Human PRSS1/2/3 ELISA Kit

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  • Alternative name

    Trypsin-1 ELISA KIT; Beta-trypsin ELISA KIT; Cationic trypsinogen ELISA KIT; Serine protease 1 ELISA KIT; Trypsin IPRSS1 ELISA KIT; TRP1 ELISA KIT; TRY1 ELISA KIT; TRYP1 ELISA KIT

  • Catalog
    E028153
  • species
    Human
  • GenePRSS1/2/3
  • Standard CurveHuman PRSS1/2/3 ELISA Kit
  • SpecificityNatural and recombinant Human Pan Trypsin
  • SamplesSerum, Plasma , tissue homogenates,Cell culture supernates,Other biological fluids.
  • Sensitivity Intra-assay Precision Intra-Assay Precision (Precision within an assay) Three samples of kn
  • Intended UseHuman PRSS1/2/3 ELISA Kit allows for the in vitro quantitative determination of PRSS1/2/3 , concentrations in serum, Plasma , tissue homogenates and Cell culture supernates and Other biological fluids.
  • StorageFor 5-7days:Store the whole kit at 4℃
    For a Long time :Store the Substrate at 4℃, other reagent should store at -20℃.
  • Product Description
    specifical
    Principle of the Assay: Human Pan Trypsin ELISA Kit was based on standard sandwich enzyme-linked immunesorbent assay technology. A monoclonal antibody from mouse specific for Pan Trypsin has been precoated onto 96-well plates. Standards(Expression system for standard: NSO; Immunogen sequence: A16-S247) and test samples are added to the wells, a biotinylated detection polyclonal antibody from goat specific for Pan Trypsin is added subsequently and then followed by washing with PBS or TBS buffer. Avidin-Biotin-Peroxidase Complex was added and unbound conjugates were washed away with PBS or TBS buffer. HRP substrate TMB was used to visualize HRP enzymatic reaction. TMB was catalyzed by HRP to produce a blue color product that changed into yellow after adding acidic stop solution. The density of yellow is proportional to the Human Pan Trypsin amount of sample captured in plate. Background/Introduction: Trypsin is a serine protease from the PA clan superfamily, found in the digestive system of many vertebrates, where it hydrolyses proteins. In the duodenum, trypsin catalyzes the hydrolysis of peptide bonds, breaking down proteins into smaller peptides. The peptide products are then further hydrolyzed into amino acids via other proteases, rendering them available for absorption into the blood stream. Tryptic digestion is a necessary step in protein absorption as proteins are generally too large to be absorbed through the lining of the small intestine. Additionally, Trypsin is produced as the inactive zymogen trypsinogen in the pancreas. When the pancreas is stimulated by cholecystokinin, it is then secreted into the first part of the small intestine (the duodenum) via the pancreatic duct. Once in the small intestine, the enzyme enteropeptidase activates trypsinogen into trypsin by proteolytic cleavage. Auto catalysis can happen with trypsin using trypsinogen as the substrate. This activation mechanism is common for most serine proteases, and serves to prevent autodegradation of the pancreas.



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