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— Global Procalcitonin Antibody Market report covers product scope, market overview, opportunities, risk, and driving force. It analyzes the top manufacturers of Procalcitonin Antibody, with sales, revenue, and price in 2016 and 2017. It also display the competitive situation among the top manufacturers, with sales, revenue and market share in 2016 and 2017. Companies profiled in this research report are Thermo Fisher, Roche Diagnostics, bioMerieux, HyTest, Wondfo, Ningbo Medicalsystem Biotechnology, Snibe, Vazyme Biotech, Getein Biotech, Hotgen Biotech, Lumigenex, Shanghai Medicine'nest Pharmaceutical, Kitgen, Beijing KeyGen and Fantibody. Access this report at https://www.themarketreports.com/report/global-procalcitonin-antibody-market-by-manufacturers-countries-type-and-application-forecast-to-2022 To provide the historical development this report includes global market by regions, with sales, revenue and market share of Procalcitonin Antibody, for each region, from 2012 to 2017 and market analysis by type and application, with sales market share and growth rate by type, application, from 2012 to 2017. This report also analyze the key regions, with sales, revenue and market share by key countries in North America, Europe, Asia-Pacific, South America, and Middle East and Africa. Later, this report provides Procalcitonin Antibody Market forecast, by regions, type and application, with sales and revenue, from 2017 to 2022. In addition to above this report includes Procalcitonin Antibody sales channel, distributors, traders, dealers, and sum up with research findings and conclusion. Purchase this premium report at: https://www.themarketreports.com/report/buy-now/521002 Market Analysis by Regions • North America (USA, Canada and Mexico) • Europe (Germany, France, UK, Russia and Italy) • Asia-Pacific (China, Japan, Korea, India and Southeast Asia) • South America (Brazil, Argentina, Columbia etc.) • Middle East and Africa (Saudi Arabia, UAE, Egypt, Nigeria and South Africa) Inquire about this report at: https://www.themarketreports.com/report/ask-your-query/521002 For more information, please visit https://www.themarketreports.com/report/global-procalcitonin-antibody-market-by-manufacturers-countries-type-and-application-forecast-to-2022


Semenov A.G.,HyTest Ltd. | Katrukha A.G.,HyTest Ltd. | Katrukha A.G.,Moscow State University
Clinical Chemistry | Year: 2016

BACKGROUND: Protease neprilysin is known to be responsible for the degradation of natriuretic peptides. A recent heart failure (HF) drug, LCZ696 (Entresto™), that combines a neprilysin inhibitor and an angiotensin II receptor inhibitor was suggested to augment circulating B-type natriuretic peptide (BNP) concentrations, making the results of BNP measurements diagnostically ambiguous. Because the main form of measured BNP in HF patients is represented by its uncleaved precursor, proBNP, it is important to know the susceptibility of proBNP to cleavage by neprilysin. METHODS: BNP 1-32 and nonglycosylated and glycosylated forms of proBNP 1-108 were incubated with neprilysin for different time periods. BNP immunoreactivity was analyzed using 2 sandwich immunoassays: one utilizing monoclonal antibody (mAb) KY-BNP-II (epitope 14-21) as capture with mAb 50E1 (epitope 26-32) for detection and a single-epitope sandwich BNP (SES-BNP) immunoassay specific to the epitope 11-17. Mass-spectrometry was applied to determine the sites of BNP cleavage. RESULTS: In contrast to BNP, both forms of proBNP were resistant to degradation by neprilysin. The SES-BNP assay was much less susceptible to the BNP cleavage by neprilysin compared with the immunoassay utilizing antibodies specific to the region 14-21, comprising the site Arg17-Ile18, known as the site of BNP cleavage by neprilysin. CONCLUSIONS: These findings suggest that modulation of neprilysin activity by specific inhibitors may not greatly influence the circulating concentrations of immunoreactive BNP, mostly represented in HF by proBNP, which is not susceptible to neprilysin. The different susceptibility of the BNP regions to neprilysin-dependent degradation highlights the importance of the choice of epitopes for reliable BNP immunodetection. © 2016 American Association for Clinical Chemistry.


Semenov A.G.,HyTest Ltd. | Seferian K.R.,HyTest Ltd.
Clinica Chimica Acta | Year: 2011

B-type Natriuretic Peptide (BNP) is a circulating hormone primarily produced by the myocardium in response to volume overload and increased filling pressure. BNP acts to increase natriuresis and to decrease cardiac load and blood pressure. The appearance of active BNP hormone in the bloodstream is preceded by the proteolytic cleavage of its precursor, proBNP. The products of proBNP processing, BNP and the N-terminal fragment of proBNP (NT-proBNP), have been extensively shown to be powerful biomarkers of heart failure (HF) and risk assessments for cardiovascular complications. In contrast to the clinical utility of proBNP-derived peptides, knowledge of posttranslational proBNP maturation and molecular aspects of its processing are far from being completely comprehended. A clear understanding of proBNP processing mechanisms in normal and diseased states appears to be required to improve our understanding of HF development and the clinical significance of both proBNP and proBNP-derived peptides. The aim of the present review is to summarize the available data in the field of human proBNP maturation and processing and to discuss potential clinical implications. © 2011 Elsevier B.V.


