PANCREATIC ELASTASE a Highly Specific and Convenient Assay for the Quantitative Monoclonal ELISA Determination of Pancreatic Elastase

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PANCREATIC ELASTASE A highly specific and convenient assay for the quantitative Monoclonal ELISA determination of Pancreatic Elastase. PANCREATIC Pancreatic Elastase by two ELASTASE monoclonal Ab ELISA methods [μg/ml] 800 Monoclonal elisa 700 R² = 0.9426 600 500 400 300 Cat. No. Description IDK ELISA 200 K6915 IDK® Pancreatic Elastase ELISA kit. 96 100 wells. 0 0 200 400 600 800 Comparison ELISA • Sample: Faeces Biohit Healthcare Ltd • Highly specific Monoclonal Ab Pioneer House | Pioneer Business Park North Road | Ellesmere Port ELISA system Cheshire CH65 1AD | UK • Range 40 - 720 µg/mL Tel. +44 (0)151 550 4 550 Fax. +44 (0)151 550 4 551 • 5 x standards, 2 x controls [email protected] • Automatable www.biohithealthcare.co.uk 7 EN2017/0 K6915 PANCREATIC ELASTASE Monoclonal ELISA IDK® Pancreatic Elastase ELISA Background Indications: Highly specific monoclonal Ab based Pancreatic elastase is an anionic endoprotease • Diagnosis/exclusion of exocrine ELISA for the determination of of the serine protease family with a molecular pancreas insufficiency in cases of pancreatic elastase in stool: weight of 26kDa. Together with other digestive o unexplained diarrhea enzymes it is synthesized as an inactive pro- o gut microbiota dysbiosis • Monoclonal test system enzyme in the acinar cells of the pancreas and is o IBS/IBD secreted into the duodenum. o steatorrhea • Short incubation: 2 x 30 min • Small sample volume: 15mg After activation, pancreatic elastase cleaves o flatulence peptides after neutral amino acids. Pancreatic o weight loss • Automatable elastase is mainly bound to bile salts during o upper abdominal pain intestinal passage and is not degraded. In o diet intolerances Includes universal extraction buffer human faeces it is 5–6 fold more concentrated than in pancreatic juice. • Monitoring of exocrine pancreas IDK Extract® enabling complete stool function in analytics from one single extract: o cystic fibrosis o diabetes mellitus o chronic pancreatitis Faecal Calprotectin Haemoglobin (FIT) alpha-1-antitrypsin Faecal Bile Acids The concentration of pancreatic elastase in faecal samples reflects the Lactoferrin secretory capacity of the pancreas. …and more. .

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Purification and Identification of a Binding Protein for Pancreatic
Biochem. J. (2003) 372, 227–233 (Printed in Great Britain) 227 Purification and identification of a binding protein for pancreatic secretory trypsin inhibitor: a novel role of the inhibitor as an anti-granzyme A Satoshi TSUZUKI*1,2,Yoshimasa KOKADO*1, Shigeki SATOMI*, Yoshie YAMASAKI*, Hirofumi HIRAYASU*, Toshihiko IWANAGA† and Tohru FUSHIKI* *Laboratory of Nutrition Chemistry, Division of Food Science and Biotechnology, Graduate School of Agriculture, Kyoto University, Kitashirakawa Oiwake-cho, Sakyo-ku, Kyoto 606-8502, Japan, and †Laboratory of Anatomy, Graduate School of Veterinary Medicine, Hokkaido University, Kita 18-Nishi 9, Kita-ku, Sapporo 060-0818, Japan Pancreatic secretory trypsin inhibitor (PSTI) is a potent trypsin of GzmA-expressing intraepithelial lymphocytes in the rat small inhibitor that is mainly found in pancreatic juice. PSTI has been intestine. We concluded that the PSTI-binding protein isolated shown to bind specifically to a protein, distinct from trypsin, on from the dispersed cells is GzmA that is produced in the the surface of dispersed cells obtained from tissues such as small lymphocytes of the tissue. The rGzmA hydrolysed the N-α- intestine. In the present study, we affinity-purified the binding benzyloxycarbonyl-L-lysine thiobenzyl ester (BLT), and the BLT protein from the 2 % (w/v) Triton X-100-soluble fraction of hydrolysis was inhibited by PSTI. Sulphated glycosaminoglycans, dispersed rat small-intestinal cells using recombinant rat PSTI. such as fucoidan or heparin, showed almost no effect on the Partial N-terminal sequencing of the purified protein gave a inhibition of rGzmA by PSTI, whereas they decreased the inhi- sequence that was identical with the sequence of mouse granzyme bition by antithrombin III.
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Chymotrypsin: a Serine Protease Reaction Mechanism Step
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Serine Proteases with Altered Sensitivity to Activity-Modulating
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Human Elastase 1: Evidence for Expression in the Skin and the Identi®Cation of a Frequent Frameshift Polymorphism
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