Abcam, ab239722, Pepsin/Pepsinogen Assay Kit (Fluorometric)

Size: 100Test
Pepsin/Pepsinogen Assay Kit (Fluorometric) (ab238722) is a homogenous assay that allows for quantification of pepsin activity in gastric tissues (stomach, duodenum etc.
Key facts
Detection method:Fluorescent,
Sample types:Plasma, Serum, Other biological fluids,
Assay Platform:Microplate reader

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.

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.