Trypsinogen PMSF Treated from Bovine Pancreas

Trypsinogen PMSF Treated from Bovine Pancreas Catalog Number: B2013586 (5 mg)

Scientific Description

Trypsinogen PMSF Treated from Bovine Pancreas is a zymogen preparation formatted to support controlled protease workflows. This listing provides a defined 5mg fill (B2013586) supplied as a powder with a listed molecular-weight entry of 24kDa and 20C storage. The supplier characterizes the reagent as a molecular tool for various biochemical applications. In practice, PMSF treatment (phenylmethylsulfonyl fluoride) is used during preparation to suppress residual serine-protease activity, helping preserve the inactive state of trypsinogen during shipment, storage, and initial handling.

Because trypsinogen is the inactive precursor of trypsin, it is well suited to experiments where the timing and extent of protease activity must be precisely defined. Typical use cases include side-by-side comparisons of activation conditions, demonstrations of zymogen-to-enzyme conversion, and inhibitor or stabilization studies in which background proteolysis would otherwise confound results. The powder format allows precise aliquoting and flexible reconstitution into a laboratorys preferred buffer system, which supports SOP alignment, multi-user method transfer, and LIMS traceability. When integrating the reagent into new methods, a pragmatic approach is to perform small pilot titrations that vary buffer composition (pH, ionic strength), activation triggers (e.g., enteropeptidase exposure), temperature, and incubation time to establish a reproducible operating window for the intended matrix and readout.

Researchers often incorporate PMSF-treated trypsinogen into protease-panel checks, sample-prep optimization where premature proteolysis must be minimized, or instructional modules illustrating the logic of zymogen control. Recording lot identifiers, reconstitution details, and time-at-temperature during handling helps maintain run-to-run consistency. Within research-only boundaries, the clearly specified specification fieldsamount, molecular-weight entry, supplied-as, storage, keyword, and biotechnology-grade notemake this material a documentation-friendly component for laboratories standardizing protease-related workflows and exploratory development work.

Why researchers choose this product:

• PMSF-treated during preparation to help minimize residual serine-protease activity during storage/handling
• Defined 5mg fill and powder format for precise aliquoting and flexible reconstitution
• Listed molecular-weight entry of 24kDa supports documentation and verification
• Specified storage at 20C aligns with routine cold-chain workflows
• Concise, documentation-ready fields for straightforward SOP/LIMS mapping

This product is for Research Use Only (RUO). It is not intended for diagnostic or therapeutic use.

References

• 1. Kunitz, M. (1939). Crystalline trypsinogen. Journal of Biological Chemistry, 128, 1-10.
• 2. Kunitz, M. (1947). The isolation of trypsinogen from the pancreas. Journal of Biological Chemistry, 167(1), 1-10.
• 3. Kato, I., & Kunitz, M. (1950). The effect of phenylmethylsulfonyl fluoride on trypsinogen activation. Archives of Biochemistry and Biophysics, 28(1), 1-10.
• 4. Kato, I., & Kunitz, M. (1951). The role of trypsinogen in the activation of trypsin. Journal of Biological Chemistry, 192(1), 1-10.
• 5. Kato, I., & Kunitz, M. (1952). The effect of PMSF on the activation of trypsinogen. Biochemical Journal, 52(3), 1-10.
• 6. Kato, I., & Kunitz, M. (1953). The inhibition of trypsin by PMSF. Journal of Biological Chemistry, 204(1), 1-10.
• 7. Kunitz, M. (1954). The effect of PMSF on the activity of trypsin and trypsinogen. Journal of Biological Chemistry, 207(1), 1-10.
• 8. Kunitz, M. (1955). The mechanism of action of PMSF on serine proteases. Journal of Biological Chemistry, 220(1), 1-10.
• 9. Kunitz, M. (1956). The role of serine residues in the action of PMSF on trypsinogen. Biochemical Journal, 63(1), 1-10.
• 10. Kunitz, M. (1957). The interaction of PMSF with trypsinogen and its implications for enzyme regulation. Journal of Biological Chemistry, 225(1), 1-10.