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Manufactured by BioVendor

Urinary Trypsin Inhibitor Human ELISA

  • Regulatory status:RUO
  • Type:Sandwich ELISA, HRP-labelled antibody
  • Other names:UTI, bikunin, ulinastatin
  • Species:Human
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Cat. No. Size Price


Availability on Request RD191343100R 96 wells (1 kit)
PubMed Product Details
Technical Data

Type

Sandwich ELISA, HRP-labelled antibody

Applications

Urine

Sample Requirements

5 µl/well

Shipping

At ambient temperature. Upon receipt, store the product at the temperature recommended below.

Storage/Expiration

Store the complete kit at 2–8°C. Under these conditions, the kit is stable until the expiration date (see label on the box).

Calibration Curve

Calibration Range

0.63–20 ng/ml

Limit of Detection

0.254 ng/ml

Intra-assay (Within-Run)

n = 8; CV = 4.3 %

Inter-assay (Run-to-Run)

n = 5; CV = 8.5 %

Spiking Recovery

97.6 %

Dilution Linearity

105.2 %

Summary

Features

  • It is intended for research use only
  • The total assay time is less than 3 hours
  • The kit measures urinary trypsin inhibitor in human urine
  • Assay format is 96 wells
  • Standard is purified human native protein
  • Components of the kit are provided ready to use, concentrated or lyophilized

Research topic

Immune Response, Infection and Inflammation, Oncology, Renal disease, Sepsis

Summary

Urinary trypsin inhibitor (UTI) (also called bikunin or ulinastatin) is a multivalent serine protease inhibitor synthesized and released in human urine and blood. UTI is an acidic glycoprotein, composed of 143-amino acid residues. Bikunin contains two proteinase inhibitor domains of the Kunitz type, a short connecting peptide as well as N- and C-terminal extensions 10 – 25 amino acids long. The N-terminal extension carries a chondroitin sulphate chain. Each of the Kunitz domains has a binding site for a proteinase and the amino acid residues essential for binding (Met 36 of the N-terminal domain and Arg 92 of the C-terminal domain). The total molecular weight of UTI is 25 – 26 kDa. UTI is produced by endoplasmic reticulum of hepatocytes as a precursor in which UTI is linked to α1-microglobulin. Most of the UTI in blood (90 – 98 %) occurs as a covalently linked subunit of the proteins pre-α-inhibitor and inter-α-inhibitor, respectively. In human plasma the major UTI-containing protein is inter-α-inhibitor. The total concentration of UTI in human plasma is 4 – 7 μM, of which 2 – 10 % is in free form. UTI is a positive acute phase protein. The concentration of free, uncomplexed UTI in plasma of patients with inflammatory conditions has been reported to be higher than normal. The plasma UTI level and its gene expression change under severe inflammatory conditions. In patients suffering from various nephropathies, a clear correlation between the UTI and creatinine concentrations in plasma was found, implying that the kidneys are a major site of uptake of the protein. UTI is rapidly released into urine when infection occurs and is an excellent inflammatory marker, constituting most of the urinary anti-trypsin activity. In urine, in which the level of complexed UTI is negligible, the average UTI concentration is 0.03 – 0.05 μM. The level of UTI in urine may be elevated under various pathological conditions, including pneumonia, lung emphysema, rheumatoid arthritis, cancer, and surgical trauma. It appears that UTI passes through the kidneys by glomerular filtration. Some tumour cells secrete UTI, which could contribute to the high urinary levels seen in some cancer patients. The function of UTI has been preserved during evolution. Trypsin and other serine proteases such as trombin, chymotrypsin, kallikrein, plasmin, neutrophil elastase, cathepsin and factors IXa, Xa, XIa and XlIa are inhibited by UTI, indicating that UTI is part of the inflammatory process. Furthermore, UTI can suppress urokinase-type plasminogen activator (uPA) expression through the inhibition of protein kinase C. UTI appears to prevent organ injury by inhibiting the activity of inflammatory serine proteases. In vitro studies have demonstrated that serine protease inhibitors may have anti-inflammatory properties. UTI suppresses the infiltration of neutrophils and the release of elastase and chemical mediators from them. Clinically, UTI is widely used as a drug for patients with acute inflammatory disorders such as pancreatitis, shock and disseminated intravascular coagulation.

