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Trypsinogen, PMSF treated from Bovine Pancreas Proteins Molecular Depot
Trypsinogen, PMSF treated from Bovine Pancreas Proteins Molecular Depot

Trypsinogen, PMSF treated from Bovine Pancreas

$995.00

    Catalog Number: B2021178 (1 vial)

    Trypsinogen is an inactive precursor of the enzyme trypsin, a serine protease essential for protein digestion. It is produced in the pancreas and activated in the small intestine. This product has been used as a molecular tool for various biochemical applications. It has also been used in a wide array of other chemical and immunological applications. Custom bulk amounts of this product are available upon request.

    Products are for in vitro research use only (RUO).

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VR Headset

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2 Touch Controllers

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Trypsinogen, PMSF Treated from Bovine Pancreas – Catalog Number: B2021178 (1 vial)

Catalog number: B2021178
Lot number: Batch Dependent
Expiration Date: Batch dependent
Amount: 1 vial
Molecular Weight or Concentration: ~24 kDa
Supplied as: Lyophilized Powder
Applications: a molecular tool for various biochemical applications
Storage: 2-8°C
Keywords:
Grade: Biotechnology grade. All products are highly pure. All solutions are made with Type I ultrapure water (resistivity >18 MΩ-cm) and are filtered through 0.22 um.

 

Trypsinogen, PMSF Treated from Bovine Pancreas (Catalog B2021178, 1 vial) is the chemically stabilized precursor of trypsin, rendered inactive through treatment with phenylmethylsulfonyl fluoride (PMSF). This inactivation prevents unwanted proteolytic activity during storage and initial handling—preserving the integrity of the zymogen for research applications involving controlled activation. Trypsinogen is essential in studies of enzyme activation, protease inhibition, and pancreatic enzyme cascades, and its preservation via PMSF ensures enhanced stability without compromising eventual activation functionality.

In functional studies, PMSF-treated trypsinogen is particularly valuable in workflows that examine the dynamics of zymogen conversion to active protease under tightly regulated conditions. Researchers commonly employ it when constructing enzyme cascade models, evaluating protease inhibitor effects, or developing instructional modules on digestive enzyme biochemistry. Given its lyophilized powder format and implicit stability at cool temperatures, it offers flexibility in storage and reconstitution across various experimental setups.

For best results, labs typically aliquot the preparation under cold conditions and store at low temperatures to preserve activity potential. Pilot activation protocols—such as those leveraging enteropeptidase—help determine optimal concentrations and time points for downstream readouts. The comprehensive documentation fields, including catalog number, zymogen state, and grade annotations, facilitate seamless integration into LIMS and SOP-driven environments, enhancing reproducibility across multi-user facilities.

Why researchers choose this product:

  • PMSF inactivation ensures minimized basal activity and enhanced zymogen stability
  • Lyophilized format enables reliable aliquoting and reconstitution
  • Supports controlled activation studies and enzyme cascade modeling
  • Documentation-ready, biotechnology-grade purity supports quality systems

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.

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    Products are for in vitro research use only (RUO). They are not intended for human or animal use, diagnosis, therapy, resale to consumers, or residential delivery. Sales are limited to verified business addresses.

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Product Resources:

Copy of Technical Specifications

FeatureDetails
Viewing Head Siedentopf type trinocular head, inclined at 30°, Interpupillary adjustment 53mm to 75mm, graduated diopter on left eyetube (30mm I.D. eyetubes)
Eyepieces SWH10X Widefield high eyepoint eyepiece, Field No. 22, tube O.D. 30.0 mm
Nosepiece Quintuple
Quintuple LWD Planachromat Phase 10x, 20x
Condenser TC Condenser N.A. 0.30, W.D. 73.0mm
Stage180mm(X) x 245mm(Y) plain stage with replaceable glass insert with 45mm opening, Glass Stage plate insert
IlluminationKoehler without iris, with phase slider, 3W LED
WarrantyLIMITED LIFETIME WARRANTY

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