Semenov A.G.,HyTest Ltd. | Tamm N.N.,HyTest Ltd. | Seferian K.R.,HyTest Ltd. | Postnikov A.B.,HyTest Ltd. | And 5 more authors.
Clinical Chemistry | Year: 2010

BACKGROUND: B-type natriuretic peptide (BNP) and its N-terminal fragment (NT-proBNP) are the products of the enzyme-mediated cleavage of their precursor molecule, proBNP. The clinical significance of proBNP-derived peptides as biomarkers of heart failure has been explored thoroughly, whereas little is known about the mechanisms of proBNP processing. We investigated the role of 2 candidate convertases, furin and corin, in human proBNP processing. METHODS: We measured proBNP expression in HEK 293 and furin-deficient LoVo cells. We used a furin inhibitor and a furin-specific small interfering RNA (siRNA) to explore the implication of furin in proBNP processing. Recombinant proBNPs were incubated with HEK 293 cells transfected with the corin-expressing plasmid. We applied mass spectrometry to analyze the products of furin- and corin-mediated cleavage. RESULTS: Reduction of furin activity significantly impaired proBNP processing in HEK 293 cells. Furin-deficient LoVo cells were unable to process proBNP, whereas coexpression with furin resulted in effective proBNP processing. Mass spectrometric analysis revealed that the furin-mediated cleavage of proBNP resulted in BNP 1-32, whereas corin-mediated cleavage led to the production of BNP 4-32. Some portion of proBNP in the plasma of heart failure patients was not glycosylated in the cleavage site region and was susceptible to furin-mediated cleavage. CONCLUSIONS: Both furin and corin are involved in the proBNP processing pathway, giving rise to distinct BNPforms. The significance of the presence of unprocessed proBNP in circulation that could be cleaved by the endogenous convertases should be further investigated for better understanding BNP physiology. © 2010 American Association for Clinical Chemistry.


The present invention relates to an immunoassay for detection of BNP, proBNP and fragments thereof. Essentially the assay comprises: a) contacting the antigen with a first antibody specific to a fragment corresponding to amino acids 11-22 of BNP, or to a part of this peptide comprising at least three amino acids of said sequence, to obtain a first order immune complex. b) contacting the first order immune complex obtained at step (a) with a second antibody recognizing said first order immune complex, to obtain a second order immune complex, wherein said antibody is unable to recognize free BNP, proBNP or free first antibody; c) Detecting the second order immune complex.


Trademark
Hytest Ltd | Date: 2013-04-26

Monoclonal antibody reagents for diagnostic use (other than medical).


Patent
Hytest Ltd. | Date: 2010-06-29

The present invention relates to a method for diagnosing a cardiovascular or cancer disease by detecting IGFBP-4 (Insulin-like Growth Factor Binding Protein-4) fragments in a patient sample. Antibodies specifically recognizing novel epitopes originated by enzyme-dependent cleavage of IGFBP-4 are also disclosed.


The present invention describes the method for determining the risk of future major adverse cardiovascular events, which comprises detection proteolytic fragments of IGFBP-4 or IGFBP-5 (insulin-like growth factor binding protein 4 or insulin-like growth factor binding protein 5) in patients blood. The present invention provides antibodies and immunoas-says, suitable for specific measurement of proteolytic fragments of IGFBPs. In current invention the IGFBP fragments are suggested to be utilized as blood biomarkers for the risk prediction of major adverse cardiovascular events (MACE).


The present invention relates to a method for diagnosing a cardiovascular or cancer disease by detecting IGFBP-4 (Insulin-like Growth Factor Binding Protein-4) fragments in a patient sample. Antibodies specifically recognizing novel epitopes originated by enzyme-dependent cleavage of IGFBP-4 are also disclosed.


Patent
Hytest Ltd. | Date: 2015-04-17

The present invention relates to an immunoassay for detection of BNP, proBNP and fragments thereof. Essentially the assay comprises: a) contacting the antigen with a first antibody specific to a fragment corresponding to amino acids 11-22 of BNP, or to a part of this peptide comprising at least three amino acids of said sequence, to obtain a first order immune complex. b) contacting the first order immune complex obtained at step (a) with a second antibody recognizing said first order immune complex, to obtain a second order immune complex, wherein said antibody is unable to recognize free BNP, proBNP or free first antibody; c) Detecting the second order immune complex.

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