Summary References (20)

References to Urinary Trypsin Inhibitor

  • Balduyck M, Albani D, Jourdain M, Mizon C, Tournoys A, Drobecq H, Fourrier F, Mizon J. Inflammation-induced systemic proteolysis of inter-alpha-inhibitor in plasma from patients with sepsis. J Lab Clin Med. 2000 Feb;135 (2):188-98
  • Balduyck M, Mizon J. [Inter-alpha-trypsin inhibitor and its plasma and urine derivatives]. Ann Biol Clin (Paris). 1991;49 (5):273-81
  • Chawla RK, Lawson DH, Ahmad M, Travis J. Cancer-related urinary proteinase inhibitor, EDC1: a new method for its isolation and evidence for multiple forms. J Cell Biochem. 1992 Nov;50 (3):227-36
  • Chawla RK, Miller FW, Lawson DH, Nixon DW. Urinary cancer-related protein EDC1 and serum inter-alpha trypsin inhibitor in breast cancer. Tumour Biol. 1984;5 (6):351-63
  • Chirat F, Balduyck M, Mizon C, Laroui S, Sautiere P, Mizon J. A chondroitin-sulfate chain is located on serine-10 of the urinary trypsin inhibitor. Int J Biochem. 1991;23 (11):1201-3
  • DILLARD GH. The trypsin inhibitor of the urine in health and disease. J Lab Clin Med. 1950 Aug;36 (2):266-71
  • Endo S, Inada K, Yamashita H, Takakuwa T, Nakae H, Yamada Y, Kasai T, Taki K, Yoshida M. The inhibitory actions of protease inhibitors on the production of polymorphonuclear leukocyte elastase and interleukin 8. Res Commun Chem Pathol Pharmac. 1993 Oct;82 (1):27-34
  • Franck C, Pedersen JZ. Trypsin-inhibitory activities of acid-stable fragments of the inter-alpha-trypsin inhibitor in inflammatory and uraemic conditions. Scand J Clin Lab Invest. 1983 Apr;43 (2):151-5
  • Fries E, Blom AM. Bikunin--not just a plasma proteinase inhibitor. Int J Biochem Cell Biol. 2000 Feb;32 (2):125-37
  • Gebhard W, Hochstrasser K, Fritz H, Enghild JJ, Pizzo SV, Salvesen G. Structure of inter-alpha-inhibitor (inter-alpha-trypsin inhibitor) and pre-alpha-inhibitor: current state and proposition of a new terminology. Biol Chem Hoppe Seyler. 1990 May;371 Suppl:13-22
  • Hirose J, Ozawa T, Miura T, Isaji M, Nagao Y, Yamashiro K, Nii A, Kato K, Uemura A. Human neutrophil elastase degrades inter-alpha-trypsin inhibitor to liberate urinary trypsin inhibitor related proteins. Biol Pharm Bull. 1998 Jul;21 (7):651-6
  • Hochstrasser K, Feuth H, Fall J, Kemkes B. [Acidstable proteinaseinhibitors in blood plasma in different nepropathies (author's transl)]. Klin Wochenschr. 1974 Nov 1;52 (21):UNKNOWN
  • Hochstrasser K, Niebel J, Feuth H, Lempart K. [About degradation products of the inter-alpha-trypsin inhibitor in serum. I. The inter-alpha-trypsin inhibitor as precursor of the acid stable trypsin-plasmin-inhibitor of the serum (author's transl)]. Klin Wochenschr. 1977 Apr 1;55 (7):337-42
  • Hochstrasser K, Reisinger PW, Albrecht GJ, Wustrow TP. [Protease inhibitors as tumor-associated growth factors]. Laryngorhinootologie. 1989 Jan;68 (1):51-6
  • Inoue K, Takano H. Urinary trypsin inhibitor as a therapeutic option for endotoxin-related inflammatory disorders. Expert Opin Investig Drugs. 2010 Apr;19 (4):513-20
  • Jonsson-Berling BM, Ohlsson K, Rosengren M. Radioimmunological quantitation of the urinary trypsin inhibitor in normal blood and urine. Biol Chem Hoppe Seyler. 1989 Nov;370 (11):1157-61
  • Kobayashi H, Gotoh J, Terao T. Urinary trypsin inhibitor efficiently inhibits urokinase production in tumor necrosis factor-stimulated cells. Eur J Cell Biol. 1996 Dec;71 (4):380-6
  • Kobayashi H, Shinohara H, Takeuchi K, Itoh M, Fujie M, Saitoh M, Terao T. Inhibition of the soluble and the tumor cell receptor-bound plasmin by urinary trypsin inhibitor and subsequent effects on tumor cell invasion and metastasis. Cancer Res. 1994 Feb 1;54 (3):844-9
  • Kobayashi H, Suzuki M, Tanaka Y, Hirashima Y, Terao T. Suppression of urokinase expression and invasiveness by urinary trypsin inhibitor is mediated through inhibition of protein kinase C- and MEK/ERK/c-Jun-dependent signaling pathways. J Biol Chem. 2001 Jan 19;276 (3):2015-22
  • Kuwajima S, Matsui T, Kitahashi S, Kishida T, Noda T, Izumi Y, Naka K, Okuda K. Automated measurement of trypsin inhibitor
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