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AB239722

Pepsin/Pepsinogen Assay Kit (Fluorometric)

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(1 Publication)

Pepsin/Pepsinogen Assay Kit (Fluorometric) (ab238722) is a homogenous assay that allows for quantification of pepsin activity in gastric tissues (stomach, duodenum etc.

View Alternative Names

Pepsin A-4, Pepsinogen-4, PGA4, Pepsin A-5, Pepsinogen-5, PGA5, Pepsin A-3, Pepsinogen-3, PGA3

3 Images
Biochemical assay - Pepsin/Pepsinogen Assay Kit (Fluorometric) (AB239722)
  • Biochemical assay

Supplier Data

Biochemical assay - Pepsin/Pepsinogen Assay Kit (Fluorometric) (AB239722)

Estimation of pepsinogen activity in pooled normal human serum and single-donor serum from a gastric ulcer patient with confirmed H. Pylori infection (each 10 μl of undiluted serum).

Data are mean ± SEM of 3 replicates, assayed according to the kit protocol.

Biochemical assay - Pepsin/Pepsinogen Assay Kit (Fluorometric) (AB239722)
  • Biochemical assay

Supplier Data

Biochemical assay - Pepsin/Pepsinogen Assay Kit (Fluorometric) (AB239722)

Kinetics of Pepsin Substrate metabolism by porcine gastric mucosal pepsin (3.33 ng purified enzyme) and specificity of substrate metabolism by pepsin versus other aspartic proteases.

The acid-activated proteases Cathepsin D and E exhibit minimal assay interference, even when present at ≥300-fold excess by mass.

Biochemical assay - Pepsin/Pepsinogen Assay Kit (Fluorometric) (AB239722)
  • Biochemical assay

Supplier Data

Biochemical assay - Pepsin/Pepsinogen Assay Kit (Fluorometric) (AB239722)

MCA standard curve.

One mole of MCA corresponds to the cleavage of one mole of fluorogenic Pepsin Substrate

Key facts

Detection method

Fluorescent

Sample types

Plasma, Serum, Other biological fluids

Assay Platform

Microplate reader

Reactivity data

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Product details

Pepsin/Pepsinogen Assay Kit (Fluorometric) (ab238722) is a homogenous assay that allows for quantification of pepsin activity in gastric tissues (stomach, duodenum etc.) and various biological fluids (serum/plasma, gastric juice, vomit). The assay utilizes a synthetic peptide substrate bearing both a fluorophore and a fluorescence quencher. Upon cleavage by pepsin, the fluorophore-bearing peptide fragment is unquenched to produce a bright fluorescent signal (Ex/Em = 328/418 nm). Lysosomal aspartic proteases in the peptidase A1 family (Cathepsin D and E) do not interfere with the assay. The assay is rapid, simple to perform and is vastly more sensitive than the classical hemoglobin degradation assay, with a detection limit of 500 μU pepsin activity per well.

This product is manufactured by BioVision, an Abcam company and was previously called K446 Pepsin/Pepsinogen Activity Assay Kit (Fluorometric). K446-100 is the same size as the 100 test size of ab239722.

The Safety Datasheet for this product has been updated for certain countries. Please check the current version in the Support and downloads section.

What's included?

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Properties and storage information

Shipped at conditions
Blue Ice
Appropriate short-term storage conditions
-20°C
Appropriate long-term storage conditions
-20°C
Storage information
-20°C

Supplementary information

This supplementary information is collated from multiple sources and compiled automatically.

Pepsin is an enzyme with the main function of breaking down proteins into peptides in the stomach. Commonly known as a protease its molecular mass is approximately 35 kDa. This enzyme arises from its inactive precursor pepsinogen which activates in the acidic environment of the stomach. Expression predominantly occurs in the gastric chief cells. Pepsin remains a critical player in protein digestion with pepsin solutions often utilized for in vitro digestion studies.
Biological function summary

Pepsin fulfills an important role in the digestive process by breaking down larger protein molecules into smaller peptides facilitating nutrient absorption. It does not form part of a larger protein complex but operates independently within the gastric environment. Pepsin's enzymatic action targets specific peptide bonds ensuring efficient degradation of dietary proteins into absorbable forms. The specificity of its substrate binding ensures effective digestion and subsequent utilization of amino acids.

Pathways

Pepsin's activity integrates into proteolytic pathways particularly the catabolic processes in the gastrointestinal tract. It interacts with other digestive enzymes including trypsin and chymotrypsin which further hydrolyze peptides originated by pepsin. These interactions highlight its seamless fit in the digestive enzyme cascade optimized for effective protein turnover and nutrient release into the body. The pepsin pathway coordinates closely with the gastric and duodenal enzymatic processes.

Conditions such as peptic ulcers and Zollinger-Ellison syndrome link closely with excessive or dysregulated pepsin activity. Increased pepsin secretion in response to elevated gastric acid levels contributes to the degradation of the stomach lining aggravating ulcer formation. Alcohol-induced gastric mucosal damage also associates with heightened pepsin activity. Dysfunctional interactions involving pepsin and other gastric enzymes such as pepsinogen underline the pathological implications within these disorders.

Product protocols

Target data

Shows particularly broad specificity; although bonds involving phenylalanine and leucine are preferred, many others are also cleaved to some extent.
See full target information PGA4

Additional targets

PGA5,PGA3

Publications (1)

Recent publications for all applications. Explore the full list and refine your search

Scientific reports 11:17071 PubMed34426628

2021

Usefulness of matrix metalloproteinase-7 in saliva as a diagnostic biomarker for laryngopharyngeal reflux disease.

Applications

Unspecified application

Species

Unspecified reactive species

Nu-Ri Im,Byoungjae Kim,Kwang-Yoon Jung,Seung-Kuk Baek
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