n\nStorage and Stability:\nMay be stored at 4 degrees C for short-term only. Aliquot to avoid repeated freezing and thawing. Store at -20 degrees C. Aliquots are stable for 12 months. For maximum recovery of product, centrifuge the original vial after thawing and prior to removing the cap.

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SPECIFICATIONS

Catalog Number

T8690-05A

Size

1ml

Applications

ELISA, IP, WB

Hosts

Rabbit

Reactivities

Bov

Form

Supplied as a liquid in PBS, 0.01% sodium azide.

P Type

Pab

Purity

Purified by ammonium sulfate precipitation.

Isotype

IgG

References

1. Thomas E Creighton (1993). Proteins: Structures and Molecular Properties (2nd ed.). W H Freeman and Company. pp. 434. ISBN 0-7167-2317-4. 2. Voet & Voet (1995). Biochemisty (2nd ed.). John Wiley & Sons. pp. 399-400. ISBN 0-471-58651-X. 3. Scheele G, Bartelt D, Bieger W (March 1981). \"Characterization of human exocrine pancreatic proteins by two-dimensional isoelectric focusing/sodium dodecyl sulfate gel electrophoresis\". Gastroenterology 80 (3): 461-73. PMID 6969677.\n4. Whitcomb DC, Gorry MC, Preston RA, Furey W, Sossenheimer MJ, Ulrich CD, Martin SP, Gates LK Jr, Amann ST, Toskes PP, Liddle R, McGrath K, Uomo G, Post JC, Ehrlich GD (1996). \"Hereditary pancreatitis is caused by a mutation in the cationic trypsinogen gene\". Nature Genetics14 (2): 141-5. doi:10.1038/ng1096-141. PMID 8841182. 5. Rebours V, L

Additional Info

Recognizes bovine TRYPSINOGEN. Reactive with single band in immunoelectrophoresis.