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Cat. No.: HY-E71364

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Pepsin (USP)

Pepsin (USP) is a proteolytic enzyme. Pepsin (USP) catalyzes cleavage of peptide bonds in proteins and synthetic peptides. Pepsin (USP) dissolves protein nutrients, cleaves proteins into peptones, produces large polypeptides, smaller peptides, and free amino acids, affects amino acid release rates and protein allergenicity. Pepsin (USP) can be used for biochemical research.

For research use only. We do not sell to patients.

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Please store the product under the recommended conditions in the Certificate of Analysis.

Pepsin (USP) Chemical Structure

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Fluorescent Dye

Strong Fluorescence Signal / Multi-Disciplinary Applications / High Fluorescence Specificity

Biological Activity
- Description
- In Vitro
Chemical Information
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Biological Activity

Description

All Endogenous Metabolite Isoforms :

In Vitro

Pepsin (USP) has a bilobed three-dimensional structure with an extended active site cleft containing two catalytically essential aspartyl residues, and its flap region undergoes conformational changes upon inhibitor binding to enhance interaction^[1].
pepsin (USP) hydrolyzes native α-lactalbumin^[2].
Pepsin (USP) rapidly hydrolyzes α_s1-casein and α_s2-casein with limited resistant regions^[2].
pepsin (USP)-mediated κ-casein hydrolysis and casein micelle coagulation are modulated by temperature, pepsin concentration, pH, calcium concentration, whey protein concentration, ionic strength, and milk species^[2].
pepsin (USP) shows limited hydrolysis of native ovalbumin at pH 4 but extensive hydrolysis at pH 2^[2].
pepsin (USP) extensively hydrolyzes raw myofibrillar proteins except for tropomyosin^[2].

MedChemExpress (MCE) has not independently confirmed the accuracy of these methods. They are for reference only.

Chemical Information

SMILES

[Pepsin (USP)]
Shipping

Room temperature in continental US; may vary elsewhere.
Storage

Please store the product under the recommended conditions in the Certificate of Analysis.

Purity & Documentation

Handling Instructions (2659 KB)

References

[1]. Gould JL, et al. The quarterly review of biology. Q Rev Biol. 1976;51(2):211-244. [Content Brief]

[2]. Yang M, et al. Digestion of food proteins: the role of pepsin. Crit Rev Food Sci Nutr. 2025;65(30):6919-6940. [Content Brief]

Calculators

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Help & FAQs

How should lyophilized recombinant proteins be reconstituted and stored?

1. Before opening the cap, centrifuge the vial at 13000 rpm for 20-30 seconds. This step will ensure that any lyophilized powder that may have adhered to the cap or walls is collected at the bottom of the vial, minimizing the risk of product loss.

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Biological Activity
- Description
- In Vitro
Chemical Information
Purity & Documentation
References

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Pepsin (USP)

All Endogenous Metabolite Isoforms

Biological Activity

Chemical Information

Purity & Documentation

References

Calculators

Help & FAQs

Pepsin (USP) Related Classifications

HY-E71364 Related Classifications